Trimerization of the reovirus cell attachment protein (sigma 1) induces conformational changes in sigma 1 necessary for its cell-binding function. Virology 1991 Oct;184(2):758-61
Date
10/01/1991Pubmed ID
1887593DOI
10.1016/0042-6822(91)90447-jScopus ID
2-s2.0-0025955495 (requires institutional sign-in at Scopus site) 19 CitationsAbstract
The implications of reovirus sigma l protein trimerization on its cell-binding function were investigated. Both monomeric and trimeric forms of sigma l were found to be present when full-length type 3 reovirus Sl transcripts prepared in vitro were translated in rabbit reticulocyte lysates. Pulse-chase experiments demonstrated that monomers were precursors of trimers. However, only the trimeric form was capable of binding to cell surface receptors. Protease and antibody recognition analyses revealed significant structural differences between these two sigma l forms at both the N- and C-termini. Our results suggest that trimerization of protein sigma l is accompanied by extensive conformational changes necessary for its cell attachment function.
Author List
Leone G, Duncan R, Lee PWAuthor
Gustavo Leone PhD Sr Associate Dean, Director, Professor in the Pathology department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AnimalsAntibodies, Viral
Antigen-Antibody Complex
Capsid Proteins
In Vitro Techniques
Macromolecular Substances
Mice
Protein Conformation
Receptors, Virus
Recombinant Proteins
Reoviridae
Structure-Activity Relationship
Viral Proteins
