Almost half of the RTX domain is dispensable for complement receptor 3 binding and cell-invasive activity of the Bordetella adenylate cyclase toxin.
Acylation
Adenylate Cyclase Toxin
/ metabolism
Amino Acid Sequence
Animals
Antibodies, Neutralizing
/ metabolism
Bordetella pertussis
/ pathogenicity
CHO Cells
Calcium
/ metabolism
Cricetulus
Epitopes
/ metabolism
Humans
Macrophage-1 Antigen
/ chemistry
Protein Binding
Protein Domains
Protein Folding
Structure-Activity Relationship
THP-1 Cells
Bordetella pertussis
CD11b/CD18 integrin receptor
RTX toxin
adenylate cyclase toxin
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:
07 2021
07 2021
Historique:
received:
29
01
2021
revised:
21
05
2021
accepted:
25
05
2021
pubmed:
30
5
2021
medline:
26
8
2021
entrez:
29
5
2021
Statut:
ppublish
Résumé
The whooping cough agent Bordetella pertussis secretes an adenylate cyclase toxin (CyaA) that through its large carboxy-proximal Repeat-in-ToXin (RTX) domain binds the complement receptor 3 (CR3). The RTX domain consists of five blocks (I-V) of characteristic glycine and aspartate-rich nonapeptides that fold into five Ca
Identifiants
pubmed: 34051233
pii: S0021-9258(21)00631-1
doi: 10.1016/j.jbc.2021.100833
pmc: PMC8214218
pii:
doi:
Substances chimiques
Adenylate Cyclase Toxin
0
Antibodies, Neutralizing
0
Epitopes
0
Macrophage-1 Antigen
0
Calcium
SY7Q814VUP
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
100833Informations de copyright
Copyright © 2021 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.