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Related Experiment Video

Updated: Jul 15, 2026

Personalized Peptide Arrays for Detection of HLA Alloantibodies in Organ Transplantation

Personalized Peptide Arrays for Detection of HLA Alloantibodies in Organ Transplantation

Published on: September 6, 2017

Structural basis for HLA-DQ binding by the streptococcal superantigen SSA.

E Sundberg¹, T S Jardetzky

¹Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208, USA.

Nature Structural Biology

|February 27, 1999

Summary

Streptococcal superantigen (SSA) binds primarily to HLA-DQ molecules, not HLA-DR. This study presents the crystal structure of SSA, clarifying its interaction with HLA-DQ and other MHC isotypes.

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Immunopeptidomics: Isolation of Mouse and Human MHC Class I- and II-Associated Peptides for Mass Spectrometry Analysis

Immunopeptidomics: Isolation of Mouse and Human MHC Class I- and II-Associated Peptides for Mass Spectrometry Analysis

Published on: October 15, 2021

Area of Science:

Immunology
Structural Biology
Microbiology

Background:

Streptococcal superantigen (SSA) is a toxin from Streptococcus pyogenes.
SSA shares sequence identity with staphylococcal enterotoxin B (SEB) but exhibits different binding behavior.
Previous studies suggested SSA and SEB bind distinct sites or subsets of HLA-DR molecules.

Purpose of the Study:

To determine the specific Human Leukocyte Antigen (HLA) molecules bound by SSA.
To elucidate the structural basis of SSA's interaction with HLA molecules.
To understand the differential affinities of bacterial superantigens for MHC isotypes.

Main Methods:

Crystallography to determine the 1.85 Å resolution structure of SSA.
Binding assays to assess SSA's interaction with HLA-DR and HLA-DQ molecules.

Main Results:

SSA predominantly binds to HLA-DQ molecules, contrary to previous assumptions.
The crystal structure of SSA provides atomic-level detail of its conformation.
Differential binding affinities of SSA for HLA-DQ versus HLA-DR were observed.

Conclusions:

SSA's primary interaction is with HLA-DQ, not HLA-DR.
The determined SSA structure offers insights into superantigen-MHC interactions.
This work provides a foundation for understanding superantigen specificity across different MHC isotypes.