Understanding the accessory viral proteins unique to the severe acute respiratory syndrome (SARS) coronavirus
- PMID: 16820226
- PMCID: PMC7114237
- DOI: 10.1016/j.antiviral.2006.05.010
Understanding the accessory viral proteins unique to the severe acute respiratory syndrome (SARS) coronavirus
Abstract
A novel coronavirus, termed the severe acute respiratory syndrome coronavirus (SARS-CoV), infected humans in Guangdong, China, in November 2002 and the subsequent efficient human-to-human transmissions of this virus caused profound disturbances in over 30 countries worldwide in 2003. Eventually, this epidemic was controlled by isolation and there has been no human infection reported since January 2004. However, research on different aspects of the SARS-CoV is not waning, as it is not known if this virus will re-emerge, especially since its origins and potential reservoir(s) are unresolved. The SARS-CoV genome is nearly 30 kb in length and contains 14 potential open reading frames (ORFs). Some of these ORFs encode for genes that are homologous to proteins found in all known coronaviruses, namely the replicase genes (ORFs 1a and 1b) and the four structural proteins: nucleocapsid, spike, membrane and envelope, and these proteins are expected to be essential for the replication of the virus. The remaining eight ORFs encodes for accessory proteins, varying in length from 39 to 274 amino acids, which are unique to SARS-CoV. This review will summarize the expeditious research on these accessory viral proteins in three major areas: (i) the detection of antibodies against accessory proteins in the serum of infected patients, (ii) the expression, processing and cellular localization of the accessory proteins, and (iii) the effects of the accessory proteins on cellular functions. These in-depth molecular and biochemical characterizations of the SARS-CoV accessory proteins, which have no homologues in other coronaviruses, may offer clues as to why the SARS-CoV causes such a severe and rapid attack in humans, while other coronaviruses that infect humans seem to be more forgiving.
Figures
Similar articles
-
The role of severe acute respiratory syndrome (SARS)-coronavirus accessory proteins in virus pathogenesis.Viruses. 2012 Nov 7;4(11):2902-23. doi: 10.3390/v4112902. Viruses. 2012. PMID: 23202509 Free PMC article. Review.
-
Characterization of viral proteins encoded by the SARS-coronavirus genome.Antiviral Res. 2005 Feb;65(2):69-78. doi: 10.1016/j.antiviral.2004.10.001. Antiviral Res. 2005. PMID: 15708633 Free PMC article. Review.
-
The molecular biology of SARS coronavirus.Ann N Y Acad Sci. 2007 Apr;1102(1):26-38. doi: 10.1196/annals.1408.002. Ann N Y Acad Sci. 2007. PMID: 17470909 Free PMC article. Review.
-
Characterization of accessory genes in coronavirus genomes.Virol J. 2020 Aug 27;17(1):131. doi: 10.1186/s12985-020-01402-1. Virol J. 2020. PMID: 32854725 Free PMC article.
-
Severe acute respiratory syndrome coronavirus group-specific open reading frames encode nonessential functions for replication in cell cultures and mice.J Virol. 2005 Dec;79(23):14909-22. doi: 10.1128/JVI.79.23.14909-14922.2005. J Virol. 2005. PMID: 16282490 Free PMC article.
Cited by
-
Identification and epitope mapping of swine acute diarrhea syndrome coronavirus accessory protein NS7a via monoclonal antibodies.Virus Res. 2022 May;313:198742. doi: 10.1016/j.virusres.2022.198742. Epub 2022 Mar 11. Virus Res. 2022. PMID: 35283248 Free PMC article.
-
Severe acute respiratory syndrome coronavirus accessory protein 9b is a virion-associated protein.Virology. 2009 Jun 5;388(2):279-85. doi: 10.1016/j.virol.2009.03.032. Epub 2009 Apr 25. Virology. 2009. PMID: 19394665 Free PMC article.
-
Mechanisms of severe acute respiratory syndrome coronavirus-2 induced liver damage and alteration of some liver biomarkers: A review.Medicine (Baltimore). 2023 May 12;102(19):e33517. doi: 10.1097/MD.0000000000033517. Medicine (Baltimore). 2023. PMID: 37171303 Free PMC article. Review.
-
Genetic determinants of pathogenesis by feline infectious peritonitis virus.Vet Immunol Immunopathol. 2011 Oct 15;143(3-4):265-8. doi: 10.1016/j.vetimm.2011.06.021. Epub 2011 Jun 12. Vet Immunol Immunopathol. 2011. PMID: 21719115 Free PMC article. Review.
-
Beyond Channel Activity: Protein-Protein Interactions Involving Viroporins.Subcell Biochem. 2018;88:329-377. doi: 10.1007/978-981-10-8456-0_15. Subcell Biochem. 2018. PMID: 29900504 Free PMC article. Review.
References
-
- Bini A., Simpson-Haidaris P.J., Kudryk B.J. Fibrin/fibrinogen. In: Bikfalvi A., editor. Encylopedic Reference of Vascular Biology and Pathology. Springer–Verlag; Berlin: 2000. p. 372.
-
- Blatch G.L., Lassle M. The tetratricopeptide repeat: a structural motif mediating protein–protein interactions. Bioessays. 1999;21:932–939. - PubMed
-
- Brown T.D.K., Brierly I. The coronavirus nonstructural proteins. In: Siddell S.G., editor. The Coronaviridae. Plenum Press; New York, NY: 1995. pp. 191–217.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Miscellaneous