IdeS, a secreted proteinase of Streptococcus pyogenes, is bound to a nuclease at the bacterial surface where it inactivates opsonizing IgG antibodies.
DNase
IdeS
IgG
Streptococcus
bacteria
immunity
proteinase
proteolysis
virulence
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
Nov 2023
Nov 2023
Historique:
received:
12
05
2023
revised:
25
09
2023
accepted:
04
10
2023
medline:
27
11
2023
pubmed:
15
10
2023
entrez:
14
10
2023
Statut:
ppublish
Résumé
The important bacterial pathogen Streptococcus pyogenes secretes IdeS (immunoglobulin G-degrading enzyme of S. pyogenes), a proteinase that cleaves human immunoglobulin G (IgG) antibodies in the hinge region resulting in Fc (fragment crystallizable) and F(ab')
Identifiants
pubmed: 37838172
pii: S0021-9258(23)02373-6
doi: 10.1016/j.jbc.2023.105345
pmc: PMC10654033
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Cysteine Endopeptidases
EC 3.4.22.-
Immunoglobulin Fc Fragments
0
Immunoglobulin G
0
Peptide Hydrolases
EC 3.4.-
Mac-1-like protein, Streptococcus
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
105345Informations de copyright
Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.