The zinc-dependent major histocompatibility complex class II binding site of streptococcal pyrogenic exotoxin C is critical for maximal superantigen function and toxic activity

Infect Immun. 2003 Mar;71(3):1548-50. doi: 10.1128/IAI.71.3.1548-1550.2003.

Abstract

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 beta-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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Bacterial Proteins*
  • Binding Sites
  • Exotoxins / chemistry
  • Exotoxins / toxicity*
  • HLA-DR2 Antigen / metabolism*
  • Membrane Proteins*
  • Rabbits
  • Structure-Activity Relationship
  • Superantigens / chemistry
  • Superantigens / toxicity*
  • Zinc / pharmacology*

Substances

  • Bacterial Proteins
  • Exotoxins
  • HLA-DR2 Antigen
  • Membrane Proteins
  • SpeA protein, Streptococcus pyogenes
  • Superantigens
  • erythrogenic toxin
  • Zinc