Sequences of the Cell-attachment Sites of Reovirus Type 3 and Its Anti-idiotypic/antireceptor Antibody: Modeling of Their Three-dimensional Structures

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1988 Sep 1

PMID 2457914

Citations 31

Authors

W V Williams

H R Guy

D H Rubin

F Robey

J N Myers

T Kieber-Emmons

D B Weiner

M I Greene

Affiliations

Soon will be listed here.

Abstract

Previous studies have identified an area of amino acid sequence similarity shared by the reovirus type 3 cell-attachment protein sigma 1 and an anti-idiotypic/antireceptor monoclonal antibody (mAb) 87.92.6 that mimics reovirus type 3 by attaching to the same cell-surface receptor. We found that synthetic peptides corresponding to this area of primary sequence similarity bind a neutralizing mAb 9BG5 against which the mAb 87.92.6 is directed. The synthetic peptides compete with mAb 87.92.6 and reovirus type 3 for binding by mAb 9BG5 and displace mAb 87.92.6 and reovirus type 3 from binding to the cell-surface reovirus type 3 receptor. Such observations show that the shared primary structure between reovirus type 3 sigma 1 polypeptide and antireceptor mAb 87.92.6 defines the oligopeptide neutralizing/cell-attachment epitope of reovirus type 3. Computer modeling of this epitope, by use of sequence similarities of known immunoglobulin hypervariable loop conformations, permits an examination of the rudimentary three-dimensional structure of this epitope.

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