The transmembrane domains of the type III secretion system effector Tir are involved in its secretion and cellular activities.
EPEC
Tir
bacterial virulence
transmembrane domains
type III secretion system
Journal
Frontiers in cellular and infection microbiology
ISSN: 2235-2988
Titre abrégé: Front Cell Infect Microbiol
Pays: Switzerland
ID NLM: 101585359
Informations de publication
Date de publication:
2023
2023
Historique:
received:
20
11
2022
accepted:
01
02
2023
entrez:
3
3
2023
pubmed:
4
3
2023
medline:
7
3
2023
Statut:
epublish
Résumé
Enteropathogenic We created Tir TMD variants with the original or alternative TMD sequence. We found that the C-terminal TMD of Tir (TMD2) is critical for the ability of Tir to escape integration into the bacterial membrane. However, the TMD sequence was not by itself sufficient and its effect was context-dependent. Moreover, the N-terminal TMD of Tir (TMD1) was important for the postsecretion function of Tir at the host cell. Taken together, our study further supports the hypothesis that the TMD sequences of translocated proteins encode information crucial for protein secretion and their postsecretion function.
Identifiants
pubmed: 36864885
doi: 10.3389/fcimb.2023.1103552
pmc: PMC9971567
doi:
Substances chimiques
Type III Secretion Systems
0
Tir protein, E coli
0
Receptors, Cell Surface
0
Escherichia coli Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1103552Informations de copyright
Copyright © 2023 Braverman, Gershberg and Sal-Man.
Déclaration de conflit d'intérêts
The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.
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