Literature DB >> 9878456

Identification of domains involved in superantigenicity of streptococcal pyrogenic exotoxin F (SpeF).

A Eriksson1, S E Holm, M Norgren.   

Abstract

A series of 11 synthetic peptides of 30 amino acids, each with 10 amino acids overlap which spanned the entire sequence of streptococcal pyrogenic exotoxin F (SpeF), were employed in proliferation studies on human peripheral blood mononuclear cells (PBMCs). Regions 41-70, 141-170 and 181-210 were identified as important for SpeF-induced lymphocyte activation. Secondary structure predictions of these peptides showed similarities to regions in other superantigens known to be important for T cell mitogenicity. Furthermore, antisera specific to peptides covering amino acids 1-70 and 181-228 were able to inhibit SpeF-induced mitogenicity by 25% when pre-incubated with SpeF prior to PBMC activation. Copyright 1998 Academic Press

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Year:  1998        PMID: 9878456     DOI: 10.1006/mpat.1998.0234

Source DB:  PubMed          Journal:  Microb Pathog        ISSN: 0882-4010            Impact factor:   3.738


  3 in total

1.  Inhibition of bacterial superantigens by peptides and antibodies.

Authors:  K Visvanathan; A Charles; J Bannan; P Pugach; K Kashfi; J B Zabriskie
Journal:  Infect Immun       Date:  2001-02       Impact factor: 3.441

2.  Streptococcal DNase B is immunologically identical to superantigen SpeF but involves separate domains.

Authors:  A Eriksson; B Eriksson; S E Holm; M Norgren
Journal:  Clin Diagn Lab Immunol       Date:  1999-01

3.  Cleavage of antigen-bound immunoglobulin G by SpeB contributes to streptococcal persistence in opsonizing blood.

Authors:  Anna Eriksson; Mari Norgren
Journal:  Infect Immun       Date:  2003-01       Impact factor: 3.441

  3 in total

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