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Thomas J. Scriba,2,
Eric L. Brown,3
Rodney E. Phillips,2 and
Andrew K. Sewell4
Department of Biology and Biochemistry, University of Bath, Bath BA2 7AY,1 Nuffield Department of Clinical Medicine, Peter Medawar Building for Pathogen Research, University of Oxford, Oxford OX1 3SY, United Kingdom,2 University of Texas School of Public Health, 1200 Herman Pressler, Houston, Texas 77030,3 Department of Medical Biochemistry and Immunology, Cardiff University School of Medicine, Henry Wellcome Building, Heath Park, Cardiff CF14 4XN, United Kingdom4
Received 28 June 2007/ Returned for modification 17 August 2007/ Accepted 25 September 2007
In this study, we report the use of peptide-major histocompatibility complex tetramer technology to study the interactions that occur between Staphylococcus aureus proteins and human leukocytes. We demonstrated that this technology can be used to study the activity of superantigens such as toxic shock syndrome toxin 1 and also found that despite similarities to known proteins (i.e., major histocompatibility complex [MHC] class II molecules and superantigens), the S. aureus Eap protein does not block MHC-T-cell receptor interactions and is not a superantigen. Instead, it has nonspecific cross-linking activity that is dependent upon having at least two of its six 110-amino-acid repeats.
Published ahead of print on 15 October 2007.
These authors contributed equally to this work.
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