Monoclonal antibodies defining functional sites on the toxin superantigen staphylococcal enterotoxin B

Abdel R Hamad, Andrew Herman, Philippa Marrack, John W. Kappler

Research output: Contribution to journalArticle

Abstract

Four monoclonal antibodies (mAbs) were produced binding to four nonoverlapping epitopes on the superantigen staphylococcal enterotoxin B (SEB). The mAbs were tested for their ability to detect SEB bound to major histocompatibility complex (MHC) class II, to inhibit SEB binding to MHC class II, to inhibit SEB stimulation of T cell hybridomas, to bind to various nonfunctional mutants of SEB, and to capture and present SEB and its mutants to T cells in the absence of MHC class II. We concluded that two mAbs, B344 and B327, bound to epitopes not required for superantigen function, one mAb, 2B33, blocked an MHC interaction site on SEB, and the fourth mAb, B87, blocked the T cell recognition site on SEB. Moreover, two mAbs (B344 and 2B33) were capable of presenting SEB, although much less efficiently than APC, to CD4- but not CD4+ T cell hybridomas. The results confirm the functional domains on SEB originally defined by mutation and show that MHC class II is not always an essential component of the superantigen ligand.

Original languageEnglish (US)
Pages (from-to)615-621
Number of pages7
JournalJournal of Experimental Medicine
Volume180
Issue number2
DOIs
StatePublished - Aug 1 1994
Externally publishedYes

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Superantigens
Monoclonal Antibodies
Major Histocompatibility Complex
T-Lymphocytes
Hybridomas
Epitopes
staphylococcal enterotoxin B
Ligands

ASJC Scopus subject areas

  • Immunology

Cite this

Monoclonal antibodies defining functional sites on the toxin superantigen staphylococcal enterotoxin B. / Hamad, Abdel R; Herman, Andrew; Marrack, Philippa; Kappler, John W.

In: Journal of Experimental Medicine, Vol. 180, No. 2, 01.08.1994, p. 615-621.

Research output: Contribution to journalArticle

Hamad, Abdel R ; Herman, Andrew ; Marrack, Philippa ; Kappler, John W. / Monoclonal antibodies defining functional sites on the toxin superantigen staphylococcal enterotoxin B. In: Journal of Experimental Medicine. 1994 ; Vol. 180, No. 2. pp. 615-621.
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