| Literature DB >> 2452893 |
K Taniguchi1, Y Hoshino, K Nishikawa, K Y Green, W L Maloy, Y Morita, S Urasawa, A Z Kapikian, R M Chanock, M Gorziglia.
Abstract
The neutralization epitopes of human and simian rotavirus protein VP7 were studied by producing six neutralizing monoclonal antibodies (N-MAbs) and using these N-MAbs to select antigenic mutants that resisted neutralization by the N-MAbs used for their selection. Cross-neutralization tests between the N-MAbs and the antibody-selected antigenic mutants identified one cross-reactive and five distinct serotype-specific neutralization epitopes which operationally overlapped one another and constituted a single antigenic site. In addition, the amino acid substitutions in human rotavirus VP7 that are responsible for the antigenic alterations in the mutants selected with anti-VP7 cross-reactive or serotype-specific N-MAbs were identified. All the amino acid substitutions in the antigenic mutants occurred in one of two variable regions: amino acids 87 to 101 and 208 to 221.Entities:
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Year: 1988 PMID: 2452893 PMCID: PMC253268
Source DB: PubMed Journal: J Virol ISSN: 0022-538X Impact factor: 5.103