ArticleInfection and immunity2012
VirK is a periplasmic protein required for efficient secretion of plasmid-encoded toxin from enteroaggregative Escherichia coli.
Article in Infection and immunity, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 30 citations in OpenAlex.
- PhoP-regulated VirK acts as an accessory factor to maintain virulence in polymyxin-resistant Klebsiella pneumoniae.Nucleic acids research · 2026Article
- Genomic insights into multidrug resistance in clinicalFrontiers in microbiology · 2026Article
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- Volatile Metabolome and Transcriptomic Analysis ofMicroorganisms · 2025Article
- The carRS-ompV-virK operon of Vibrio cholerae senses antimicrobial peptides and activates the expression of multiple resistance systems.Scientific reports · 2025Article
- Glyoxylate Shunt and Pyruvate-to-Acetoin Shift Are Specific Stress Responses Induced by Colistin and Ceragenin CSA-13 in Enterobacter hormaechei ST89.Microbiology spectrum · 2023Article
- Comparative Genomic Analysis of a NovelMicroorganisms · 2023Article
- SurA-like and Skp-like Proteins as Important Virulence Determinants of the Gram Negative Bacterial Pathogens.International journal of molecular sciences · 2022Review
- Folding Control in the Path of Type 5 Secretion.Toxins · 2021Review
- Transcriptomic Analysis ofMolecules (Basel, Switzerland) · 2019Article
- Curcumin Blocks Cytotoxicity of Enteroaggregative and EnteropathogenicFrontiers in cellular and infection microbiology · 2019Article
- Article
- The Periplasmic Chaperone Network ofFrontiers in microbiology · 2017Article
- Unravelling potential virulence factor candidates in Xanthomonas citri. subsp. citri by secretome analysis.PeerJ · 2016Article
- A Shigella flexneri virulence plasmid encoded factor controls production of outer membrane vesicles.G3 (Bethesda, Md.) · 2014Article
- Maf-dependent bacterial flagellin glycosylation occurs before chaperone binding and flagellar T3SS export.Molecular microbiology · 2014Article
- Bacterial serine proteases secreted by the autotransporter pathway: classification, specificity, and role in virulence.Cellular and molecular life sciences : CMLS · 2014Review
- Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Despite the autotransporter (AT) moniker, AT secretion appears to involve the function of periplasmic chaperones. We identified four periplasmic proteins that specifically bound to plasmid-encoded toxin (Pet), an AT produced by enteroaggregative Escherichia coli (EAEC). These proteins include the 17-kDa Skp chaperone and the 37-kDa VirK protein. We found that the virK gene is present in different Enterobacteriaceae. VirK bound to misfolded conformations of the Pet passenger domain, but it did not bind to the folded passenger domain or to the β domain of Pet. Assays with an EAECΔvirK mutant and its complemented version showed that, in the absence of VirK, Pet was not secreted but was instead retained in the periplasm as proteolytic fragments. In contrast, Pet was secreted from a Δskp mutant. VirK was not required for the insertion of porin proteins into the outer membrane but assisted with insertion of the Pet β domain into the outer membrane. Loss of VirK function blocked the EAEC-mediated cytotoxic effect against HEp-2 cells. Thus, VirK facilitates the secretion of the AT Pet by maintaining the passenger domain in a conformation that both avoids periplasmic proteolysis and facilitates β-domain insertion into the outer membrane.
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