ArticleJournal of bacteriology1998
Endochitinase is transported to the extracellular milieu by the eps-encoded general secretory pathway of Vibrio cholerae.
Article in Journal of bacteriology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
35 citing papers in PubMed, 83 citations in OpenAlex.
- Genomic adaptations of Vibrio campbellii to thermal and salinity stress: insights into marine pathogen resilience in a changing ocean.BMC genomics · 2025Article
- ChiVariARIBA: a modular, editable workflow and database for characterising chitin gene variation inMicrobial genomics · 2025Article
- The zoonotic pathogen Wohlfahrtiimonas chitiniclastica - current findings from a clinical and genomic perspective.BMC microbiology · 2024Review
- Interaction Networks Are Driven by Community-Responsive Phenotypes in a Chitin-Degrading Consortium of Soil Microbes.mSystems · 2022Article
- Comparative Genomic Analysis of the Human PathogenFrontiers in cellular and infection microbiology · 2022Article
- Article
- Suppressor Mutations in Type II Secretion Mutants of Vibrio cholerae: Inactivation of the VesC Protease.mSphere · 2020Article
- Chitinase Expression in Listeria monocytogenes Is Influenced byApplied and environmental microbiology · 2017Article
- Super-Resolution Imaging of Protein Secretion Systems and the Cell Surface of Gram-Negative Bacteria.Frontiers in cellular and infection microbiology · 2017Review
- Zinc coordination is essential for the function and activity of the type II secretion ATPase EpsE.MicrobiologyOpen · 2016Article
- Survival and proliferation of the lysogenic bacteriophage CTXΦ in Vibrio cholerae.Virologica Sinica · 2015Review
- Article
- Txc, a new type II secretion system of Pseudomonas aeruginosa strain PA7, is regulated by the TtsS/TtsR two-component system and directs specific secretion of the CbpE chitin-binding protein.Journal of bacteriology · 2014Article
- Functional and structural characterization of Vibrio cholerae extracellular serine protease B, VesB.The Journal of biological chemistry · 2014Article
- Microbiota from Litopenaeus vannamei: digestive tract microbial community of Pacific white shrimp (Litopenaeus vannamei).SpringerPlus · 2014Article
- Proteomic analysis of the Vibrio cholerae type II secretome reveals new proteins, including three related serine proteases.The Journal of biological chemistry · 2011Article
- Levels of the secreted Vibrio cholerae attachment factor GbpA are modulated by quorum-sensing-induced proteolysis.Journal of bacteriology · 2009Article
- Docking and assembly of the type II secretion complex of Vibrio cholerae.Journal of bacteriology · 2009Article
- Xylella fastidiosa afimbrial adhesins mediate cell transmission to plants by leafhopper vectors.Applied and environmental microbiology · 2009Article
- Legionella pneumophila type II secretome reveals unique exoproteins and a chitinase that promotes bacterial persistence in the lung.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The chiA gene of Vibrio cholerae encodes a polypeptide which degrades chitin, a homopolymer of N-acetylglucosamine (GlcNAc) found in cell walls of fungi and in the integuments of insects and crustaceans. chiA has a coding capacity corresponding to a polypeptide of 846 amino acids having a predicted molecular mass of 88.7 kDa. A 52-bp region with promoter activity was found immediately upstream of the chiA open reading frame. Insertional inactivation of the chromosomal copy of the gene confirmed that expression of chitinase activity by V. cholerae required chiA. Fluorescent analogues were used to demonstrate that the enzymatic activity of ChiA was specific for beta,1-4 glycosidic bonds located between GlcNAc monomers in chitin. Antibodies against ChiA were obtained by immunization of a rabbit with a MalE-ChiA hybrid protein. Polypeptides with antigenic similarity to ChiA were expressed by classical and El Tor biotypes of V. cholerae and by the closely related bacterium Aeromonas hydrophila. Immunoblotting experiments using the wild-type strain 569B and the secretion mutant M14 confirmed that ChiA is an extracellular protein which is secreted by the eps system. The eps system is also responsible for secreting cholera toxin, an oligomeric protein with no amino acid homology to ChiA. These results indicate that ChiA and cholera toxin have functionally similar extracellular transport signals that are essential for eps-dependent secretion.
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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.