ArticlemBio2013
Flagellar localization of a Helicobacter pylori autotransporter protein.
Article in mBio, 2013. 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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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
27 citing papers in PubMed, 40 citations in OpenAlex.
- Pathogenicity and virulence ofVirulence · 2025Review
- Vacuolating Cytotoxin A (VacA) and Extracellular Vesicles inIranian journal of pathology · 2025Review
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- Characterization of three novelFrontiers in microbiology · 2024Article
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- Polymorphism of virulence genes and biofilm associated with in vitro induced resistance to clarithromycin in Helicobacter pylori.Gut pathogens · 2023Article
- tRNA queuosine modification is involved in biofilm formation and virulence in bacteria.Nucleic acids research · 2023Article
- Control of the flagellation pattern inJournal of bacteriology · 2023Article
- Study ofCancers · 2023Article
- A Tripartite Efflux System Affects Flagellum Stability inInternational journal of molecular sciences · 2022Article
- Phylogenetic Classification and Functional Review of Autotransporters.Frontiers in immunology · 2022Review
- Group BACS infectious diseases · 2021Article
- Genetic requirements and transcriptomics of Helicobacter pylori biofilm formation on abiotic and biotic surfaces.NPJ biofilms and microbiomes · 2020Article
- Phylogenetic Distribution, Ultrastructure, and Function of Bacterial Flagellar Sheaths.Biomolecules · 2020Review
- In silico proteomic and phylogenetic analysis of the outer membrane protein repertoire of gastric Helicobacter species.Scientific reports · 2018Article
- Genetic and Physiological Adaptations of Marine BacteriumFrontiers in microbiology · 2018Article
- Reductive evolution in outer membrane protein biogenesis has not compromised cell surface complexity in Helicobacter pylori.MicrobiologyOpen · 2017Article
- Role of Flagella in the Pathogenesis of Helicobacter pylori.Current microbiology · 2017Review
- CRISPR-like sequences inGut pathogens · 2017Article
- The Helicobacter pylori Autotransporter ImaA Tempers the Bacterium's Interaction with α5β1 Integrin.Infection and immunity · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
unlabelledHelicobacter pylori contains four genes that are predicted to encode proteins secreted by the autotransporter (type V) pathway. One of these, the pore-forming toxin VacA, has been studied in great detail, but thus far there has been very little investigation of three VacA-like proteins. We show here that all three VacA-like proteins are >250 kDa in mass and localized on the surface of H. pylori. The expression of the three vacA-like genes is upregulated during H. pylori colonization of the mouse stomach compared to H. pylori growth in vitro, and a wild-type H. pylori strain outcompeted each of the three corresponding isogenic mutant strains in its ability to colonize the mouse stomach. One of the VacA-like proteins localizes to a sheath that overlies the flagellar filament and bulb, and therefore, we designate it FaaA (flagella-associated autotransporter A). In comparison to a wild-type H. pylori strain, an isogenic faaA mutant strain exhibits decreased motility, decreased flagellar stability, and an increased proportion of flagella in a nonpolar site. The flagellar localization of FaaA differs markedly from the localization of other known autotransporters, and the current results reveal an important role of FaaA in flagellar localization and motility. IMPORTANCE: The pathogenesis of most bacterial infections is dependent on the actions of secreted proteins, and proteins secreted by the autotransporter pathway constitute the largest family of secreted proteins in pathogenic Gram-negative bacteria. In this study, we analyzed three autotransporter proteins (VacA-like proteins) produced by Helicobacter pylori, a Gram-negative bacterium that colonizes the human stomach and contributes to the pathogenesis of gastric cancer and peptic ulcer disease. We demonstrate that these three proteins each enhance the capacity of H. pylori to colonize the stomach. Unexpectedly, one of these proteins (FaaA) is localized to a sheath that overlies H. pylori flagella. The absence of FaaA results in decreased H. pylori motility as well as a reduction in flagellar stability and a change in flagellar localization. The atypical localization of FaaA reflects a specialized function of this autotransporter designed to optimize H. pylori colonization of the gastric niche.
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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.