https://microbewiki.kenyon.edu/index.php?title=Ebola&feed=atom&action=historyEbola - Revision history2024-03-29T04:56:38ZRevision history for this page on the wikiMediaWiki 1.39.6https://microbewiki.kenyon.edu/index.php?title=Ebola&diff=109289&oldid=prevCjackson9401: /* Ebola Evades the Immune System */2015-04-14T17:31:30Z<p><span dir="auto"><span class="autocomment">Ebola Evades the Immune System</span></span></p>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>[[File:TIM.png|500px|thumb|right|Original figure legend: (A) VP40-GFP VLPs lacking any viral entry protein are bound and internalized by hTIM1. 293T cells transduced with hACE2 (mock), hTIM1 or AA-hTIM1 were incubated for 6 h with VP40-GFP VLPs bearing EBOV GP or no GP. Being inherently fluorescent, these VLPs can be detected independently of whether they undergo fusion, in contrast to the pseudoviruses and VLPs used in previous figures. The supernatant of cells expressing only GFP (mock supernatant) served as negative control. Uninternalized VLPs were detached by acid-stripping and extensive trypsinization, after which internalized VLPs were detected by flow cytometry. Figure depicts results representative of three independent experiments performed in duplicates. (B) In parallel with the infection in A, expression levels of hTIM1 and AA-hTIM1 were assessed. (C) MLVgag-GFP pseudovirions lacking viral GPs are bound and internalized at least as efficiently as those bearing EBOV GP. 293T cells transduced with hACE2 (mock), hTIM1 or AA-hTIM1 were infected for 6 h with purified and RT-activity normalized MLVgag-GFP pseudovirions. The supernatant of cells expressing only GFP (mock supernatant) served as negative control. Cell surface-bound pseudovirions were detached by acid-stripping and extensive trypsinization, after which internalized virions were detected by flow cytometry. Data shown are representative of three independent experiments performed in duplicates. (D) In parallel with the infection in C, expression levels of hTIM1 and AA-hTIM1 were assessed. Figure provided by <del style="font-weight: bold; text-decoration: none;">Reid, Patrick</del>, et al. [http://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1003232 PLOS Pathology]]]</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>[[File:TIM.png|500px|thumb|right|Original figure legend: (A) VP40-GFP VLPs lacking any viral entry protein are bound and internalized by hTIM1. 293T cells transduced with hACE2 (mock), hTIM1 or AA-hTIM1 were incubated for 6 h with VP40-GFP VLPs bearing EBOV GP or no GP. Being inherently fluorescent, these VLPs can be detected independently of whether they undergo fusion, in contrast to the pseudoviruses and VLPs used in previous figures. The supernatant of cells expressing only GFP (mock supernatant) served as negative control. Uninternalized VLPs were detached by acid-stripping and extensive trypsinization, after which internalized VLPs were detected by flow cytometry. Figure depicts results representative of three independent experiments performed in duplicates. (B) In parallel with the infection in A, expression levels of hTIM1 and AA-hTIM1 were assessed. (C) MLVgag-GFP pseudovirions lacking viral GPs are bound and internalized at least as efficiently as those bearing EBOV GP. 293T cells transduced with hACE2 (mock), hTIM1 or AA-hTIM1 were infected for 6 h with purified and RT-activity normalized MLVgag-GFP pseudovirions. The supernatant of cells expressing only GFP (mock supernatant) served as negative control. Cell surface-bound pseudovirions were detached by acid-stripping and extensive trypsinization, after which internalized virions were detected by flow cytometry. Data shown are representative of three independent experiments performed in duplicates. (D) In parallel with the infection in C, expression levels of hTIM1 and AA-hTIM1 were assessed. Figure provided by <ins style="font-weight: bold; text-decoration: none;">Jemielity S</ins>, et al. [http://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1003232 PLOS Pathology]]]</div></td></tr>
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<tr><td colspan="2" class="diff-side-deleted"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>===Ebola uses apoptotic mimicry to invade cells===</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>===Ebola uses apoptotic mimicry to invade cells===</div></td></tr>
</table>Cjackson9401https://microbewiki.kenyon.edu/index.php?title=Ebola&diff=109288&oldid=prevCjackson9401: /* Ebola Evades the Immune System */2015-04-14T17:30:11Z<p><span dir="auto"><span class="autocomment">Ebola Evades the Immune System</span></span></p>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>In a normal immune system response [http://en.wikipedia.org/wiki/Interferon interferons] (IFNs) trigger the protective defenses of the [http://en.wikipedia.org/wiki/Immune_system immune system] to eliminate [http://en.wikipedia.org/wiki/Pathogen pathogens]. IFNs activate [http://en.wikipedia.org/wiki/STAT_protein Signal Transducers and Activators of Transcriptions (STAT) proteins], which in turn activate an immune response<sup>9</sup>. STAT1 is a crucial part of the Ebola viral infection pathway<sup>9</sup>. Normally STAT1 is [http://en.wikipedia.org/wiki/Phosphorylation phosphorylated] when activated, and consequently is translocated to the nucleus via karyopherin-mediated nuclear trafficking<sup>9</sup>. [http://en.wikipedia.org/wiki/Karyopherin Karyopherins], also known as [http://en.wikipedia.org/wiki/Importin importins], are responsible for the nuclear import of proteins that are too large for diffusion across the membrane, such as STAT1<sup>10</sup>. Karyopherins have specific structural features that allow them to participate in binding. Karyopherin-α (Kapα) consists of ten helical repeats that are called armadillos (ARMs)<sup>11</sup>. ARMs 8-10 are important for Kapα binding to [http://www.jbc.org/content/282/8/5101.full classical nuclear localization signal] (cNLS)<sup>11</sup>. It had been shown in previous studies that Zaire Ebola virus protein VP24 has the ability to bind to karyopherin α1, α5, or α6. Thus Ebola protein VP24 selectively inhibits IFN-induced gene expression by sequestering nuclear accumulation of phosphorylated STAT1 since Kapα cannot bind to and translocate STAT1<sup>12</sup>. More recent research has shown that VP24 can also bind directly to STAT1, consequently blocking STAT1 translocation to the nucleus through two inhibitory mechanisms<sup>13</sup>. Zhang et al preformed an [http://en.wikipedia.org/wiki/ELISA ELISA test] to determine if Ebola virus VP24 or Sudan Virus VP24 could bind to purified STAT1<sup>13</sup>. It can be seen that there is a strong binding affinity between STAT1 and both versions of VP24 as compared to the negative control [http://en.wikipedia.org/wiki/Bovine_serum_albumin BSA] <sup>13</sup>.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>In a normal immune system response [http://en.wikipedia.org/wiki/Interferon interferons] (IFNs) trigger the protective defenses of the [http://en.wikipedia.org/wiki/Immune_system immune system] to eliminate [http://en.wikipedia.org/wiki/Pathogen pathogens]. IFNs activate [http://en.wikipedia.org/wiki/STAT_protein Signal Transducers and Activators of Transcriptions (STAT) proteins], which in turn activate an immune response<sup>9</sup>. STAT1 is a crucial part of the Ebola viral infection pathway<sup>9</sup>. Normally STAT1 is [http://en.wikipedia.org/wiki/Phosphorylation phosphorylated] when activated, and consequently is translocated to the nucleus via karyopherin-mediated nuclear trafficking<sup>9</sup>. [http://en.wikipedia.org/wiki/Karyopherin Karyopherins], also known as [http://en.wikipedia.org/wiki/Importin importins], are responsible for the nuclear import of proteins that are too large for diffusion across the membrane, such as STAT1<sup>10</sup>. Karyopherins have specific structural features that allow them to participate in binding. Karyopherin-α (Kapα) consists of ten helical repeats that are called armadillos (ARMs)<sup>11</sup>. ARMs 8-10 are important for Kapα binding to [http://www.jbc.org/content/282/8/5101.full classical nuclear localization signal] (cNLS)<sup>11</sup>. It had been shown in previous studies that Zaire Ebola virus protein VP24 has the ability to bind to karyopherin α1, α5, or α6. Thus Ebola protein VP24 selectively inhibits IFN-induced gene expression by sequestering nuclear accumulation of phosphorylated STAT1 since Kapα cannot bind to and translocate STAT1<sup>12</sup>. More recent research has shown that VP24 can also bind directly to STAT1, consequently blocking STAT1 translocation to the nucleus through two inhibitory mechanisms<sup>13</sup>. Zhang et al preformed an [http://en.wikipedia.org/wiki/ELISA ELISA test] to determine if Ebola virus VP24 or Sudan Virus VP24 could bind to purified STAT1<sup>13</sup>. It can be seen that there is a strong binding affinity between STAT1 and both versions of VP24 as compared to the negative control [http://en.wikipedia.org/wiki/Bovine_serum_albumin BSA] <sup>13</sup>.</div></td></tr>
<tr><td colspan="2" class="diff-side-deleted"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;"></ins></div></td></tr>
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<tr><td colspan="2" class="diff-side-deleted"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;"></ins></div></td></tr>
<tr><td colspan="2" class="diff-side-deleted"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">[[File:TIM.png|500px|thumb|right|Original figure legend: (A) VP40-GFP VLPs lacking any viral entry protein are bound and internalized by hTIM1. 293T cells transduced with hACE2 (mock), hTIM1 or AA-hTIM1 were incubated for 6 h with VP40-GFP VLPs bearing EBOV GP or no GP. Being inherently fluorescent, these VLPs can be detected independently of whether they undergo fusion, in contrast to the pseudoviruses and VLPs used in previous figures. The supernatant of cells expressing only GFP (mock supernatant) served as negative control. Uninternalized VLPs were detached by acid-stripping and extensive trypsinization, after which internalized VLPs were detected by flow cytometry. Figure depicts results representative of three independent experiments performed in duplicates. (B) In parallel with the infection in A, expression levels of hTIM1 and AA-hTIM1 were assessed. (C) MLVgag-GFP pseudovirions lacking viral GPs are bound and internalized at least as efficiently as those bearing EBOV GP. 293T cells transduced with hACE2 (mock), hTIM1 or AA-hTIM1 were infected for 6 h with purified and RT-activity normalized MLVgag-GFP pseudovirions. The supernatant of cells expressing only GFP (mock supernatant) served as negative control. Cell surface-bound pseudovirions were detached by acid-stripping and extensive trypsinization, after which internalized virions were detected by flow cytometry. Data shown are representative of three independent experiments performed in duplicates. (D) In parallel with the infection in C, expression levels of hTIM1 and AA-hTIM1 were assessed. Figure provided by Reid, Patrick, et al. [http://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1003232 PLOS Pathology]]]</ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>===Ebola uses apoptotic mimicry to invade cells===</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>===Ebola uses apoptotic mimicry to invade cells===</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del style="font-weight: bold; text-decoration: none;">[[File:TIM.png|500px|thumb|right|Original figure legend: (A) VP40-GFP VLPs lacking any viral entry protein are bound and internalized by hTIM1. 293T cells transduced with hACE2 (mock), hTIM1 or AA-hTIM1 were incubated for 6 h with VP40-GFP VLPs bearing EBOV GP or no GP. Being inherently fluorescent, these VLPs can be detected independently of whether they undergo fusion, in contrast to the pseudoviruses and VLPs used in previous figures. The supernatant of cells expressing only GFP (mock supernatant) served as negative control. Uninternalized VLPs were detached by acid-stripping and extensive trypsinization, after which internalized VLPs were detected by flow cytometry. Figure depicts results representative of three independent experiments performed in duplicates. (B) In parallel with the infection in A, expression levels of hTIM1 and AA-hTIM1 were assessed. (C) MLVgag-GFP pseudovirions lacking viral GPs are bound and internalized at least as efficiently as those bearing EBOV GP. 293T cells transduced with hACE2 (mock), hTIM1 or AA-hTIM1 were infected for 6 h with purified and RT-activity normalized MLVgag-GFP pseudovirions. The supernatant of cells expressing only GFP (mock supernatant) served as negative control. Cell surface-bound pseudovirions were detached by acid-stripping and extensive trypsinization, after which internalized virions were detected by flow cytometry. Data shown are representative of three independent experiments performed in duplicates. (D) In parallel with the infection in C, expression levels of hTIM1 and AA-hTIM1 were assessed. Figure provided by Reid, Patrick, et al. [http://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1003232 PLOS Pathology]]]</del></div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Ebola virus is very large, which can make it very difficult to enter using the classic [http://en.wikipedia.org/wiki/Clathrin clathrin] [http://en.wikipedia.org/wiki/Endocytosis endocytosis] pathway<sup>1</sup>. It is suspected that because of its size, Ebola is taken up through cellular [http://medical-dictionary.thefreedictionary.com/micropinocytosis micropinocytosis]<sup>1</sup>. Studies have shown that Ebola virus has an enriched amount of [http://en.wikipedia.org/wiki/Phosphatidylserine phosphatidylserine] (PS) on its surface<sup>1</sup>. PS is a type of [http://en.wikipedia.org/wiki/Lipid lipid] that is normally present in the inner leaflet of the [http://en.wikipedia.org/wiki/Cell_membrane plasma membrane] in healthy cells<sup>1</sup>. However PS is presented on the outer leaflet when the cell becomes unhealthy or is partaking in a [http://en.wikipedia.org/wiki/Programmed_cell_death programmed cell death] mechanism<sup>15</sup>. PS on the outer leaflet signals neighboring cells to [http://en.wikipedia.org/wiki/Phagocytosis phagocytose] the ‘marked’ cell<sup>15</sup>. This mechanism is mediated by TIM1 and does not produce an inflammatory or immune response<sup>14</sup>. Consequently this form of viral uptake has been termed ‘apoptotic mimicry’ and ensures that the virus will be taken into the cell without signaling the immune system<sup>1</sup>.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Ebola virus is very large, which can make it very difficult to enter using the classic [http://en.wikipedia.org/wiki/Clathrin clathrin] [http://en.wikipedia.org/wiki/Endocytosis endocytosis] pathway<sup>1</sup>. It is suspected that because of its size, Ebola is taken up through cellular [http://medical-dictionary.thefreedictionary.com/micropinocytosis micropinocytosis]<sup>1</sup>. Studies have shown that Ebola virus has an enriched amount of [http://en.wikipedia.org/wiki/Phosphatidylserine phosphatidylserine] (PS) on its surface<sup>1</sup>. PS is a type of [http://en.wikipedia.org/wiki/Lipid lipid] that is normally present in the inner leaflet of the [http://en.wikipedia.org/wiki/Cell_membrane plasma membrane] in healthy cells<sup>1</sup>. However PS is presented on the outer leaflet when the cell becomes unhealthy or is partaking in a [http://en.wikipedia.org/wiki/Programmed_cell_death programmed cell death] mechanism<sup>15</sup>. PS on the outer leaflet signals neighboring cells to [http://en.wikipedia.org/wiki/Phagocytosis phagocytose] the ‘marked’ cell<sup>15</sup>. This mechanism is mediated by TIM1 and does not produce an inflammatory or immune response<sup>14</sup>. Consequently this form of viral uptake has been termed ‘apoptotic mimicry’ and ensures that the virus will be taken into the cell without signaling the immune system<sup>1</sup>.</div></td></tr>
</table>Cjackson9401https://microbewiki.kenyon.edu/index.php?title=Ebola&diff=109287&oldid=prevCjackson9401: /* Ebola Evades the Immune System */2015-04-14T17:29:32Z<p><span dir="auto"><span class="autocomment">Ebola Evades the Immune System</span></span></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 17:29, 14 April 2015</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>===Ebola uses apoptotic mimicry to invade cells===</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>===Ebola uses apoptotic mimicry to invade cells===</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>[[File:TIM.png|500px|thumb|right|Figure provided by Reid, Patrick, et al. [http://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1003232 PLOS Pathology]]]</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>[[File:TIM.png|500px|thumb|right|<ins style="font-weight: bold; text-decoration: none;">Original figure legend: (A) VP40-GFP VLPs lacking any viral entry protein are bound and internalized by hTIM1. 293T cells transduced with hACE2 (mock), hTIM1 or AA-hTIM1 were incubated for 6 h with VP40-GFP VLPs bearing EBOV GP or no GP. Being inherently fluorescent, these VLPs can be detected independently of whether they undergo fusion, in contrast to the pseudoviruses and VLPs used in previous figures. The supernatant of cells expressing only GFP (mock supernatant) served as negative control. Uninternalized VLPs were detached by acid-stripping and extensive trypsinization, after which internalized VLPs were detected by flow cytometry. Figure depicts results representative of three independent experiments performed in duplicates. (B) In parallel with the infection in A, expression levels of hTIM1 and AA-hTIM1 were assessed. (C) MLVgag-GFP pseudovirions lacking viral GPs are bound and internalized at least as efficiently as those bearing EBOV GP. 293T cells transduced with hACE2 (mock), hTIM1 or AA-hTIM1 were infected for 6 h with purified and RT-activity normalized MLVgag-GFP pseudovirions. The supernatant of cells expressing only GFP (mock supernatant) served as negative control. Cell surface-bound pseudovirions were detached by acid-stripping and extensive trypsinization, after which internalized virions were detected by flow cytometry. Data shown are representative of three independent experiments performed in duplicates. (D) In parallel with the infection in C, expression levels of hTIM1 and AA-hTIM1 were assessed. </ins>Figure provided by Reid, Patrick, et al. [http://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1003232 PLOS Pathology]]]</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Ebola virus is very large, which can make it very difficult to enter using the classic [http://en.wikipedia.org/wiki/Clathrin clathrin] [http://en.wikipedia.org/wiki/Endocytosis endocytosis] pathway<sup>1</sup>. It is suspected that because of its size, Ebola is taken up through cellular [http://medical-dictionary.thefreedictionary.com/micropinocytosis micropinocytosis]<sup>1</sup>. Studies have shown that Ebola virus has an enriched amount of [http://en.wikipedia.org/wiki/Phosphatidylserine phosphatidylserine] (PS) on its surface<sup>1</sup>. PS is a type of [http://en.wikipedia.org/wiki/Lipid lipid] that is normally present in the inner leaflet of the [http://en.wikipedia.org/wiki/Cell_membrane plasma membrane] in healthy cells<sup>1</sup>. However PS is presented on the outer leaflet when the cell becomes unhealthy or is partaking in a [http://en.wikipedia.org/wiki/Programmed_cell_death programmed cell death] mechanism<sup>15</sup>. PS on the outer leaflet signals neighboring cells to [http://en.wikipedia.org/wiki/Phagocytosis phagocytose] the ‘marked’ cell<sup>15</sup>. This mechanism is mediated by TIM1 and does not produce an inflammatory or immune response<sup>14</sup>. Consequently this form of viral uptake has been termed ‘apoptotic mimicry’ and ensures that the virus will be taken into the cell without signaling the immune system<sup>1</sup>.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Ebola virus is very large, which can make it very difficult to enter using the classic [http://en.wikipedia.org/wiki/Clathrin clathrin] [http://en.wikipedia.org/wiki/Endocytosis endocytosis] pathway<sup>1</sup>. It is suspected that because of its size, Ebola is taken up through cellular [http://medical-dictionary.thefreedictionary.com/micropinocytosis micropinocytosis]<sup>1</sup>. Studies have shown that Ebola virus has an enriched amount of [http://en.wikipedia.org/wiki/Phosphatidylserine phosphatidylserine] (PS) on its surface<sup>1</sup>. PS is a type of [http://en.wikipedia.org/wiki/Lipid lipid] that is normally present in the inner leaflet of the [http://en.wikipedia.org/wiki/Cell_membrane plasma membrane] in healthy cells<sup>1</sup>. However PS is presented on the outer leaflet when the cell becomes unhealthy or is partaking in a [http://en.wikipedia.org/wiki/Programmed_cell_death programmed cell death] mechanism<sup>15</sup>. PS on the outer leaflet signals neighboring cells to [http://en.wikipedia.org/wiki/Phagocytosis phagocytose] the ‘marked’ cell<sup>15</sup>. This mechanism is mediated by TIM1 and does not produce an inflammatory or immune response<sup>14</sup>. Consequently this form of viral uptake has been termed ‘apoptotic mimicry’ and ensures that the virus will be taken into the cell without signaling the immune system<sup>1</sup>.</div></td></tr>
</table>Cjackson9401https://microbewiki.kenyon.edu/index.php?title=Ebola&diff=109284&oldid=prevCjackson9401: /* References */2015-04-14T17:27:31Z<p><span dir="auto"><span class="autocomment">References</span></span></p>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><!--Do not remove this line--></div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><!--Do not remove this line--></div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Edited by Constanza Jackson, a student of [http://www.jsd.claremont.edu/faculty/profile.asp?FacultyID=254 Nora Sullivan] in BIOL168L (Microbiology) in [http://www.jsd.claremont.edu/ The Keck Science Department of the Claremont Colleges] Spring <del style="font-weight: bold; text-decoration: none;">2014</del>.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>Edited by Constanza Jackson, a student of [http://www.jsd.claremont.edu/faculty/profile.asp?FacultyID=254 Nora Sullivan] in BIOL168L (Microbiology) in [http://www.jsd.claremont.edu/ The Keck Science Department of the Claremont Colleges] Spring <ins style="font-weight: bold; text-decoration: none;">2015</ins>.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><!--Do not edit or remove this line-->[[Category:Pages edited by students of Nora Sullivan at the Claremont Colleges]]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><!--Do not edit or remove this line-->[[Category:Pages edited by students of Nora Sullivan at the Claremont Colleges]]</div></td></tr>
</table>Cjackson9401https://microbewiki.kenyon.edu/index.php?title=Ebola&diff=109283&oldid=prevCjackson9401: /* Ebola uses apoptotic mimicry to invade cells */2015-04-14T17:26:52Z<p><span dir="auto"><span class="autocomment">Ebola uses apoptotic mimicry to invade cells</span></span></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 17:26, 14 April 2015</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l46">Line 46:</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Ebola virus is very large, which can make it very difficult to enter using the classic [http://en.wikipedia.org/wiki/Clathrin clathrin] [http://en.wikipedia.org/wiki/Endocytosis endocytosis] pathway<sup>1</sup>. It is suspected that because of its size, Ebola is taken up through cellular [http://medical-dictionary.thefreedictionary.com/micropinocytosis micropinocytosis]<sup>1</sup>. Studies have shown that Ebola virus has an enriched amount of [http://en.wikipedia.org/wiki/Phosphatidylserine phosphatidylserine] (PS) on its surface<sup>1</sup>. PS is a type of [http://en.wikipedia.org/wiki/Lipid lipid] that is normally present in the inner leaflet of the [http://en.wikipedia.org/wiki/Cell_membrane plasma membrane] in healthy cells<sup>1</sup>. However PS is presented on the outer leaflet when the cell becomes unhealthy or is partaking in a [http://en.wikipedia.org/wiki/Programmed_cell_death programmed cell death] mechanism<sup>15</sup>. PS on the outer leaflet signals neighboring cells to [http://en.wikipedia.org/wiki/Phagocytosis phagocytose] the ‘marked’ cell<sup>15</sup>. This mechanism is mediated by TIM1 and does not produce an inflammatory or immune response<sup>14</sup>. Consequently this form of viral uptake has been termed ‘apoptotic mimicry’ and ensures that the virus will be taken into the cell without signaling the immune system<sup>1</sup>.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Ebola virus is very large, which can make it very difficult to enter using the classic [http://en.wikipedia.org/wiki/Clathrin clathrin] [http://en.wikipedia.org/wiki/Endocytosis endocytosis] pathway<sup>1</sup>. It is suspected that because of its size, Ebola is taken up through cellular [http://medical-dictionary.thefreedictionary.com/micropinocytosis micropinocytosis]<sup>1</sup>. Studies have shown that Ebola virus has an enriched amount of [http://en.wikipedia.org/wiki/Phosphatidylserine phosphatidylserine] (PS) on its surface<sup>1</sup>. PS is a type of [http://en.wikipedia.org/wiki/Lipid lipid] that is normally present in the inner leaflet of the [http://en.wikipedia.org/wiki/Cell_membrane plasma membrane] in healthy cells<sup>1</sup>. However PS is presented on the outer leaflet when the cell becomes unhealthy or is partaking in a [http://en.wikipedia.org/wiki/Programmed_cell_death programmed cell death] mechanism<sup>15</sup>. PS on the outer leaflet signals neighboring cells to [http://en.wikipedia.org/wiki/Phagocytosis phagocytose] the ‘marked’ cell<sup>15</sup>. This mechanism is mediated by TIM1 and does not produce an inflammatory or immune response<sup>14</sup>. Consequently this form of viral uptake has been termed ‘apoptotic mimicry’ and ensures that the virus will be taken into the cell without signaling the immune system<sup>1</sup>.</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>T-cell Immunoglobulin and Mucin-domain containing proteins (TIM) selectively bind to PS<sup>14</sup>. Very recent research has demonstrated that when PS receptors on macrophages are inhibited, Ebola virus entry is blocked<sup>14</sup>. This data suggests that TIM is responsible in some part for the micropinocytosis of large enveloped viruses<sup>14</sup>. Jemielity S, et al tested this hypothesis by using GFP-fused matrix proteins as reporters that allow the detection of prefusion stages of viral entry<sup>14</sup>. The results of the figure provided indicate that virions bind to and internalize using TIM1 in a way that is not dependent on viral entry proteins but rather on the components of the viral membrane<sup>14</sup>.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>T-cell Immunoglobulin and Mucin-domain containing proteins (TIM) selectively bind to PS<sup>14</sup>. Very recent research has demonstrated that when PS receptors on <ins style="font-weight: bold; text-decoration: none;">[http://en.wikipedia.org/wiki/Macrophage </ins>macrophages<ins style="font-weight: bold; text-decoration: none;">] </ins>are inhibited, Ebola virus entry is blocked<sup>14</sup>. This data suggests that TIM is responsible in some part for the micropinocytosis of large enveloped viruses<sup>14</sup>. Jemielity S, et al tested this hypothesis by using <ins style="font-weight: bold; text-decoration: none;">[http://en.wikipedia.org/wiki/Green_fluorescent_protein </ins>GFP<ins style="font-weight: bold; text-decoration: none;">]</ins>-fused matrix proteins as <ins style="font-weight: bold; text-decoration: none;">[http://www.bio.davidson.edu/genomics/method/reporters.html </ins>reporters<ins style="font-weight: bold; text-decoration: none;">] </ins>that allow the detection of prefusion stages of viral entry<sup>14</sup>. The results of the figure provided indicate that virions bind to and internalize using TIM1 in a way that is not dependent on viral entry proteins but rather on the components of the viral membrane<sup>14</sup>.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==Further Reading==</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>==Further Reading==</div></td></tr>
</table>Cjackson9401https://microbewiki.kenyon.edu/index.php?title=Ebola&diff=109282&oldid=prevCjackson9401: /* Ebola uses apoptotic mimicry to invade cells */2015-04-14T17:24:49Z<p><span dir="auto"><span class="autocomment">Ebola uses apoptotic mimicry to invade cells</span></span></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 17:24, 14 April 2015</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Ebola virus is very large, which can make it very difficult to enter using the classic [http://en.wikipedia.org/wiki/Clathrin clathrin] [http://en.wikipedia.org/wiki/Endocytosis endocytosis] pathway<sup>1</sup>. It is suspected that because of its size, Ebola is taken up through cellular [http://medical-dictionary.thefreedictionary.com/micropinocytosis micropinocytosis]<sup>1</sup>. Studies have shown that Ebola virus has an enriched amount of [http://en.wikipedia.org/wiki/Phosphatidylserine phosphatidylserine] (PS) on its surface<sup>1</sup>. PS is a type of [http://en.wikipedia.org/wiki/Lipid lipid] that is normally present in the inner leaflet of the [http://en.wikipedia.org/wiki/Cell_membrane plasma membrane] in healthy cells<sup>1</sup>. However PS is presented on the outer leaflet when the cell becomes unhealthy or is partaking in a [http://en.wikipedia.org/wiki/Programmed_cell_death programmed cell death] mechanism<sup>15</sup>. PS on the outer leaflet signals neighboring cells to [http://en.wikipedia.org/wiki/Phagocytosis phagocytose] the ‘marked’ cell<sup>15</sup>. This mechanism is mediated by TIM1 and does not produce an inflammatory or immune response<sup>14</sup>. Consequently this form of viral uptake has been termed ‘apoptotic mimicry’ and ensures that the virus will be taken into the cell without signaling the immune system<sup>1</sup>.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Ebola virus is very large, which can make it very difficult to enter using the classic [http://en.wikipedia.org/wiki/Clathrin clathrin] [http://en.wikipedia.org/wiki/Endocytosis endocytosis] pathway<sup>1</sup>. It is suspected that because of its size, Ebola is taken up through cellular [http://medical-dictionary.thefreedictionary.com/micropinocytosis micropinocytosis]<sup>1</sup>. Studies have shown that Ebola virus has an enriched amount of [http://en.wikipedia.org/wiki/Phosphatidylserine phosphatidylserine] (PS) on its surface<sup>1</sup>. PS is a type of [http://en.wikipedia.org/wiki/Lipid lipid] that is normally present in the inner leaflet of the [http://en.wikipedia.org/wiki/Cell_membrane plasma membrane] in healthy cells<sup>1</sup>. However PS is presented on the outer leaflet when the cell becomes unhealthy or is partaking in a [http://en.wikipedia.org/wiki/Programmed_cell_death programmed cell death] mechanism<sup>15</sup>. PS on the outer leaflet signals neighboring cells to [http://en.wikipedia.org/wiki/Phagocytosis phagocytose] the ‘marked’ cell<sup>15</sup>. This mechanism is mediated by TIM1 and does not produce an inflammatory or immune response<sup>14</sup>. Consequently this form of viral uptake has been termed ‘apoptotic mimicry’ and ensures that the virus will be taken into the cell without signaling the immune system<sup>1</sup>.</div></td></tr>
<tr><td colspan="2" class="diff-side-deleted"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">T-cell Immunoglobulin and Mucin-domain containing proteins (TIM) selectively bind to PS<sup>14</sup>. Very recent research has demonstrated that when PS receptors on macrophages are inhibited, Ebola virus entry is blocked<sup>14</sup>. This data suggests that TIM is responsible in some part for the micropinocytosis of large enveloped viruses<sup>14</sup>. Jemielity S, et al tested this hypothesis by using GFP-fused matrix proteins as reporters that allow the detection of prefusion stages of viral entry<sup>14</sup>. The results of the figure provided indicate that virions bind to and internalize using TIM1 in a way that is not dependent on viral entry proteins but rather on the components of the viral membrane<sup>14</sup>.</ins></div></td></tr>
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</table>Cjackson9401https://microbewiki.kenyon.edu/index.php?title=Ebola&diff=109079&oldid=prevCjackson9401: /* Ebola Evades the Immune System */2015-04-14T10:43:42Z<p><span dir="auto"><span class="autocomment">Ebola Evades the Immune System</span></span></p>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[File:TIM.png|500px|thumb|right|Figure provided by Reid, Patrick, et al. [http://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1003232 PLOS Pathology]]]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>[[File:TIM.png|500px|thumb|right|Figure provided by Reid, Patrick, et al. [http://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1003232 PLOS Pathology]]]</div></td></tr>
<tr><td colspan="2" class="diff-side-deleted"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;"></ins></div></td></tr>
<tr><td colspan="2" class="diff-side-deleted"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">Ebola virus is very large, which can make it very difficult to enter using the classic [http://en.wikipedia.org/wiki/Clathrin clathrin] [http://en.wikipedia.org/wiki/Endocytosis endocytosis] pathway<sup>1</sup>. It is suspected that because of its size, Ebola is taken up through cellular [http://medical-dictionary.thefreedictionary.com/micropinocytosis micropinocytosis]<sup>1</sup>. Studies have shown that Ebola virus has an enriched amount of [http://en.wikipedia.org/wiki/Phosphatidylserine phosphatidylserine] (PS) on its surface<sup>1</sup>. PS is a type of [http://en.wikipedia.org/wiki/Lipid lipid] that is normally present in the inner leaflet of the [http://en.wikipedia.org/wiki/Cell_membrane plasma membrane] in healthy cells<sup>1</sup>. However PS is presented on the outer leaflet when the cell becomes unhealthy or is partaking in a [http://en.wikipedia.org/wiki/Programmed_cell_death programmed cell death] mechanism<sup>15</sup>. PS on the outer leaflet signals neighboring cells to [http://en.wikipedia.org/wiki/Phagocytosis phagocytose] the ‘marked’ cell<sup>15</sup>. This mechanism is mediated by TIM1 and does not produce an inflammatory or immune response<sup>14</sup>. Consequently this form of viral uptake has been termed ‘apoptotic mimicry’ and ensures that the virus will be taken into the cell without signaling the immune system<sup>1</sup>.</ins></div></td></tr>
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</table>Cjackson9401https://microbewiki.kenyon.edu/index.php?title=Ebola&diff=109070&oldid=prevCjackson9401: /* Ebola viral protein VP24 */2015-04-14T10:38:53Z<p><span dir="auto"><span class="autocomment">Ebola viral protein VP24</span></span></p>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>In a normal immune system response [http://en.wikipedia.org/wiki/Interferon interferons] (IFNs) trigger the protective defenses of the [http://en.wikipedia.org/wiki/Immune_system immune system] to eliminate [http://en.wikipedia.org/wiki/Pathogen pathogens]. IFNs activate [http://en.wikipedia.org/wiki/STAT_protein Signal Transducers and Activators of Transcriptions (STAT) proteins], which in turn activate an immune response<sup>9</sup>. STAT1 is a crucial part of the Ebola viral infection pathway<sup>9</sup>. Normally STAT1 is [http://en.wikipedia.org/wiki/Phosphorylation phosphorylated] when activated, and consequently is translocated to the nucleus via karyopherin-mediated nuclear trafficking<sup>9</sup>. [http://en.wikipedia.org/wiki/Karyopherin Karyopherins], also known as [http://en.wikipedia.org/wiki/Importin importins], are responsible for the nuclear import of proteins that are too large for diffusion across the membrane, such as STAT1<sup>10</sup>. Karyopherins have specific structural features that allow them to participate in binding. Karyopherin-α (Kapα) consists of ten helical repeats that are called armadillos (ARMs)<sup>11</sup>. ARMs 8-10 are important for Kapα binding to [http://www.jbc.org/content/282/8/5101.full classical nuclear localization signal] (cNLS)<sup>11</sup>. It had been shown in previous studies that Zaire Ebola virus protein VP24 has the ability to bind to karyopherin α1, α5, or α6. Thus Ebola protein VP24 selectively inhibits IFN-induced gene expression by sequestering nuclear accumulation of phosphorylated STAT1 since Kapα cannot bind to and translocate STAT1<sup>12</sup>. More recent research has shown that VP24 can also bind directly to STAT1, consequently blocking STAT1 translocation to the nucleus through two inhibitory mechanisms<sup>13</sup>. Zhang et al preformed an [http://en.wikipedia.org/wiki/ELISA ELISA test] to determine if Ebola virus VP24 or Sudan Virus VP24 could bind to purified STAT1<sup>13</sup>. It can be seen that there is a strong binding affinity between STAT1 and both versions of VP24 as compared to the negative control [http://en.wikipedia.org/wiki/Bovine_serum_albumin BSA] <sup>13</sup>.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>In a normal immune system response [http://en.wikipedia.org/wiki/Interferon interferons] (IFNs) trigger the protective defenses of the [http://en.wikipedia.org/wiki/Immune_system immune system] to eliminate [http://en.wikipedia.org/wiki/Pathogen pathogens]. IFNs activate [http://en.wikipedia.org/wiki/STAT_protein Signal Transducers and Activators of Transcriptions (STAT) proteins], which in turn activate an immune response<sup>9</sup>. STAT1 is a crucial part of the Ebola viral infection pathway<sup>9</sup>. Normally STAT1 is [http://en.wikipedia.org/wiki/Phosphorylation phosphorylated] when activated, and consequently is translocated to the nucleus via karyopherin-mediated nuclear trafficking<sup>9</sup>. [http://en.wikipedia.org/wiki/Karyopherin Karyopherins], also known as [http://en.wikipedia.org/wiki/Importin importins], are responsible for the nuclear import of proteins that are too large for diffusion across the membrane, such as STAT1<sup>10</sup>. Karyopherins have specific structural features that allow them to participate in binding. Karyopherin-α (Kapα) consists of ten helical repeats that are called armadillos (ARMs)<sup>11</sup>. ARMs 8-10 are important for Kapα binding to [http://www.jbc.org/content/282/8/5101.full classical nuclear localization signal] (cNLS)<sup>11</sup>. It had been shown in previous studies that Zaire Ebola virus protein VP24 has the ability to bind to karyopherin α1, α5, or α6. Thus Ebola protein VP24 selectively inhibits IFN-induced gene expression by sequestering nuclear accumulation of phosphorylated STAT1 since Kapα cannot bind to and translocate STAT1<sup>12</sup>. More recent research has shown that VP24 can also bind directly to STAT1, consequently blocking STAT1 translocation to the nucleus through two inhibitory mechanisms<sup>13</sup>. Zhang et al preformed an [http://en.wikipedia.org/wiki/ELISA ELISA test] to determine if Ebola virus VP24 or Sudan Virus VP24 could bind to purified STAT1<sup>13</sup>. It can be seen that there is a strong binding affinity between STAT1 and both versions of VP24 as compared to the negative control [http://en.wikipedia.org/wiki/Bovine_serum_albumin BSA] <sup>13</sup>.</div></td></tr>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>===Ebola uses apoptotic mimicry to invade cells===</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>===Ebola uses apoptotic mimicry to invade cells===</div></td></tr>
</table>Cjackson9401https://microbewiki.kenyon.edu/index.php?title=Ebola&diff=109069&oldid=prevCjackson9401: /* References */2015-04-14T10:38:25Z<p><span dir="auto"><span class="autocomment">References</span></span></p>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> [http://www.ncbi.nlm.nih.gov/pubmed/17928350 12. Reid, Patrick, et al. Ebola Virus VP24 Proteins Inhibit the Interaction of NPI-1 Subfamily Karyopherin α Proteins with Activated STAT1. Journal of Virology. 2007, 13469-13477.]<br></div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> [http://www.ncbi.nlm.nih.gov/pubmed/17928350 12. Reid, Patrick, et al. Ebola Virus VP24 Proteins Inhibit the Interaction of NPI-1 Subfamily Karyopherin α Proteins with Activated STAT1. Journal of Virology. 2007, 13469-13477.]<br></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><br> [http://www.plospathogens.org/article/fetchObject.action?uri=info:doi/10.1371/journal.ppat.1002550&representation=PDF 13. Zhang, Adrianna, et al. The Ebola Virus Interferon Antagonist VP24 Directly Binds STAT1 and Has a Novel, Pyramidal Fold. Plos Pathogens. 2013. 1-12.]</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><br> [http://www.plospathogens.org/article/fetchObject.action?uri=info:doi/10.1371/journal.ppat.1002550&representation=PDF 13. Zhang, Adrianna, et al. The Ebola Virus Interferon Antagonist VP24 Directly Binds STAT1 and Has a Novel, Pyramidal Fold. Plos Pathogens. 2013. 1-12.]<ins style="font-weight: bold; text-decoration: none;"><br></ins></div></td></tr>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> [http://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1003232 14. Jemielity S, et al. TIM-family Proteins Promote Infection of Multiple Enveloped Viruses through Virion-associated Phosphatidylserine. PLoS. 2013, 9, 1-14.]<br></div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> [http://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1003232 14. Jemielity S, et al. TIM-family Proteins Promote Infection of Multiple Enveloped Viruses through Virion-associated Phosphatidylserine. PLoS. 2013, 9, 1-14.]<br></div></td></tr>
</table>Cjackson9401https://microbewiki.kenyon.edu/index.php?title=Ebola&diff=109068&oldid=prevCjackson9401: /* References */2015-04-14T10:37:57Z<p><span dir="auto"><span class="autocomment">References</span></span></p>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> [http://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1003232 14. Jemielity S, et al. TIM-family Proteins Promote Infection of Multiple Enveloped Viruses through Virion-associated Phosphatidylserine. PLoS. 2013, 9, 1-14.]<br></div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div><br> [http://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1003232 14. Jemielity S, et al. TIM-family Proteins Promote Infection of Multiple Enveloped Viruses through Virion-associated Phosphatidylserine. PLoS. 2013, 9, 1-14.]<br></div></td></tr>
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<tr><td colspan="2" class="diff-side-deleted"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;"><br> [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1134557/pdf/biochemj00105-0011.pdf 15. Zachowski, A, et al. Phospholipids in animal eukaryotic membranes: transverse asymmetry and movement. Biochem. 1993. 1–14.]<br></ins></div></td></tr>
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</table>Cjackson9401