Presence of actin binding motif in VgrG-1 toxin of Vibrio cholerae reveals the molecular mechanism of actin cross-linking.
Actin and actin binding motif
Actin cross-linking domain
T6SS
VgrG-1
Journal
International journal of biological macromolecules
ISSN: 1879-0003
Titre abrégé: Int J Biol Macromol
Pays: Netherlands
ID NLM: 7909578
Informations de publication
Date de publication:
15 Jul 2019
15 Jul 2019
Historique:
received:
14
02
2019
revised:
04
04
2019
accepted:
04
04
2019
pubmed:
20
4
2019
medline:
20
11
2019
entrez:
20
4
2019
Statut:
ppublish
Résumé
Type VI secretion systems (T6SS) plays a crucial role in Vibrio cholerae mediated pathogenicity. Tip of T6SS is homologous to gp27/gp5 complex or tail spike of T4 bacteriophage. VgrG-1 of V. cholerae T6SS is unusual among other VgrG because its effector domain is trans-located into the cytosol of eukaryotic cells with an additional actin cross-linking domain (ACD) at its C terminal end. ACD of VgrG-1 (VgrG-1-ACD) causes T6SS dependent host cell cytotoxicity through actin cytoskeleton disruption to prevent bacterial engulfment by macrophages. ACD mediated actin cross-linking promotes survival of the bacteria in the small intestine of humans, along with other virulence factors; establishes successful infection with the onset of diarrhoea in humans. Our studies demonstrated VgrG-1-ACD can bind to actin besides actin cross-linking activity. Computational analysis of ACD revealed the presence of actin binding motif (ABM). Mutations in ABM lead to loss of actin binding in vitro. VgrG-1-ACD having the mutated ABM cannot cross-link actin efficiently in vitro and manifests less actin cytoskeleton disruption when transfected in HeLa cells.
Identifiants
pubmed: 31002899
pii: S0141-8130(19)31153-5
doi: 10.1016/j.ijbiomac.2019.04.026
pii:
doi:
Substances chimiques
Actins
0
Toxins, Biological
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
775-785Informations de copyright
Copyright © 2019 Elsevier B.V. All rights reserved.