VP5 autocleavage is required for efficient infection by in vitro-recoated aquareovirus particles.

Abstract

Grass carp reovirus (GCRV) is a member of the genus Aquareovirus in the family Reoviridae, and contains five core proteins (VP1-VP4 and VP6) and two outer-capsid proteins (VP5 and VP7) in its particle. Previous studies have revealed that the outer-capsid proteins of reovirus are responsible for initiating infection, but the mechanism is poorly understood. Using baculovirus-expressed VP5 and VP7 to recoat purified cores, in vitro assembly of GCRV was achieved in this study. Recoated GCRV (R-GCRV) closely resembled native GCRV (N-GCRV) in particle morphology, protein composition and infectivity. Similar to N-GCRV, the infectivity of R-GCRV could be inhibited by treating cells with the weak base NH4Cl. In addition, recoated particles carrying an Asn→Ala substitution at residue 42 of VP5 (VP5N42A/VP7 R-GCRV) were no longer infectious. These results provide strong evidence that autocleavage of VP5 is critical for aquareovirus to initiate efficient infection.

• Authors: Shicui Yan, Jie Zhang, Hong Guo, Liming Yan, Qingxiu Chen, Fuxian Zhang, Qin Fang
• Journal: The Journal of general virology (J Gen Virol) Vol. 96 Issue Pt 7 Pg. 1795-800 (Jul 2015) ISSN: 1465-2099 [Electronic] England
• PMID: 25742690 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Viral Structural Proteins

Topics

• Animals
• Baculoviridae (genetics)
• Fishes
• Genetic Vectors
• Proteolysis
• Reoviridae (genetics, physiology)
• Viral Structural Proteins (metabolism)
• Virus Assembly
• Virus Internalization
• Virus Replication