5a8f

Structural highlights

Function

POLG_SAFV Forms a complex with host RAN and probably binds to exportins carrying activated MAPK in order to mediate the hyperphosphorylation of host Phe/Gly containing nuclear pore proteins (Nups) resulting in cessation of active nucleocytoplasmic transport (Probable). Proteins with NLS signals fail to import, cellular mRNAs fail to export, and some proteins small enough for diffusion are not retained anymore (efflux) (By similarity). The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity).[UniProtKB:Q66765]^[1] Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.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. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes.^[2] Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.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. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes.^[3] Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.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. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes.^[4] Lies on the inner surface of the capsid shell (PubMed:27279624). 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. After genome has been released, the channel shrinks (By similarity).[UniProtKB:P03300]^[5] VP0 precursor is a component of immature procapsids.[UniProtKB:P08617] Involved in host translation shutoff by inhibiting cap-dependent mRNA translation (By similarity). Nuclear localization is required for this function (By similarity). The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity). Inhibits the phosphorylation of the leader protein (PubMed:25210192).[UniProtKB:Q66765]^[6] Affects membrane integrity and causes an increase in membrane permeability. Associates with and induces structural rearrangements of intracellular membranes (By similarity). It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).[UniProtKB:P03305][UniProtKB:P08545] Serves as membrane anchor via its hydrophobic domain. Forms a primer, VPg-pU, which is utilized by the polymerase for the initiation of RNA chains.[UniProtKB:P03304] Cysteine protease that generates mature viral proteins from the precursor polyprotein (By similarity). In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate cooperatively bind to the protease. Cleaves host PABP1, this cleavage is important for viral replication (By similarity).[UniProtKB:P03304][UniProtKB:P12296] Replicates the genomic and antigenomic RNAs by recognizing replications specific signals (By similarity). Performs VPg uridylylation (By similarity).[UniProtKB:P12296]

References

1. ↑ Ciomperlik JJ, Basta HA, Palmenberg AC. Three cardiovirus Leader proteins equivalently inhibit four different nucleocytoplasmic trafficking pathways. Virology. 2015 Oct;484:194-202. PMID:26115166 doi:10.1016/j.virol.2015.06.004
2. ↑ Mullapudi E, Novacek J, Palkova L, Kulich P, Lindberg AM, van Kuppeveld FJ, Plevka P. Structure and genome release mechanism of human cardiovirus Saffold virus-3. J Virol. 2016 Jun 8. pii: JVI.00746-16. PMID:27279624 doi:http://dx.doi.org/10.1128/JVI.00746-16
3. ↑ Mullapudi E, Novacek J, Palkova L, Kulich P, Lindberg AM, van Kuppeveld FJ, Plevka P. Structure and genome release mechanism of human cardiovirus Saffold virus-3. J Virol. 2016 Jun 8. pii: JVI.00746-16. PMID:27279624 doi:http://dx.doi.org/10.1128/JVI.00746-16
4. ↑ Mullapudi E, Novacek J, Palkova L, Kulich P, Lindberg AM, van Kuppeveld FJ, Plevka P. Structure and genome release mechanism of human cardiovirus Saffold virus-3. J Virol. 2016 Jun 8. pii: JVI.00746-16. PMID:27279624 doi:http://dx.doi.org/10.1128/JVI.00746-16
5. ↑ Mullapudi E, Novacek J, Palkova L, Kulich P, Lindberg AM, van Kuppeveld FJ, Plevka P. Structure and genome release mechanism of human cardiovirus Saffold virus-3. J Virol. 2016 Jun 8. pii: JVI.00746-16. PMID:27279624 doi:http://dx.doi.org/10.1128/JVI.00746-16
6. ↑ Petty RV, Basta HA, Bacot-Davis VR, Brown BA, Palmenberg AC. Binding interactions between the encephalomyocarditis virus leader and protein 2A. J Virol. 2014 Nov;88(22):13503-9. PMID:25210192 doi:10.1128/JVI.02148-14
7. ↑ Mullapudi E, Novacek J, Palkova L, Kulich P, Lindberg AM, van Kuppeveld FJ, Plevka P. Structure and genome release mechanism of human cardiovirus Saffold virus-3. J Virol. 2016 Jun 8. pii: JVI.00746-16. PMID:27279624 doi:http://dx.doi.org/10.1128/JVI.00746-16