Structural highlights
Function
POLG_RHDVA Together with NTPase and NS4, initiates the formation of the replication complex (By similarity). Induces the proliferation of the host smooth ER membranes forming long tubular structures (By similarity). These remodeled membranes probably form the viral factories that contain the replication complex (By similarity).[UniProtKB:P54634][UniProtKB:Q66914] Displays NTPase activity, but no helicase activity (By similarity). Induces the formation of convoluted membranes derived from the host ER (By similarity). These remodeled membranes probably form the viral factories that contain the replication complex (By similarity). Together with NS2 and NS4, initiates the formation of the replication complex (By similarity).[UniProtKB:P54634][UniProtKB:Q04544][UniProtKB:Q66914] Probable key protein responsible for the formation of membrane alterations by the virus (By similarity). Induces the formation of convoluted membranes derived from the host ER (By similarity). These remodeled membranes probably form the viral factories that contain the replication complex (By similarity). Together with NS2 and NTPase, initiates the formation of the replication complex (By similarity).[UniProtKB:P54634][UniProtKB:Q66914] Viral genome-linked protein is covalently linked to the 5'-end of the positive-strand, negative-strand genomic RNAs and subgenomic RNA. Acts as a genome-linked replication primer. May recruit ribosome to viral RNA thereby promoting viral proteins translation. Interacts with host translation initiation complex to allow the translation of viral proteins.[UniProtKB:P27409] Processes the polyprotein. 3CLpro-RdRp is first released by autocleavage, then all other proteins are cleaved. May cleave polyadenylate-binding protein thereby inhibiting cellular translation.[PROSITE-ProRule:PRU00539] Replicates genomic and antigenomic RNA by recognizing replications specific signals. Also transcribes a subgenomic mRNA by initiating RNA synthesis internally on antigenomic RNA. This sgRNA codes for structural proteins. Catalyzes the covalent attachment VPg with viral RNAs (PubMed:11369764).[1] Capsid protein VP60 self assembles to form an icosahedral capsid with a T=3 symmetry, about 35 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry (PubMed:20335264). The capsid encapsulate VP2 proteins and genomic or subgenomic RNA. Attaches virion to target cells by binding histo-blood group antigens, inducing endocytosis of the viral particle (PubMed:18302385). Acidification of the endosome induces conformational change of capsid protein thereby injecting virus genomic RNA into host cytoplasm (By similarity).[2] [3]
References
- ↑ Machín A, Martín Alonso JM, Parra F. Identification of the amino acid residue involved in rabbit hemorrhagic disease virus VPg uridylylation. J Biol Chem. 2001 Jul 27;276(30):27787-92. PMID:11369764 doi:10.1074/jbc.M100707200
- ↑ Rademacher C, Krishna NR, Palcic M, Parra F, Peters T. NMR experiments reveal the molecular basis of receptor recognition by a calicivirus. J Am Chem Soc. 2008 Mar 19;130(11):3669-75. PMID:18302385 doi:10.1021/ja710854r
- ↑ Katpally U, Voss NR, Cavazza T, Taube S, Rubin JR, Young VL, Stuckey J, Ward VK, Virgin HW 4th, Wobus CE, Smith TJ. High-resolution cryo-electron microscopy structures of murine norovirus 1 and rabbit hemorrhagic disease virus reveal marked flexibility in the receptor binding domains. J Virol. 2010 Jun;84(11):5836-41. doi: 10.1128/JVI.00314-10. Epub 2010 Mar 24. PMID:20335264 doi:https://dx.doi.org/10.1128/JVI.00314-10
