|ZHAO, YUJING - College Of Wooster|
Submitted to: Meeting Proceedings
Publication Type: Abstract Only
Publication Acceptance Date: 11/17/2012
Publication Date: N/A
Interpretive Summary: Maize chlorotic dwarf virus expresses multiple proteins from a single RNA primarily by expressing one large polyprotein which is post-translationally cleaved by a virus-encoded protease. Not all of the sites of cleavage have been identified. This work describes demonstration of cleavage of the N-terminal 78-kDa polyprotein in wheat germ extracts by the virus-encoded 3C-like protease.
Technical Abstract: Maize chlorotic dwarf virus (MCDV) is a member of the genus Waikavirus and encodes a 389 kDa polyprotein from its 11784 nt genomic RNA. Like many polyprotein-encoding viruses, MCDV contains a 3C-like virus protease that is presumably responsible for maturation cleavages of the polyprotein. However, except for the capsid protein (CP) cleavage sites, the sites of cleavage and mature protein complement of MCDV are not currently known. In this work, we examined the cleavage of the N-terminal 78 kDa polyprotein segment (R78) preceding the CP block. Previous work detected proteins of ca. 50, 35, and 25 kDa using R78 antisera. Using an in vitro wheat germ extract, we co-expressed the MCDV R78 protein and the 3C-like protease to examine proteolysis products.