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Infection and Immunity, March 2003, p. 1548-1550, Vol. 71, No. 3
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.3.1548-1550.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

The Zinc-Dependent Major Histocompatibility Complex Class II Binding Site of Streptococcal Pyrogenic Exotoxin C Is Critical for Maximal Superantigen Function and Toxic Activity

Timothy J. Tripp, John K. McCormick,{dagger} Jennifer M. Webb, and Patrick M. Schlievert*

Department of Microbiology, University of Minnesota Medical School, Minneapolis, Minnesota 55455

Received 28 August 2002/ Returned for modification 10 October 2002/ Accepted 15 November 2002

The cocrystal structure of streptococcal pyrogenic exotoxin C (SPE C) with HLA-DR2a (DRA*0101,DRB5*0101) revealed a zinc-dependent interaction site through residues 167, 201, and 203 on SPE C and residue 81 on the ß-chain of HLA-DR2a (DRA*0101,DRB5*0101). Mutation of these SPE C residues resulted in dramatically reduced biological activities. Thus, the zinc-dependent major histocompatibility complex II binding site is critical for maximal biological function of SPE C.

* Corresponding author. Mailing address: Department of Microbiology, University of Minnesota Medical School, 420 Delaware St., SE, Minneapolis, MN 55455. Phone: (612) 624-9471. Fax: (612) 626-0623. E-mail: pats{at}lenti.med.umn.edu.

Editor: D. L. Burns

{dagger} Present address: The Lawson Health Research Institute, The University of Western Ontario,London, Ontario, Canada.

Infection and Immunity, March 2003, p. 1548-1550, Vol. 71, No. 3
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.3.1548-1550.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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