ArticleJournal of bacteriology2013
EscE and EscG are cochaperones for the type III needle protein EscF of enteropathogenic Escherichia coli.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 19 citations in OpenAlex.
- Type III secretion system chaperones: a helping hand for secretion.Microbiology (Reading, England) · 2026Review
- Engineering non-pathogenic bacteria for auto-transporter-driven secretion of functional interferon.Gut microbes · 2025Article
- A-to-I mRNA editing in bacteria can affect protein sequence, disulfide bond formation, and function.Nucleic acids research · 2025Article
- Article
- Type III secretion by Yersinia pseudotuberculosis is reliant upon an authentic N-terminal YscX secretor domain.Molecular microbiology · 2022Article
- Molecular Targets and Strategies for Inhibition of the Bacterial Type III Secretion System (T3SS); Inhibitors Directly Binding to T3SS Components.Biomolecules · 2021Review
- Transposon-insertion sequencing screens unveil requirements for EHEC growth and intestinal colonization.PLoS pathogens · 2019Article
- Chaperone-mediated secretion switching from early to middle substrates in the type III secretion system encoded byThe Journal of biological chemistry · 2019Article
- Structural and Functional Characterization of the Type Three Secretion System (T3SS) Needle ofFrontiers in microbiology · 2019Article
- FliS/flagellin/FliW heterotrimer couples type III secretion and flagellin homeostasis.Scientific reports · 2018Article
- The pathogenicity factor HrpF interacts with HrpA and HrpG to modulate type III secretion system (T3SS) function and t3ss expression in Pseudomonas syringae pv. averrhoi.Molecular plant pathology · 2016Article
- Type Three Secretion System in Attaching and Effacing Pathogens.Frontiers in cellular and infection microbiology · 2016Review
- Structural analysis of SepL, an enteropathogenic Escherichia coli type III secretion-system gatekeeper protein.Acta crystallographica. Section F, Structural biology communications · 2015Article
- The absence of protein Y4yS affects negatively the abundance of T3SS Mesorhizobium loti secretin, RhcC2, in bacterial membranes.Frontiers in plant science · 2015Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Type III secretion systems (T3SSs) are central virulence mechanisms used by a variety of Gram-negative bacteria to inject effector proteins into host cells. The needle polymer is an essential part of the T3SS that provides the effector proteins a continuous channel into the host cytoplasm. It has been shown for a few T3SSs that two chaperones stabilize the needle protein within the bacterial cytosol to prevent its premature polymerization. In this study, we characterized the chaperones of the enteropathogenic Escherichia coli (EPEC) needle protein EscF. We found that Orf2 and Orf29, two poorly characterized proteins encoded within the EPEC locus of enterocyte effacement (LEE), function as the needle protein cochaperones. Our finding demonstrated that both Orf2 and Orf29 are essential for type III secretion (T3S). In addition, we found that Orf2 and Orf29 associate with the bacterial membrane and form a complex with EscF. Orf2 and Orf29 were also shown to disrupt the polymerization of EscF in vitro. Prediction of the tertiary structures of Orf2 and Orf29 showed high structural homology to chaperones of other T3SS needle proteins. Overall, our data suggest that Orf2 and Orf29 function as the chaperones of the needle protein, and therefore, they have been renamed EscE and EscG.
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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.