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J Virol, April 1998, p. 3387-3389, Vol. 72, No. 4
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

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

Thomas H. McPhillips,1 David Dinan,1 Kothandaraman Subramanian,2 and Siba K. Samal2,*

Department of Biology, La Salle University, Philadelphia, Pennsylvania 19141,1 and VA-MD Regional College of Veterinary Medicine, University of Maryland, College Park, Maryland 207422

Received 30 July 1997/Accepted 22 December 1997

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.

* Corresponding author. Mailing address: VA-MD Regional College of Veterinary Medicine, University of Maryland, College Park, MD 20742. Phone: (301) 935-6083. Fax: (301) 935-6079. E-mail: ss5{at}umail.umd.edu.




This article has been cited by other articles:

  • Nason, E. L., Samal, S. K., Venkataram Prasad, B. V. (2000). Trypsin-Induced Structural Transformation in Aquareovirus. J. Virol. 74: 6546-6555 [Abstract] [Full Text]  


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