IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G.
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/107324
- author
- von Pawel-Rammingen, Ulrich LU ; Johansson, Björn LU and Björck, Lars LU
- organization
- publishing date
- 2002
- type
- Contribution to journal
- publication status
- published
- subject
- 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
- 2016-04-01 16:32:26
- date last changed
- 2022-03-30 08:30:40
@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}},
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}},
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}},
doi = {{10.1093/emboj/21.7.1607}},
volume = {{21}},
year = {{2002}},
}