Structural highlights
Function
[VP7_ROTRH] Outer capsid protein involved in attachment and possibly entry into the host epithelial cell. It is subsequently lost, together with VP4, following virus entry into the host cell. The outer layer contains 780 copies of VP7, grouped as 260 trimers. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. In integrin-dependent strains, VP7 seems to essentially target the integrin heterodimers ITGAX/ITGB2 and ITGA5/ITGB3 at a postbinding stage, once the initial attachment by VP4 has been achieved (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Rotaviruses, major causes of childhood gastroenteritis, are nonenveloped, icosahedral particles with double-strand RNA genomes. By the use of electron cryomicroscopy and single-particle reconstruction, we have visualized a rotavirus particle comprising the inner capsid coated with the trimeric outer-layer protein, VP7, at a resolution (4 A) comparable with that of X-ray crystallography. We have traced the VP7 polypeptide chain, including parts not seen in its X-ray crystal structure. The 3 well-ordered, 30-residue, N-terminal "arms" of each VP7 trimer grip the underlying trimer of VP6, an inner-capsid protein. Structural differences between free and particle-bound VP7 and between free and VP7-coated inner capsids may regulate mRNA transcription and release. The Ca(2+)-stabilized VP7 intratrimer contact region, which presents important neutralizing epitopes, is unaltered upon capsid binding.
Molecular interactions in rotavirus assembly and uncoating seen by high-resolution cryo-EM.,Chen JZ, Settembre EC, Aoki ST, Zhang X, Bellamy AR, Dormitzer PR, Harrison SC, Grigorieff N Proc Natl Acad Sci U S A. 2009 Jun 30;106(26):10644-8. Epub 2009 Jun 1. PMID:19487668[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chen JZ, Settembre EC, Aoki ST, Zhang X, Bellamy AR, Dormitzer PR, Harrison SC, Grigorieff N. Molecular interactions in rotavirus assembly and uncoating seen by high-resolution cryo-EM. Proc Natl Acad Sci U S A. 2009 Jun 30;106(26):10644-8. Epub 2009 Jun 1. PMID:19487668
