ArticleChannels (Austin, Tex.)
The binding of cholera toxin to the periplasmic vestibule of the type II secretion channel.
Article in Channels (Austin, Tex.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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27 citing papers in PubMed, 43 citations in OpenAlex.
- TssL2 of T6SS2 is required for mobility, biofilm formation, wrinkly phenotype formation, and virulence of Vibrio parahaemolyticus SH112.Applied microbiology and biotechnology · 2024Article
- Identification ofAntibiotics (Basel, Switzerland) · 2023Article
- Review
- Mechanism of secretion of TcpF by theProceedings of the National Academy of Sciences of the United States of America · 2023Article
- The Cytotoxic Necrotizing Factors (CNFs)-A Family of Rho GTPase-Activating Bacterial Exotoxins.Toxins · 2021Review
- Virulence Regulation and Innate Host Response in the Pathogenicity ofFrontiers in cellular and infection microbiology · 2020Review
- Type IV pili: dynamics, biophysics and functional consequences.Nature reviews. Microbiology · 2019Review
- Cholera Toxin Encapsulated within SeveralToxins · 2019Article
- Architecture, Function, and Substrates of the Type II Secretion System.EcoSal Plus · 2019Review
- Direct interactions between the secreted effector and the T2SS components GspL and GspM reveal a new effector-sensing step during type 2 secretion.The Journal of biological chemistry · 2018Article
- Structure and Membrane Topography of the Vibrio-Type Secretin Complex from the Type 2 Secretion System of Enteropathogenic Escherichia coli.Journal of bacteriology · 2018Article
- Crystal Structure of the Minor Pilin CofB, the Initiator of CFA/III Pilus Assembly in Enterotoxigenic Escherichia coli.The Journal of biological chemistry · 2015Article
- Article
- A dodecameric ring-like structure of the N0 domain of the type II secretin from enterotoxigenic Escherichia coli.Journal of structural biology · 2013Article
- Secretion of TcpF by the Vibrio cholerae toxin-coregulated pilus biogenesis apparatus requires an N-terminal determinant.Journal of bacteriology · 2013Article
- New insights into the assembly of bacterial secretins: structural studies of the periplasmic domain of XcpQ from Pseudomonas aeruginosa.The Journal of biological chemistry · 2013Article
- Dynamic interplay between the periplasmic and transmembrane domains of GspL and GspM in the type II secretion system.PloS one · 2013Article
- Function-related positioning of the type II secretion ATPase of Xanthomonas campestris pv. campestris.PloS one · 2013Article
- Type IV pilin proteins: versatile molecular modules.Microbiology and molecular biology reviews : MMBR · 2012Review
- Cysteine scanning mutagenesis and disulfide mapping analysis of arrangement of GspC and GspD protomers within the type 2 secretion system.The Journal of biological chemistry · 2012Article
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7 authors at 3 institutions in 1 country.
Funding
Abstract
The type II secretion system (T2SS) is a large macromolecular complex spanning the inner and outer membranes of many gram-negative bacteria. The T2SS is responsible for the secretion of virulence factors such as cholera toxin (CT) and heat-labile enterotoxin (LT) from Vibrio cholerae and enterotoxigenic Escherichia coli, respectively. CT and LT are closely related AB5 heterohexamers, composed of one A subunit and a B-pentamer. Both CT and LT are translocated, as folded protein complexes, from the periplasm across the outer membrane through the type II secretion channel, the secretin GspD. We recently published the 19 Å structure of the V. cholerae secretin (VcGspD) in its closed state and showed by SPR measurements that the periplasmic domain of GspD interacts with the B-pentamer complex. Here we extend these studies by characterizing the binding of the cholera toxin B-pentamer to VcGspD using electron microscopy of negatively stained preparations. Our studies indicate that the pentamer is captured within the large periplasmic vestibule of VcGspD. These new results agree well with our previously published studies and are in accord with a piston-driven type II secretion mechanism.
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