Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2005:287:95-131.
doi: 10.1007/3-540-26765-4_4.

Viral and cellular proteins involved in coronavirus replication

Affiliations
Review

Viral and cellular proteins involved in coronavirus replication

S T Shi et al. Curr Top Microbiol Immunol. 2005.

Abstract

As the largest RNA virus, coronavirus replication employs complex mechanisms and involves various viral and cellular proteins. The first open reading frame of the coronavirus genome encodes a large polyprotein, which is processed into a number of viral proteins required for viral replication directly or indirectly. These proteins include the RNA-dependent RNA polymerase (RdRp), RNA helicase, proteases, metal-binding proteins, and a number of other proteins of unknown function. Genetic studies suggest that most of these proteins are involved in viral RNA replication. In addition to viral proteins, several cellular proteins, such as heterogeneous nuclear ribonucleoprotein (hnRNP) A1, polypyrimidine-tract-binding (PTB) protein, poly(A)-binding protein (PABP), and mitochondrial aconitase (m-aconitase), have been identified to interact with the critical cis-acting elements of coronavirus replication. Like many other RNA viruses, coronavirus may subvert these cellular proteins from cellular RNA processing or translation machineries to play a role in viral replication.

PubMed Disclaimer

Similar articles

Cited by

References

    1. Ahola T., den Boon J.A., Ahlquist P. Helicase and capping enzyme active site mutations in brome mosaic virus protein 1a cause defects in template recruitment, negative-strand RNA synthesis, and viral RNA capping. J Virol. 2000;74:8803–8811. doi: 10.1128/JVI.74.19.8803-8811.2000. - DOI - PMC - PubMed
    1. Baker S.C., Lai M.M. An in vitro system for the leader-primed transcription of coronavirus mRNAs. EMBO J. 1990;9:4173–4179. - PMC - PubMed
    1. Baker S.C., Shieh C.K., Soe L.H., Chang M.F., Vannier D.M., Lai M.M. Identification of a domain required for autoproteolytic cleavage of murine coronavirus gene A polyprotein. J Virol. 1989;63:3693–3699. - PMC - PubMed
    1. Baker S.C., Yokomori K., Dong S., Carlisle R., Gorbalenya A.E., Koonin E.V., Lai M.M. Identification of the catalytic sites of a papain-like cysteine proteinase of murine coronavirus. J Virol. 1993;67:6056–6063. - PMC - PubMed
    1. Baker T.A., Bell S.P. Polymerases and the replisome: machines within machines. Cell. 1998;92:295–305. doi: 10.1016/S0092-8674(00)80923-X. - DOI - PubMed

MeSH terms

Substances