A neutralizing epitope of the superantigen SEA has agonist activity on T cells.

Journal Article (Journal Article)

We have previously shown that sequence 121-149 of the staphylococcal enterotoxin superantigen SEA plays an important role in superantigen function. A synthetic peptide of this region, SEA(121-149), blocks SEA binding to class II MHC molecules and induces interleukin-1 and tumor necrosis factor production in monocytes. In this study, we further emphasize the structural and functional significance of this region of SEA by showing that the SEA(121-149) peptide induces T cell proliferation in a manner similar to that of SEA. SEA(121-149) reacted with antibodies produced to SEA, and the SEA(121-149) specific antibodies neutralized SEA mitogenic activity. A tetrameric form of SEA(121-149) showed increased binding to antibodies and enhanced T cell activation, consistent with the greater avidity associated with increased valency. These data suggest that the internal domain of SEA corresponding to residues 121-149 plays an important role in superantigen activity.

Full Text

Duke Authors

Cited Authors

  • Hobeika, AC; Johnson, HM

Published Date

  • June 25, 1996

Published In

Volume / Issue

  • 223 / 3

Start / End Page

  • 565 - 571

PubMed ID

  • 8687436

International Standard Serial Number (ISSN)

  • 0006-291X

Digital Object Identifier (DOI)

  • 10.1006/bbrc.1996.0935


  • eng

Conference Location

  • United States