Abstract
Staphylococcal toxic shock syndrome toxin 1 (TSST-1) binds to major histocompatibility complex class II molecules, and the toxin-class II complexes induce proliferation of T cells expressing Vβ2 sequences. To define the residues involved in TSST-1 binding, a set of transfectants expressing 21 HLA-DRα chain mutants were analyzed for their abilities to bind and present TSST-1 and to present an antigenic peptide. Mutations at DRα positions 36 and 39 markedly decreased the ability of the DR7 molecule to bind and present TSST-1 but did not affect the ability to present an antigenic peptide. These data indicate that DRα residues 36 and 39, predicted to be located on an outer loop, are important in the formation of the TSST-1 binding site on DR molecules.
| Original language | English |
|---|---|
| Pages (from-to) | 1779-1784 |
| Number of pages | 6 |
| Journal | Journal of Experimental Medicine |
| Volume | 176 |
| Issue number | 6 |
| Publication status | Published - Dec 1 1992 |
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ASJC Scopus subject areas
- Immunology
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Identification of HLA-DRα chain residues critical for binding of the toxic shock syndrome toxin superantigen. / Panina-Bordignon, Paola; Fu, Xin Ting; Lanzavecchia, Antonio; Karr, Robert W.
In: Journal of Experimental Medicine, Vol. 176, No. 6, 01.12.1992, p. 1779-1784.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Identification of HLA-DRα chain residues critical for binding of the toxic shock syndrome toxin superantigen
AU - Panina-Bordignon, Paola
AU - Fu, Xin Ting
AU - Lanzavecchia, Antonio
AU - Karr, Robert W.
PY - 1992/12/1
Y1 - 1992/12/1
N2 - Staphylococcal toxic shock syndrome toxin 1 (TSST-1) binds to major histocompatibility complex class II molecules, and the toxin-class II complexes induce proliferation of T cells expressing Vβ2 sequences. To define the residues involved in TSST-1 binding, a set of transfectants expressing 21 HLA-DRα chain mutants were analyzed for their abilities to bind and present TSST-1 and to present an antigenic peptide. Mutations at DRα positions 36 and 39 markedly decreased the ability of the DR7 molecule to bind and present TSST-1 but did not affect the ability to present an antigenic peptide. These data indicate that DRα residues 36 and 39, predicted to be located on an outer loop, are important in the formation of the TSST-1 binding site on DR molecules.
AB - Staphylococcal toxic shock syndrome toxin 1 (TSST-1) binds to major histocompatibility complex class II molecules, and the toxin-class II complexes induce proliferation of T cells expressing Vβ2 sequences. To define the residues involved in TSST-1 binding, a set of transfectants expressing 21 HLA-DRα chain mutants were analyzed for their abilities to bind and present TSST-1 and to present an antigenic peptide. Mutations at DRα positions 36 and 39 markedly decreased the ability of the DR7 molecule to bind and present TSST-1 but did not affect the ability to present an antigenic peptide. These data indicate that DRα residues 36 and 39, predicted to be located on an outer loop, are important in the formation of the TSST-1 binding site on DR molecules.
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M3 - Article
VL - 176
SP - 1779
EP - 1784
JO - Journal of Experimental Medicine
JF - Journal of Experimental Medicine
SN - 0022-1007
IS - 6
ER -