Mason pfizer monkey virus
A Microbial Biorealm page on the genus Mason pfizer monkey virus
Classification
Higher order taxa
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae; Betaretrovirus [Others may be used. Use NCBI link to find]
Species
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NCBI: Taxonomy |
Genus species
* Human type D retrovirus
* Simian retrovirus 1
* Simian retrovirus 2
o Simian retrovirus srv-2 (isolate 2R-18B1)
* Simian SRV-like type D retrovirus
* Simian type D retrovirus -Tsukuba
* unidentified simian type D retrovirus
Description and significance
Describe the appearance, habitat, etc. of the organism, and why you think it is important.
Genome structure
Describe the size and content of the genome. How many chromosomes? Circular or linear? Other interesting features? What is known about its sequence?
ssRNA; linear; Length: 8,557 nt Replicon Type: viral segment 4 protein coding genes, 2 non protein coding genes Three gag-pro-pol-env, MPMVgp1, with protein products
Pr95 DU RT-IN gp70 SU gp20 TM p12 PR
RT-IN - RT_Rtv: Reverse transcriptases (RTs) from retroviruses (Rtvs). RTs catalyze the conversion of single-stranded RNA into double-stranded viral DNA for integration into host chromosomes. Proteins in this subfamily contain long terminal repeats (LTRs) and are multifunctional enzymes with RNA-directed DNA polymerase, DNA directed DNA polymerase, and ribonuclease hybrid (RNase H) activities. The viral RNA genome enters the cytoplasm as part of a nucleoprotein complex, and the process of reverse transcription generates in the cytoplasm forming a linear DNA duplex via an intricate series of steps. This duplex DNA is colinear with its RNA template, but contains terminal duplications known as LTRs that are not present in viral RNA. It has been proposed that two specialized template switches, known as strand-transfer reactions or "jumps", are required to generate the LTRs. PMID 9831551
Reverse transcriptase thumb domain. This domain is known as the thumb domain. It is composed of a four helix bundle. PMID: 1377403
Retroviral aspartyl protease. Single domain aspartyl proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses). These proteases are generally part of a larger polyprotein; usually pol, more rarely gag. Retroviral proteases appear to be homologous to a single domain of the two-domain eukaryotic aspartyl proteases such as pepsins, cathepsins, and renins (pfam00026)-Marchler-Bauer A, Anderson JB, Derbyshire MK, DeWeese-Scott C, Gonzales NR, Gwadz M, Hao L, He S, Hurwitz DI, Jackson JD, Ke Z, Krylov D, Lanczycki CJ, Liebert CA, Liu C, Lu F, Lu S, Marchler GH, Mullokandov M, Song JS, Thanki N, Yamashita RA, Yin JJ, Zhang D, Bryant SH. (2007) CDD: a conserved domain database for interactive domain family analysis. Nucleic Acids Res. 35: D237-40
RnaseH; RNase H. RNase H digests the RNA strand of an RNA/DNA hybrid. Important enzyme in retroviral replication cycle, and often found as a domain associated with reverse transcriptases. Structure is a mixed alpha+beta fold with three a/b/a layers. -Marchler-Bauer A, Anderson JB, Derbyshire MK, DeWeese-Scott C, Gonzales NR, Gwadz M, Hao L, He S, Hurwitz DI, Jackson JD, Ke Z, Krylov D, Lanczycki CJ, Liebert CA, Liu C, Lu F, Lu S, Marchler GH, Mullokandov M, Song JS, Thanki N, Yamashita RA, Yin JJ, Zhang D, Bryant SH. (2007) CDD: a conserved domain database for interactive domain family analysis. Nucleic Acids Res. 35: D237-40
Integrase Zinc binding domain. Integrase mediates integration of a DNA copy of the viral genome into the host chromosome. Integrase is composed of three domains. This domain is the amino-terminal domain zinc binding domain. The central domain is the catalytic domain pfam00665. The carboxyl terminal domain is a DNA binding domain pfam00552. PMID: 9228950
Integrase DNA binding domain. Integrase mediates integration of a DNA copy of the viral genome into the host chromosome. Integrase is composed of three domains. The amino-terminal domain is a zinc binding domain. The central domain is the catalytic domain pfam00665. This domain is the carboxyl terminal domain that is a non-specific DNA binding domain. PMID: 7632683
Pr95 -
gp20 TM - ENV polyprotein (coat polyprotein). - Marchler-Bauer A, Anderson JB, Derbyshire MK, DeWeese-Scott C, Gonzales NR, Gwadz M, Hao L, He S, Hurwitz DI, Jackson JD, Ke Z, Krylov D, Lanczycki CJ, Liebert CA, Liu C, Lu F, Lu S, Marchler GH, Mullokandov M, Song JS, Thanki N, Yamashita RA, Yin JJ, Zhang D, Bryant SH. (2007) CDD: a conserved domain database for interactive domain family analysis. Nucleic Acids Res. 35: D237-40 - gag gene protein p24 (core nucleocapsid protein). p24 forms inner protein layer of the nucleocapsid. ELISA tests for p24 is the most commonly used method to demonstrate virus replication both in vivo and in vitro. PMID: 9245608
gp70 SU - ENV polyprotein (coat polyprotein)- Marchler-Bauer A, Anderson JB, Derbyshire MK, DeWeese-Scott C, Gonzales NR, Gwadz M, Hao L, He S, Hurwitz DI, Jackson JD, Ke Z, Krylov D, Lanczycki CJ, Liebert CA, Liu C, Lu F, Lu S, Marchler GH, Mullokandov M, Song JS, Thanki N, Yamashita RA, Yin JJ, Zhang D, Bryant SH. (2007) CDD: a conserved domain database for interactive domain family analysis. Nucleic Acids Res. 35: D237-40
One gag, MPMVgp2, with protein product PR78. Non protein coding genes pro, MPMVgp3, and pol, MPMVgp4. Retroviral GAG p10 protein. This family consists of various retroviral GAG (core) polyproteins and encompasses the p10 region producing the p10 protein upon proteolytic cleavage of GAG by retroviral protease. The p10 or matrix protein (MA) is associated with the virus envelope glycoproteins in most mammalian retroviruses and may be involved in virus particle assembly, transport and budding. Some of the GAG polyproteins have alternate cleavage sites leading to the production of alternative and longer cleavage products (e.g. p19) the alignment of this family only covers the approximately N-terminal (GAG) 100 amino acid region of homology to p10. PMID: 9094640
Cell structure and metabolism
Interesting features of cell structure; how it gains energy; what important molecules it produces.
Ecology
Habitat; symbiosis; contributions to the environment.
Pathology
How does this organism cause disease? Human, animal, plant hosts? Virulence factors, as well as patient symptoms.
Current Research
Enter summarries of the most rescent research here--at least three required
References
Edited by student of Emily Lilly at University of Massachusetts Dartmouth.
