HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Reavy, B. Articles by Moore, N. F. Search for Related Content PubMed Articles by Reavy, B. Articles by Moore, N. F. Agricola Articles by Reavy, B. Articles by Moore, N. F.

An Inhibitor-resistant Protease Specified by an Insect Picornavirus, and the Role of Cellular Proteases in the Rapid Processing of Capsid Protein Precursors

B. Reavy

NERC Institute of Virology, Mansfield Road, Oxford OX1 3SR, U.K.

Processing of cricket paralysis virus capsid protein precursors in vitro was resistant to the effects of a number of protease inhibitors. Leupeptin was effective in preventing cleavage of capsid protein precursors, suggesting that the virus-specified protease may be a serine protease. Virus capsid proteins were produced more rapidly in vitro when rabbit reticulocyte lysate was supplemented with an extract of Drosophila melanogaster cells. This suggests that cellular proteases may be involved in rapid processing of high molecular weight capsid protein precursors.

Keywords: cricket paralysis, in vitro translation, Drosophila proteases

Present address: Genetics Department, Animal Virus Research Institute, Pirbright, Woking, Surrey GU24 0NF, U.K.

Received 25 February 1983; accepted 17 May 1983.