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Infect. Immun. doi:10.1128/IAI.00875-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

The use of peptide-MHC tetramer technology to study interactions between S. aureus proteins (TSST-1 and Eap) and human cells

Dept. of Biology and Biochemistry, University of Bath, Bath, BA2 7AY, UK; Nuffield Dept. of Clinical Medicine, Peter Medawar Building for Pathogen Research, University of Oxford, Oxford, OX1 3SY, UK; University of Texas School of Public Health, 1200 Herman Pressler, Houston, TX 77030, USA; Dept. of Medical Biochemistry and Immunology, Cardiff University School of Medicine, Henry Wellcome Building, Heath Park, Cardiff, CF14 4XN, UK

^* To whom correspondence should be addressed. Email: ruth.massey{at}zoo.ox.ac.uk.

	Abstract

In this study we report on the use of peptide major-histocompatability complex (pMHC) tetramer technology to study the interactions that occur between S. aureus proteins and human leukocytes. We demonstrate that this technology can be used to study the activity of superantigens such as TSST-1 and also find that despite similarities with known proteins (i.e. MHCII molecules and superantigens), the S. aureus Eap protein does not block MHC:TCR interactions and is not a superantigen. It has instead a non-specific crosslinking activity that is dependent upon having at least two of its six 110 amino acid repeats.

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