Alpha hemolysin of E. coli induces hemolysis of human erythrocytes independently of toxin interaction with membrane proteins.
Band 3
GPA(null)/GPB(null)
Glycophorins
RTX toxins
Spectrins
UPEC
Journal
Biochimie
ISSN: 1638-6183
Titre abrégé: Biochimie
Pays: France
ID NLM: 1264604
Informations de publication
Date de publication:
13 Oct 2023
13 Oct 2023
Historique:
received:
05
07
2023
revised:
13
09
2023
accepted:
08
10
2023
pubmed:
12
10
2023
medline:
12
10
2023
entrez:
11
10
2023
Statut:
aheadofprint
Résumé
Alpha hemolysin (HlyA) is a hemolytic and cytotoxic protein secreted by uropathogenic strains of E. coli. The role of glycophorins (GPs) as putative receptors for HlyA binding to red blood cells (RBCs) has been debated. Experiments using anti-GPA/GPB antibodies and a GPA-specific epitope nanobody to block HlyA-GP binding on hRBCs, showed no effect on hemolytic activity. Similarly, the hemolysis induced by HlyA remained unaffected when hRBCs from a GPA
Identifiants
pubmed: 37820991
pii: S0300-9084(23)00271-7
doi: 10.1016/j.biochi.2023.10.008
pii:
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
3-13Informations de copyright
Copyright © 2023 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM). All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.