Misplaced Pages

NSP5 (rotavirus)

Article snapshot taken from Wikipedia with creative commons attribution-sharealike license. Give it a read and then ask your questions in the chat. We can research this topic together.
(Redirected from NSP5(Rotavirus)) Protein family
NSP5 (rotavirus)
Identifiers
SymbolRota_NS26
PfamPF01525
InterProIPR002512
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

NSP5 (nonstructural protein 5) encoded by genome segment 11 of group A rotaviruses. In virus-infected cells NSP5 accumulates in the viroplasms. NSP5 has been shown to be autophosphorylated. Interaction of NSP5 with NSP2 was also demonstrated. In rotavirus-infected cells, the non-structural proteins NSP5 and NSP2 localize in complexes called viroplasms, where replication and assembly occur and they can drive the formation of viroplasm-like structures in the absence of other rotaviral proteins and rotavirus replication.

There is no atomic-resolution structure of NSP5 determined as of June 2019. However, the low resolution three-dimensional structure of the NSP2-NSP5 assembly has been observed by cryo-EM. NSP5 occupies the same site as RNA when binding to NSP2. The EM data from this 2006 study has not been published.

References

  1. Afrikanova I, Miozzo MC, Giambiagi S, Burrone O (September 1996). "Phosphorylation generates different forms of rotavirus NSP5". The Journal of General Virology. 77 ( Pt 9) (9): 2059–65. doi:10.1099/0022-1317-77-9-2059. PMID 8811003.
  2. Afrikanova I, Fabbretti E, Miozzo MC, Burrone OR (November 1998). "Rotavirus NSP5 phosphorylation is up-regulated by interaction with NSP2". The Journal of General Virology. 79 (11): 2679–86. doi:10.1099/0022-1317-79-11-2679. PMID 9820143.
  3. Fabbretti E, Afrikanova I, Vascotto F, Burrone OR (February 1999). "Two non-structural rotavirus proteins, NSP2 and NSP5, form viroplasm-like structures in vivo". The Journal of General Virology. 80 ( Pt 2) (2): 333–9. doi:10.1099/0022-1317-80-2-333. PMID 10073692.
  4. Jiang X, Jayaram H, Kumar M, Ludtke SJ, Estes MK, Prasad BV (November 2006). "Cryoelectron microscopy structures of rotavirus NSP2-NSP5 and NSP2-RNA complexes: implications for genome replication". Journal of Virology. 80 (21): 10829–35. doi:10.1128/JVI.01347-06. PMC 1641785. PMID 16928740.
Viral proteins (early and late)
DNA
linear ds-DNA
(Duplodnaviria,
Varidnaviria)
Herpes simplex
VSPs:
capsid:
VNPs:
Vaccinia
VNPs:
Adenoviridae
VNPs:
circular ds-DNA
(Duplodnaviria,
Varidnaviria?)
Epstein–Barr
VSPs:
VNPs:
ncRNA:
Baculoviridae
VNPs:
other
(Riboviria,
Monodnaviria)
Polyomaviridae
(SV40, MPyV, MCPyV, HaPyV)
(non-enveloped circular ds-DNA)
VSPs:
capsid:
VNPs:
oncoprotein:
Hepatitis B
(circular partially ds-DNA)
VSPs:
  • HBsAg
  • HBcAg
  • VNPs:
    RNA
    ds-RNA
    (Riboviria)
    Rotavirus
    (Duplornaviricota)
    VNPs:
    Rhinov., Polio, Hep A,
    etc. (Pisuviricota)
    VNPs:
    ss-RNA
    positive-sense
    (Riboviria)
    Hepatitis C
    (Kitrinoviricota)
    VSPs:
    VNPs:
    SARS-CoV-2
    (Pisuviricota)
    VSPs:
    VNPs:
    ss-RNA
    negative-sense
    (Negarnaviricota)
    Influenza virus
    VSPs:
    capsid:
    glycoprotein:
    VNPs:
    Parainfluenza
    VSPs:
    glycoprotein:
    Mumps
    VSPs:
    glycoprotein:
    Measles
    VSPs:
    glycoprotein:
    RSV
    VSPs:
    glycoprotein:
    Zaire ebolavirus
    VSPs:
    capsid:
    Indiana vesiculovirus
    VSPs:
    capsid:
    RT
    Structure and genome of HIV
    VSPs:
    VRAPs:
    Multiple
    Fusion protein
    oncoprotein:
  • Gag-onc fusion protein
  • Stub icon

    This molecular or cell biology article is a stub. You can help Misplaced Pages by expanding it.

    Stub icon

    This cell biology article is a stub. You can help Misplaced Pages by expanding it.

    Stub icon

    This enzyme-related article is a stub. You can help Misplaced Pages by expanding it.

    Categories: