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IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G.

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Author

Summary, in English

Recent work from several laboratories has demonstrated that proteolytic mechanisms significantly contribute to the molecular interplay between Streptococcus pyogenes, an important human pathogen, and its host. Here we describe the identification, purification and characterization of a novel extracellular cysteine proteinase produced by S.pyogenes. This enzyme, designated IdeS for Immunoglobulin G-degrading enzyme of S.pyogenes, is distinct from the well-characterized streptococcal cysteine proteinase, SpeB, and cleaves human IgG in the hinge region with a high degree of specificity. Thus, other human proteins, including immunoglobulins M, A, D and E, are not degraded by IdeS. The enzyme efficiently cleaves IgG antibodies bound to streptococcal surface structures, thereby inhibiting the killing of S.pyogenes by phagocytic cells. This and additional observations on the distribution and expression of the ideS gene indicate that IdeS represents a novel and significant bacterial virulence determinant, and a potential therapeutic target.

Publishing year

2002

Language

English

Pages

1607-1615

Publication/Series

EMBO Journal

Volume

21

Issue

7

Document type

Journal article

Publisher

Oxford University Press

Topic

  • Biochemistry and Molecular Biology

Keywords

  • Cell Line
  • Cells
  • Cultured
  • Cysteine Endopeptidases : classification
  • Cysteine Endopeptidases : immunology
  • Cysteine Endopeptidases : isolation & purification
  • Cysteine Endopeptidases : metabolism
  • Gene Expression
  • Genes
  • Bacterial
  • Immunoglobulin G : immunology
  • Human
  • Immunoglobulin G : metabolism
  • Immunoglobulins
  • Fc : immunology
  • Fc : metabolism
  • Integrins : classification
  • Integrins : immunology
  • Integrins : isolation & purification
  • Mice
  • Integrins : metabolism
  • Molecular Sequence Data
  • Neutrophils : cytology
  • Phagocytosis : immunology
  • Streptococcus pyogenes : enzymology
  • Substrate Specificity
  • Streptococcus pyogenes : immunology
  • Support
  • Non-U.S. Gov't
  • Bacterial Proteins : metabolism
  • Bacterial : metabolism
  • Antibodies
  • Bacterial : immunology
  • Animal
  • Amino Acid Sequence

Status

Published

ISBN/ISSN/Other

  • ISSN: 1460-2075