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

The Journal of General Virology
Shicui YanQin Fang

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.

References

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Sep 29, 1999·The Journal of General Virology·A A RangelS K Samal
Feb 18, 2006·Science in China. Series C, Life Sciences·Qin FangZ H Zhou
Jul 16, 2008·Journal of Molecular Biology·Lingpeng ChengZ Hong Zhou
Dec 29, 2009·Journal of Molecular Biology·Lingpeng ChengZ Hong Zhou

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