Enhancement of Aquareovirus Infectivity by Treatment with Proteases: Mechanism of Action

Overview

Journal J Virol

Publisher American Society for Microbiology

Date 1998 Apr 3

PMID 9525667

Citations 7

Authors

T H McPhillips

D Dinan

K Subramanian

S K Samal

Affiliations

Soon will be listed here.

Abstract

The effects of protease digestion on the polypeptide composition and on the infectivity of striped bass virus, an aquareovirus, were examined. Both trypsin and chymotrypsin enhanced the infectivity of the virus. Enhancement of infectivity was correlated with the digestion of the outer capsid protein, VP7. These studies support the assertion that VP7 is the outermost capsid protein and suggest that VP4 and VP5 are exposed on the outer surface of infectious particles. The possible role of VP7 in the variation in virulence observed among aquareovirus isolates is discussed.

Citing Articles

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Corexit 9500 inactivates two enveloped viruses of aquatic animals but enhances the infectivity of a nonenveloped fish virus.

Pham P, Huang Y, Chen C, Bols N Appl Environ Microbiol. 2013; 80(3):1035-41.

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Aquareovirus NS80 recruits viral proteins to its inclusions, and its C-terminal domain is the primary driving force for viral inclusion formation.

Shao L, Guo H, Yan L, Liu H, Fang Q PLoS One. 2013; 8(2):e55334.

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Antibodies against outer-capsid proteins of grass carp reovirus expressed in E. coli are capable of neutralizing viral infectivity.

Shao L, Sun X, Fang Q Virol J. 2011; 8:347.

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Molecular cloning, DNA sequence analysis, and expression of cDNA sequence of RNA genomic segment 6 (S6) that encodes a viral outer capsid protein of threadfin aquareovirus (TFV).

Seng E, Fang Q, Sin Y, Lam T Virus Genes. 2005; 30(2):209-21.

PMID: 15744578 DOI: 10.1007/s11262-004-5629-7.

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