Alphacoronavirus 1

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1. Classification

Alphacoronavirus I is classified under the domain Riboviriae or Orthornavirae, phylum Pisuviricotae, class Pisoniviricetes, order Nidovirales, and family Coronaviridae [1]. Alphacoronavirus 1 can be divided into two distinct clades, A and B, based on differences in spike genes. Based on phylogenetics, feline coronavirus (FCoV) and canine coronavirus (CCoV) have evolutionarily similar spike proteins, and can be classified as clade A. A different CCoV strain has a similar spike protein to Transmissible Gastroenteritis Virus (TGEV) in pigs. These two types of Alphacoronavirus 1 are phylogenetically classified as clade B [2]. In addition, clade A contains an additional open reading frame (ORF) that is not found in clade B, further demonstrating that TGEV and CCoV strain II are distinct from CCoV I and FCoV [3].

a. Higher order taxa

Riboviriae or Orthornavirae, Pisuviricotae, Pisoniviricetes, Nidovirales, Coronaviridae

Species

NCBI: [1]

Alphacoronavirus 1”

2. Description and significance

Describe the appearance, habitat, etc. of the organism, and why you think it is important.

• Include as many headings as are relevant to your microbe. Consider using the headings below, as they will allow readers to quickly locate specific information of major interest*

3. 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?

4. Cell structure

Interesting features of cell structure. Can be combined with “metabolic processes”

5. Metabolic processes

Describe important sources of energy, electrons, and carbon (i.e. trophy) for the organism/organisms you are focusing on, as well as important molecules it/they synthesize(s).

6. Ecology

Habitat; symbiosis; contributions to the environment.

7. Pathology

How does this organism cause disease? Human, animal, plant hosts? Virulence factors, as well as patient symptoms.

8. Current Research

Include information about how this microbe (or related microbes) are currently being studied and for what purpose

9. References

1. Taxonomy browser (Alphacoronavirus 1). (n.d.). Retrieved from https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?id=693997

2. Whittaker, G. R., N. M. Andre, and J. K. Millet. 2018. Improving Virus Taxonomy by Recontextualizing Sequence-Based Classification with Biologically Relevant Data: the Case of the Alphacoronavirus 1 Species. mSphere 3(1):e00463-17.

3. Decaro, N., V. Mari, G. Elia, G. Lanave, G. Dowgier, M. L. Colaianni, V. Martella, and C. Buonavoglia. 2015. Full-Length Genome Analysis of Canine Coronavirus Type I. Virus Research 210:100–105.

4. Santana-Clavijo, N. S., D. P. Reyes Romero, D. F. Arango Fajardo, A. Velandia Muñoz, S. A. Taniwaki, S. O. de Souza Silva, and P. E. Brandão. 2020. Molecular diversity of Alphacoronavirus 1 in dogs and cats in Colombia. Heliyon 6(7):e04381.

5. Olarte Castillo, X. A., J. F. dos Remedios, F. Heeger, H. Hofer, S. Karl, A. D. Greenwood, and M. L. East. 2021. The virus-host interface: Molecular interactions of Alphacoronavirus-1 variants from wild and domestic hosts with mammalian aminopeptidase N. Molecular Ecology 30(11):2607-2625.

6. Shen, Z., G. Wang, Y. Yang, J. Shi, L. Fang, F. Li, S. Xiao, Z. F. Fu, and G. Peng. 2019. A conserved region of nonstructural protein 1 from alphacoronaviruses inhibits host gene expression and is critical for viral virulence. Journal of Biological Chemistry 294(37):13606-13618.

7. Schubert, K., E. D. Karousis, A. Jomaa, A. Scaiola, B. Echeverria, L. A. Gurzeler, M. Leibundgut, V. Thiel, O. Muhlemann, and N. Ban. 2020. SARS-CoV-2 Nsp1 binds the ribosomal mRNA channel to inhibit translation. Nature Structural & Molecular Biology 27(10):959-966.

8. Fehr, A. R., and S. Perlman. 2015. Coronaviruses: an overview of their replication and pathogenesis. Methods in Molecular Biology 1282:1–23.

9. de Barros, B., C. de Castro, D. Pereira, L. G. Ribeiro, J. Júnior, S. Casseb, G. M. Holanda, A. Cruz, E. Júnior, and J. Mascarenhas. 2019. First Complete Genome Sequence of a Feline Alphacoronavirus 1 Strain from Brazil. Microbiology Resource Announcements 8(10):e01535-18.

10. Wong, A. H. M., A. C. A. Tomlinson, D. Zhou, M. Satkunarajah, K. Chen, C. Sharon, M. Desforges, P. J. Talbot, and J. M. Rini. 2017. Receptor-binding loops in alphacoronavirus adaptation and evolution. Nature Communications 8(1):1735.

11. Shen, Z., Y. Yang, S. Yang, G. Zhang, S. Xiao, Z. F. Fu, and G. Peng. 2020. Structural and biological basis of Alphacoronavirus nsp1 associated with host proliferation and immune evasion. Viruses 12(8):812.

12. Jansson, A. M. 2013. Structure of alphacoronavirus transmissible gastroenteritis virus nsp1 has implications for coronavirus nsp1 function and evolution. Journal of virology 87(5):2949–2955.

13. Madhugiri, R., M. Fricke, M. Marz, and J. Ziebuhr. 2014. RNA structure analysis of alphacoronavirus terminal genome regions. Virus Research 194:76-89.

14. Burrough, E. R. 2021. Porcine Coronaviral Enteritis. Merck Veterinary Manual.

15. Bittar, C., R. R. Guaragna Machado, M. T. Comelis, L. M. Bueno, M. R. Beguelini, E. Morielle-Versute, M. L. Nogueira, and P. Rahal. 2020. Alphacoronavirus detection in lungs, liver, and intestines of bats from Brazil. Microbial Ecology 79(1):203-212.

16. Cruz, J. L., M. Becares, I. Sola, J. C. Oliveros, L. Enjuanes, and S. Zúñiga. 2013. Alphacoronavirus protein 7 modulates host innate immune response. Journal of virology 87(17), 9754–9767.

17. Putz, E. M., D. Gotthardt, and V. Sexl. 2014. STAT1-S727-the license to kill. Oncoimmunology 3(9):e955441.