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

In English

Författare

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.

Publiceringsår

2002

Språk

Engelska

Sidor

1607-1615

Publikation/Tidskrift/Serie

EMBO Journal

Volym

21

Issue

7

Dokumenttyp

Artikel i tidskrift

Förlag

Oxford University Press

Ämne

  • Biochemistry and Molecular Biology

Nyckelord

  • 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

Aktiv

Published

ISBN/ISSN/Övrigt

  • ISSN: 1460-2075