ArticleJournal of bacteriology2011
Involvement of the GspAB complex in assembly of the type II secretion system secretin of Aeromonas and Vibrio species.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 41 citations in OpenAlex.
- The PDZ domain of EpsC is required for extracellular secretion of VesB by the Type II secretion system inJournal of bacteriology · 2025Article
- Review
- Article
- Bacterial secretins: Mechanisms of assembly and membrane targeting.Protein science : a publication of the Protein Society · 2020Review
- In vivo structure of the Legionella type II secretion system by electron cryotomography.Nature microbiology · 2019Article
- Diverse effects of nitric oxide reductase NorV on Aeromonas hydrophila virulence-associated traits under aerobic and anaerobic conditions.Veterinary research · 2019Article
- Structure and assembly of pilotin-dependent and -independent secretins of the type II secretion system.PLoS pathogens · 2019Article
- Architecture, Function, and Substrates of the Type II Secretion System.EcoSal Plus · 2019Review
- Expanding Role of Type II Secretion in Bacterial Pathogenesis and Beyond.Infection and immunity · 2017Review
- Alterations in Peptidoglycan Cross-Linking Suppress the Secretin Assembly Defect Caused by Mutation of GspA in the Type II Secretion System.Journal of bacteriology · 2017Article
- Transposons to toxins: the provenance, architecture and diversification of a widespread class of eukaryotic effectors.Nucleic acids research · 2016Article
- Article
- Crystal structure of the pilotin from the enterohemorrhagic Escherichia coli type II secretion system.Journal of structural biology · 2013Article
- Assembly of the type II secretion system such as found in Vibrio cholerae depends on the novel Pilotin AspS.PLoS pathogens · 2013Article
- A Single Amino Acid Substitution Changes the Self-Assembly Status of a Type IV Piliation Secretin.Journal of bacteriology · 2012Article
- YghG (GspSβ) is a novel pilot protein required for localization of the GspSβ type II secretion system secretin of enterotoxigenic Escherichia coli.Infection and immunity · 2012Article
- On the path to uncover the bacterial type II secretion system.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- The type II secretion system: biogenesis, molecular architecture and mechanism.Nature reviews. Microbiology · 2012Review
- Structural insights into the Type II secretion nanomachine.Current opinion in structural biology · 2012Review
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Authors and funding
7 authors at 5 institutions in 2 countries.
Funding
Abstract
The type II secretion system (T2SS) functions as a transport mechanism to translocate proteins from the periplasm to the extracellular environment. The ExeA homologue in Aeromonas hydrophila, GspA(Ah), is an ATPase that interacts with peptidoglycan and forms an inner membrane complex with the ExeB homologue (GspB(Ah)). The complex may be required to generate space in the peptidoglycan mesh that is necessary for the transport and assembly of the megadalton-sized ExeD homologue (GspD(Ah)) secretin multimer in the outer membrane. In this study, the requirement for GspAB in the assembly of the T2SS secretin in Aeromonas and Vibrio species was investigated. We have demonstrated a requirement for GspAB in T2SS assembly in Aeromonas salmonicida, similar to that previously observed in A. hydrophila. In the Vibrionaceae species Vibrio cholerae, Vibrio vulnificus, and Vibrio parahaemolyticus, gspA mutations significantly decreased assembly of the secretin multimer but had minimal effects on the secretion of T2SS substrates. The lack of effect on secretion of the mutant of gspA of V. cholerae (gspA(Vc)) was explained by the finding that native secretin expression greatly exceeds the level needed for efficient secretion in V. cholerae. In cross-complementation experiments, secretin assembly and secretion in an A. hydrophila gspA mutant were partially restored by the expression of GspAB from V. cholerae in trans, further suggesting that GspAB(Vc) performs the same role in Vibrio species as GspAB(Ah) does in the aeromonads. These results indicate that the GspAB complex is functional in the assembly of the secretin in Vibrio species but that a redundancy of GspAB function may exist in this genus.
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