ArticleJournal of bacteriology2005
Polarity of enteropathogenic Escherichia coli EspA filament assembly and protein secretion.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 57 citations in OpenAlex.
- Article
- Article
- A polymorphic helix of a Salmonella needle protein relays signals defining distinct steps in type III secretion.PLoS biology · 2019Article
- Assembly, structure, function and regulation of type III secretion systems.Nature reviews. Microbiology · 2017Review
- Article
- Type Three Secretion System in Attaching and Effacing Pathogens.Frontiers in cellular and infection microbiology · 2016Review
- Engineering the Controlled Assembly of Filamentous Injectisomes in E. coli K-12 for Protein Translocation into Mammalian Cells.ACS synthetic biology · 2015Article
- EscO, a functional and structural analog of the flagellar FliJ protein, is a positive regulator of EscN ATPase activity of the enteropathogenic Escherichia coli injectisome.Journal of bacteriology · 2014Article
- Bacterial type III secretion systems: specialized nanomachines for protein delivery into target cells.Annual review of microbiology · 2014Review
- Structure of a type III secretion needle at 7-Å resolution provides insights into its assembly and signaling mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Multi-Functional Characteristics of the Pseudomonas aeruginosa Type III Needle-Tip Protein, PcrV; Comparison to Orthologs in other Gram-negative Bacteria.Frontiers in microbiology · 2011Article
- Microaerobic conditions enhance type III secretion and adherence of enterohaemorrhagic Escherichia coli to polarized human intestinal epithelial cells.Environmental microbiology · 2010Article
- N-terminal type III secretion signal of enteropathogenic Escherichia coli translocator proteins.Journal of bacteriology · 2010Article
- The two-component system QseEF and the membrane protein QseG link adrenergic and stress sensing to bacterial pathogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Secretion of flagellin by the LEE-encoded type III secretion system of enteropathogenic Escherichia coli.BMC microbiology · 2009Article
- Post-transcriptional processing of the LEE4 operon in enterohaemorrhagic Escherichia coli.Molecular microbiology · 2009Article
- Architectures and biogenesis of non-flagellar protein appendages in Gram-negative bacteria.The EMBO journal · 2008Review
- What's the point of the type III secretion system needle?Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Enterohemorrhagic Escherichia coli exploits EspA filaments for attachment to salad leaves.Applied and environmental microbiology · 2008Article
- Identification of amino acid residues within the N-terminal domain of EspA that play a role in EspA filament biogenesis and function.Journal of bacteriology · 2008Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Type III secretion systems (TTSS) are sophisticated macromolecular structures that play an imperative role in bacterial infections and human disease. The TTSS needle complex is conserved among bacterial pathogens and shows broad similarity to the flagellar basal body. However, the TTSS of enteropathogenic and enterohemorrhagic Escherichia coli, two important human enteric pathogens, is unique in that it has an approximately 12-nm-diameter filamentous extension to the needle that is composed of the secreted translocator protein EspA. EspA filaments and flagellar structures have very similar helical symmetry parameters. In this study we investigated EspA filament assembly and the delivery of effector proteins across the bacterial cell wall. We show that EspA filaments are elongated by addition of EspA subunits to the tip of the growing filament. Moreover, EspA filament length is modulated by the availability of intracellular EspA subunits. Finally, we provide direct evidence that EspA filaments are hollow conduits through which effector proteins are delivered to the extremity of the bacterial cell (and subsequently into the host cell).
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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.