3cji

Structural highlights

Function

POLG_SVV1 Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (PubMed:18940610). Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 325 Angstroms (Probable). VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3 (By similarity). All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (By similarity). VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes (PubMed:18940610).[UniProtKB:P12296]^{[1] [2]} Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (PubMed:18940610). Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 270 Angstroms (Probable). VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3 (By similarity). All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (By similarity). VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes (PubMed:18940610).[UniProtKB:P12296]^{[3] [4]} Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (Probable). Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 270 Angstroms (PubMed:18420805). VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (By similarity). VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes (By similarity).[UniProtKB:P12296]^[5] Lies on the inner surface of the capsid shell (PubMed:18940610). After binding to the host receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP4 is released, capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm (By similarity). After genome has been released, the channel shrinks (By similarity).[UniProtKB:P12296]^[6] VP0 precursor is a component of immature procapsids.[UniProtKB:P08617] Mediates self-processing of the polyprotein by a translational effect termed 'ribosome skipping'. Mechanistically, 2A-mediated cleavage occurs between the C-terminal glycine and the proline of the downstream protein 2B.[UniProtKB:P03305] Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication.[UniProtKB:P03305] Associates with and induces structural rearrangements of intracellular membranes.[UniProtKB:P03305] Covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. Acts as a genome-linked replication primer.[UniProtKB:P03305] Cysteine protease that generates mature viral proteins from the precursor polyprotein (By similarity). Inactivates crucial host adapter molecules in order to suppress antiviral type-I interferon (type-I IFN) and NF-kappaB production to escape host antiviral innate immune responses (PubMed:30408499, PubMed:29427864, PubMed:28566380). Deubiquitinase that acts on both lysine-48- and lysine-63-linked polyubiquitin chains and inhibits the ubiquitination of the ATP-dependent RNA helicase RIGI, TANK-binding kinase 1 (TBK1), and TNF receptor-associated factor 3 (TRAF3), thereby blocking the expression of IFN-beta and IFN stimulated gene 54 (ISG54) (PubMed:30408499). Induces host IRF3 and IRF7 degradation thereby suppressing IRF3- and IRF7-induced type-I IFN production (PubMed:29427864). Also decreases host IRF3 phosphorylation leading to negligible IRF3 activation (PubMed:29427864). Cleaves host MAVS, TRIF and TANK, which are then unable to regulate pattern recognition receptor (PRR)-mediated type-I IFN production (PubMed:28566380).[UniProtKB:P12296]^{[7] [8] [9]} Replicates the genomic and antigenomic RNAs by recognizing replications specific signals (By similarity). Performs VPg uridylylation (By similarity).[UniProtKB:P12296]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

1. ↑ Venkataraman S, Reddy SP, Loo J, Idamakanti N, Hallenbeck PL, Reddy VS. Structure of Seneca Valley Virus-001: an oncolytic picornavirus representing a new genus. Structure. 2008 Oct 8;16(10):1555-61. PMID:18940610 doi:http://dx.doi.org/S0969-2126(08)00303-1
2. ↑ Hales LM, Knowles NJ, Reddy PS, Xu L, Hay C, Hallenbeck PL. Complete genome sequence analysis of Seneca Valley virus-001, a novel oncolytic picornavirus. J Gen Virol. 2008 May;89(Pt 5):1265-1275. PMID:18420805 doi:10.1099/vir.0.83570-0
3. ↑ Venkataraman S, Reddy SP, Loo J, Idamakanti N, Hallenbeck PL, Reddy VS. Structure of Seneca Valley Virus-001: an oncolytic picornavirus representing a new genus. Structure. 2008 Oct 8;16(10):1555-61. PMID:18940610 doi:http://dx.doi.org/S0969-2126(08)00303-1
4. ↑ Hales LM, Knowles NJ, Reddy PS, Xu L, Hay C, Hallenbeck PL. Complete genome sequence analysis of Seneca Valley virus-001, a novel oncolytic picornavirus. J Gen Virol. 2008 May;89(Pt 5):1265-1275. PMID:18420805 doi:10.1099/vir.0.83570-0
5. ↑ Hales LM, Knowles NJ, Reddy PS, Xu L, Hay C, Hallenbeck PL. Complete genome sequence analysis of Seneca Valley virus-001, a novel oncolytic picornavirus. J Gen Virol. 2008 May;89(Pt 5):1265-1275. PMID:18420805 doi:10.1099/vir.0.83570-0
6. ↑ Venkataraman S, Reddy SP, Loo J, Idamakanti N, Hallenbeck PL, Reddy VS. Structure of Seneca Valley Virus-001: an oncolytic picornavirus representing a new genus. Structure. 2008 Oct 8;16(10):1555-61. PMID:18940610 doi:http://dx.doi.org/S0969-2126(08)00303-1
7. ↑ Qian S, Fan W, Liu T, Wu M, Zhang H, Cui X, Zhou Y, Hu J, Wei S, Chen H, Li X, Qian P. Seneca Valley Virus Suppresses Host Type I Interferon Production by Targeting Adaptor Proteins MAVS, TRIF, and TANK for Cleavage. J Virol. 2017 Jul 27;91(16):e00823-17. PMID:28566380 doi:10.1128/JVI.00823-17
8. ↑ Xue Q, Liu H, Zhu Z, Yang F, Ma L, Cai X, Xue Q, Zheng H. Seneca Valley Virus 3C(pro) abrogates the IRF3 response by degrading IRF3 and IRF7. Virology. 2018 May;518:1-7. PMID:29427864 doi:10.1016/j.virol.2018.01.028
9. ↑ Xue Q, Liu H, Zhu Z, Yang F, Xue Q, Cai X, Liu X, Zheng H. Seneca Valley Virus 3C protease negatively regulates the type I interferon pathway by acting as a viral deubiquitinase. Antiviral Res. 2018 Dec;160:183-189. PMID:30408499 doi:10.1016/j.antiviral.2018.10.028
10. ↑ Venkataraman S, Reddy SP, Loo J, Idamakanti N, Hallenbeck PL, Reddy VS. Structure of Seneca Valley Virus-001: an oncolytic picornavirus representing a new genus. Structure. 2008 Oct 8;16(10):1555-61. PMID:18940610 doi:http://dx.doi.org/S0969-2126(08)00303-1