Disease relevance of cap

• In addition, we show that overproduction of the La capsid polypeptide results in curing of the ScV-La virus, analogous to the production of plants resistant to RNA viruses by virtue of systemic production of viral coat protein [1].
• Expression, assembly, and proteolytic processing of Helminthosporium victoriae 190S totivirus capsid protein in insect cells [2].
• In contrast with members of the family Reoviridae, there are two well-established capsid arrangements for dsRNA fungal viruses, exemplified by the totiviruses L-A and UmV and the chrysovirus PcV [3].
• The icosahedral L-A capsid is formed by 120 copies of Gag and has architecture similar to that seen in the reovirus, blue tongue virus and rice dwarf virus inner protein shells [4].
• Available structural data indicate that their RNA-dependent RNA polymerase (RDRP) is packaged as an integral capsid component, either as a replicative complex at the pentameric vertex (as in reovirus capsids) or as a fusion protein with the coat protein (as in some totivirus) [3].

High impact information on cap

• Virus-like particle capsid proteins encoded by different L double-stranded RNAs of Saccharomyces cerevisiae: their roles in maintenance of M double-stranded killer plasmids [5].
• The yeast virus ScV-L1 has only two genes, cap and pol, which encode the capsid polypeptide and the viral polymerase, respectively [1].
• Most double-stranded RNA viruses have a characteristic capsid consisting of 60 asymmetric coat protein dimers in a so-called T = 2 organization, a feature probably related to their unique life cycle [3].
• Assembly of the Hv190S totivirus capsid is independent of posttranslational modification of the capsid protein [6].
• We also showed that the unmodified p88 is competent for assembly into virus-like particles, indicating that neither phosphorylation nor proteolytic processing of CP is required for capsid assembly [6].

Biological context of cap

• Both have two open reading frames on their single essential RNAs: cap (encoding a capsid polypeptide) and pol (encoding an RNA-dependent RNA polymerase) [7].
• A tiling approach to virus capsid assembly explaining a structural puzzle in virology [8].

References