ArticleJournal of microbiology (Seoul, Korea)2014
Interaction between the α-barrel tip of Vibrio vulnificus TolC homologs and AcrA implies the adapter bridging model.
Article in Journal of microbiology (Seoul, Korea), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- Progress of Antimicrobial Mechanisms of Stilbenoids.Pharmaceutics · 2024Review
- Membrane Efflux Pumps of PathogenicMicroorganisms · 2022Review
- TolCV1 Has Multifaceted Roles DuringFrontiers in cellular and infection microbiology · 2021Article
- Recent paradigm shift in the assembly of bacterial tripartite efflux pumps and the type I secretion system.Journal of microbiology (Seoul, Korea) · 2019Review
- ATP-Binding Cassette Transporter VcaM from Vibrio cholerae is Dependent on the Outer Membrane Factor Family for Its Function.International journal of molecular sciences · 2018Article
- Molecular architecture of the bacterial tripartite multidrug efflux pump focusing on the adaptor bridging model.Journal of microbiology (Seoul, Korea) · 2015Review
- Functional analysis of Vibrio vulnificus RND efflux pumps homologous to Vibrio cholerae VexAB and VexCD, and to Escherichia coli AcrAB.Journal of microbiology (Seoul, Korea) · 2015Article
- Functional analysis of TolC homologs in Vibrio vulnificus.Current microbiology · 2014Article
- Interaction mediated by the putative tip regions of MdsA and MdsC in the formation of a Salmonella-specific tripartite efflux pump.PloS one · 2014Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The AcrAB-TolC multidrug efflux pump confers resistance to Escherichia coli against many antibiotics and toxic compounds. The TolC protein is an outer membrane factor that participates in the formation of type I secretion systems. The genome of Vibrio vulnificus encodes two proteins homologous to the E. coli TolC, designated TolCV1 and TolCV2. Here, we show that both TolCV1 and TolCV2 partially complement the E. coli TolC function and physically interact with the membrane fusion protein AcrA, a component of the E. coli AcrAB-TolC efflux pump. Using site-directed mutational analyses and an in vivo cross-linking assay, we demonstrated that the α-barrel tip region of TolC homologs plays a critical role in the formation of functional AcrAB-TolC efflux pumps. Our findings suggest the adapter bridging model as a general assembly mechanism for tripartite drug efflux pumps in Gram-negative bacteria.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.