ArticleProceedings of the National Academy of Sciences of the United States of America2001
Directed polar secretion of protease from single cells of Vibrio cholerae via the type II secretion pathway.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
43 citing papers in PubMed, 92 citations in OpenAlex.
- Localization of EccABMC microbiology · 2022Article
- Quantification and Surface Localization of the Hemolysin A Type I Secretion System at the Endogenous Level and under Conditions of Overexpression.Applied and environmental microbiology · 2022Article
- Analysis of HubP-dependent cell pole protein targeting in Vibrio cholerae uncovers novel motility regulators.PLoS genetics · 2022Article
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- Polar delivery ofProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Targeting the Type II Secretion System: Development, Optimization, and Validation of a High-Throughput Screen for the Identification of Small Molecule Inhibitors.Frontiers in cellular and infection microbiology · 2017Article
- Vibrio cholerae hemagglutinin(HA)/protease: An extracellular metalloprotease with multiple pathogenic activities.Toxicon : official journal of the International Society on Toxinology · 2016Review
- Cytotoxic and Inflammatory Responses Induced by Outer Membrane Vesicle-Associated Biologically Active Proteases from Vibrio cholerae.Infection and immunity · 2016Article
- A new suite of tnaA mutants suggests that Escherichia coli tryptophanase is regulated by intracellular sequestration and by occlusion of its active site.BMC microbiology · 2015Article
- The Type II secretion system delivers matrix proteins for biofilm formation by Vibrio cholerae.Journal of bacteriology · 2014Article
- DNA-uptake machinery of naturally competent Vibrio cholerae.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Chemistry with spatial control using particles and streams().RSC advances · 2012Article
- Cationic antimicrobial peptides disrupt the Streptococcus pyogenes ExPortal.Molecular microbiology · 2012Article
- Poles apart: prokaryotic polar organelles and their spatial regulation.Cold Spring Harbor perspectives in biology · 2011Review
- Surface association and the MreB cytoskeleton regulate pilus production, localization and function in Pseudomonas aeruginosa.Molecular microbiology · 2010Article
- Specificity of the type II secretion systems of enterotoxigenic Escherichia coli and Vibrio cholerae for heat-labile enterotoxin and cholera toxin.Journal of bacteriology · 2010Article
- Reactogenicity of live-attenuated Vibrio cholerae vaccines is dependent on flagellins.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- 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
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacteria have long been thought of as little more than sacks of homogeneously distributed enzymes. However, recent cytological studies indicate that bacteria are compartmentalized with proteins involved in processes such as cell division, motility, chemotaxis, and development located at distinct sites. We have used the green fluorescent protein as a reporter to determine the cellular distribution of the extracellular protein secretion (eps)-encoded type II secretion complex responsible for extracellular secretion of cholera toxin and hemagglutinin/protease in Vibrio cholerae. Real-time monitoring of green fluorescent protein fused to EpsM in living cells indicated that, like the single polar flagellum, the Eps complex is located at the old pole after cell division. Eps-dependent protease secretion was also visualized in single cells by fluorescence microscopy by using intramolecularly quenched casein. This analysis demonstrated that active protease secretion is focused at the poles and colocalizes with the site of the polar Eps apparatus. These results suggest that the type II secretion complex is responsible for directed delivery of virulence factors during cholera pathogenesis.
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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.