Further characterization of an alkaline protease activity associated with iridescent virus type 6. Brief report

Abstract

Iridescent virus type 6 infecting Galleria mellonella larvae contained an associated alkaline protease activity which appeared to be tightly bound to the virions and essentially localized on the outside of the viral particle. Under alkaline conditions the virus was degraded by proteolytic cleavage of viral envelope proteins. Proteolytic activity was not present in virus propagated in a permissive insect cell line or when purified from isolated larval fat-bodies instead from whole larvae. The results suggest that the protease associated with Iridescent virus type 6 is of larval origin.