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

von Pawel-Rammingen, Ulrich LU ; Johansson, Björn LU and Björck, Lars LU (2002) In EMBO Journal 21(7). p.1607-1615
Abstract
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... (More)
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. (Less)
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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
in
EMBO Journal
volume
21
issue
7
pages
1607 - 1615
publisher
Oxford University Press
external identifiers
  • wos:000174992000011
  • pmid:11927545
  • scopus:0037007214
ISSN
1460-2075
DOI
10.1093/emboj/21.7.1607
language
English
LU publication?
yes
id
9b18010c-3004-437e-9f3f-7b89ac6146fe (old id 107324)
alternative location
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11927545&dopt=Abstract
date added to LUP
2007-07-05 10:44:58
date last changed
2017-10-22 04:42:14
@article{9b18010c-3004-437e-9f3f-7b89ac6146fe,
  abstract     = {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.},
  author       = {von Pawel-Rammingen, Ulrich and Johansson, Björn and Björck, Lars},
  issn         = {1460-2075},
  keyword      = {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},
  language     = {eng},
  number       = {7},
  pages        = {1607--1615},
  publisher    = {Oxford University Press},
  series       = {EMBO Journal},
  title        = {IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G.},
  url          = {http://dx.doi.org/10.1093/emboj/21.7.1607},
  volume       = {21},
  year         = {2002},
}