Viral and Cellular Proteins Involved in Coronavirus Replication
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.
KeywordsMouse Hepatitis Virus Equine Arteritis Virus Murine Coronavirus Mouse Hepatitis Virus Strain Coronavirus Replication
Unable to display preview. Download preview PDF.
- Baric RS, Nelson GW, Fleming JO, Deans RJ, Keck JG, Casteel N, Stohlman SA (1988) Interactions between coronavirus nucleocapsid protein and viral RNAs: implications for viral transcription. J Virol 62:4280–4287Google Scholar
- Bredenbeek PJ, Pachuk CJ, Noten AF, Charite J, Luytjes W, Weiss SR, Spaan WJ (1990) The primary structure and expression of the second open reading frame of the polymerase gene of the coronavirus MHV-A59; a highly conserved polymerase is expressed by an efficient ribosomal frameshifting mechanism. Nucleic Acids Res 18:1825–1832PubMedGoogle Scholar
- Denison MR, Spaan WJ, van der Meer Y, Gibson CA, Sims AC, Prentice E, Lu XT (1999) The putative helicase of the coronavirus mouse hepatitis virus is processed from the replicase gene polyprotein and localizes in complexes that are active in viral RNA synthesis. J Virol 73:6862–6871PubMedGoogle Scholar
- Gorbalenya AE, Koonin EV, Lai MM (1991) Putative papain-related thiol proteases of positive-strand RNA viruses. Identification of rubi-and aphthovirus proteases and delineation of a novel conserved domain associated with proteases of rubi-, alpha-and coronaviruses. FEBS Lett 288:201–205CrossRefPubMedGoogle Scholar
- Ma AS, Moran-Jones K, Shan J, Munro TP, Snee MJ, Hoek KS, Smith R (2002) hnRNP A3, a novel RNA trafficking response element binding protein. J Biol Chem 8:8Google Scholar
- Schalinske KL, Chen OS, Eisenstein RS (1998) Iron differentially stimulates translation of mitochondrial aconitase and ferritin mRNAs in mammalian cells. Implications for iron regulatory proteins as regulators of mitochondrial citrate utilization. J Biol Chem 273:3740–3746CrossRefPubMedGoogle Scholar