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IdeS, a highly specific immunoglobulin G (IgG)-cleaving enzyme from Streptococcus pyogenes, is inhibited by specific IgG antibodies generated during infection

Åkesson, Per LU ; Moritz, L ; Truedsson, M ; Christensson, Bertil LU and von Pawel-Rammingen, Ulrich LU (2006) In Infection and Immunity 74(1). p.497-503
Abstract
IdeS, a recently discovered cysteine proteinase secreted by the important human pathogen Streptococcus pyogenes, interferes with phagocytic killing by specifically cleaving the heavy chain of immunoglobulin G. The fact that the enzyme targets one of the key molecules of the adapted immune response raised the question of whether an antibody response against IdeS could inhibit, i.e., neutralize, enzyme activity. Paired acute- and convalescent-phase serum samples from patients with pharyngotonsillitis (n = 10), bacteremia (n = 7), and erysipelas (n = 4) were analyzed. Antibodies with the ability to neutralize IdeS enzymatic activity were already found in two-thirds of acute-phase sera. However, patients who seroconverted to IdeS, in... (More)
IdeS, a recently discovered cysteine proteinase secreted by the important human pathogen Streptococcus pyogenes, interferes with phagocytic killing by specifically cleaving the heavy chain of immunoglobulin G. The fact that the enzyme targets one of the key molecules of the adapted immune response raised the question of whether an antibody response against IdeS could inhibit, i.e., neutralize, enzyme activity. Paired acute- and convalescent-phase serum samples from patients with pharyngotonsillitis (n = 10), bacteremia (n = 7), and erysipelas (n = 4) were analyzed. Antibodies with the ability to neutralize IdeS enzymatic activity were already found in two-thirds of acute-phase sera. However, patients who seroconverted to IdeS, in particular patients with pharyngotonsillitis and erysipelas, developed specific antibodies during convalescence with an increased capability to efficiently neutralize the enzymatic activity of IdeS. Also, the presence of neutralizing antibodies decreased the ability of IdeS to mediate bacterial survival in human immune blood. In patients with bacteremia, several acute-phase sera contained neutralizing antibodies, but no correlation was found to severity or outcome of invasive infections. Still, the fact that the human immune response targets the enzymatic activity of IdeS supports the view that the enzyme plays an important role during streptococcal infection. (Less)
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; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Infection and Immunity
volume
74
issue
1
pages
497 - 503
publisher
American Society for Microbiology
external identifiers
  • wos:000234276400054
  • pmid:16369006
  • scopus:29644438454
ISSN
1098-5522
DOI
10.1128/IAI.74.1.497-503.2006
language
English
LU publication?
yes
additional info
The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Division of Infection Medicine (SUS) (013008000), Department of Experimental Medical Science (013210000)
id
c6f368e5-37e0-433c-96d9-60f1ae5fcc54 (old id 421585)
date added to LUP
2016-04-01 11:59:20
date last changed
2021-02-17 03:27:14
@article{c6f368e5-37e0-433c-96d9-60f1ae5fcc54,
  abstract     = {IdeS, a recently discovered cysteine proteinase secreted by the important human pathogen Streptococcus pyogenes, interferes with phagocytic killing by specifically cleaving the heavy chain of immunoglobulin G. The fact that the enzyme targets one of the key molecules of the adapted immune response raised the question of whether an antibody response against IdeS could inhibit, i.e., neutralize, enzyme activity. Paired acute- and convalescent-phase serum samples from patients with pharyngotonsillitis (n = 10), bacteremia (n = 7), and erysipelas (n = 4) were analyzed. Antibodies with the ability to neutralize IdeS enzymatic activity were already found in two-thirds of acute-phase sera. However, patients who seroconverted to IdeS, in particular patients with pharyngotonsillitis and erysipelas, developed specific antibodies during convalescence with an increased capability to efficiently neutralize the enzymatic activity of IdeS. Also, the presence of neutralizing antibodies decreased the ability of IdeS to mediate bacterial survival in human immune blood. In patients with bacteremia, several acute-phase sera contained neutralizing antibodies, but no correlation was found to severity or outcome of invasive infections. Still, the fact that the human immune response targets the enzymatic activity of IdeS supports the view that the enzyme plays an important role during streptococcal infection.},
  author       = {Åkesson, Per and Moritz, L and Truedsson, M and Christensson, Bertil and von Pawel-Rammingen, Ulrich},
  issn         = {1098-5522},
  language     = {eng},
  number       = {1},
  pages        = {497--503},
  publisher    = {American Society for Microbiology},
  series       = {Infection and Immunity},
  title        = {IdeS, a highly specific immunoglobulin G (IgG)-cleaving enzyme from Streptococcus pyogenes, is inhibited by specific IgG antibodies generated during infection},
  url          = {http://dx.doi.org/10.1128/IAI.74.1.497-503.2006},
  doi          = {10.1128/IAI.74.1.497-503.2006},
  volume       = {74},
  year         = {2006},
}