A mutation at glycine residue 31 of toxic shock syndrome toxin-1 defines a functional site critical for major histocompatibility complex class II binding and superantigenic activity

The Journal of Infectious Diseases
W W KumA W Chow

Abstract

Random mutagenesis with hydroxylamine was done on toxic shock syndrome toxin-1 (TSST-1) to identify the amino acid residues critical for binding to major histocompatibility complex (MHC) class II molecules of human monocytes. A double mutant with amino acid substitutions of glycine 31-->arginine and aspartic acid 184-->asparagine (G31R.D184N) demonstrated markedly reduced binding to human monocytes and induction of mitogenesis or cytokine secretion. Site-directed mutagenesis revealed that G31R, but not D184N, was at least 4 orders of magnitude less active than wild type recombinant (r) TSST-1 in these biologic activities and did not induce lethal shock in mice. The global structure of G31R remained highly similar to wild type rTSST-1 as evidenced by circular dichroism spectroscopy and binding to anti-TSST-1 polyclonal and monoclonal antibodies. These studies identified TSST-1 residue 31 as critical for binding to MHC class II molecules and for the consequent superantigenic and lethal properties of TSST-1.

Citations

May 4, 2011·The FEBS Journal·Amanda J Brosnahan, Patrick M Schlievert
Nov 30, 2006·Journal of Peptide Science : an Official Publication of the European Peptide Society·Alfonso BavosoAlfonso Tramontano
Jul 23, 2003·The Journal of Immunology : Official Journal of the American Association of Immunologists·John K McCormickPatrick M Schlievert

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