Variable region structure and Staphylococcal protein A binding specificity of a mouse monoclonal IgM anti-laminin-receptor antibody

Variable region structure and Staphylococcal protein A binding specificity of a mouse monoclonal IgM anti-laminin-receptor antibody

Autor Feijo, GCS Google Scholar
Sabbaga, J. Google Scholar
Carneiro, Celia Regina Whitaker Autor UNIFESP Google Scholar
Brigido, M. M. Google Scholar
Instituição Universidade de Brasília (UnB)
Universidade Federal de São Paulo (UNIFESP)
Resumo Staphylococcal protein A is a cell wall-attached polypeptide that acts as a B-lymphocyte superantigen. This activation correlates with specific V-H gene segment usage in the B-cell receptor. B-cell receptor assembled from members of the V(H)3 family in humans, or S107 family in mice, has an intrinsic affinity for protein A. Human V(H)3-derived antibodies bind to domain D of protein A. We have characterized a mouse IgM monoclonal antibody that binds protein A. the sequencing of the variable region suggests an almost germline-encoded V-H derived from S107 family and a V kappa 8-derived V-L. the binding specificity of the monoclonal antibody was tested with various recombinant constructions derived from protein A. We show that, unlike human V(H)3-derived antibody, mouse S107-derived immunoglobulin binds to the B domain of the bacterial superantigen.
Idioma Inglês
Data de publicação 1997-07-01
Publicado em Immunology. Oxford: Blackwell Science Ltd, v. 91, n. 3, p. 479-485, 1997.
ISSN 0019-2805 (Sherpa/Romeo, fator de impacto)
Publicador Blackwell Science Ltd
Extensão 479-485
Fonte http://dx.doi.org/10.1046/j.1365-2567.1997.00280.x
Direito de acesso Acesso aberto Open Access
Tipo Artigo
Web of Science WOS:A1997XJ55200022
Endereço permanente http://repositorio.unifesp.br/handle/11600/25747

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