ArticleInfection and immunity2012
YghG (GspSβ) is a novel pilot protein required for localization of the GspSβ type II secretion system secretin of enterotoxigenic 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 29 papers.
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Who cites it
29 citing papers in PubMed, 46 citations in OpenAlex.
- Characterization of Glycosylation-Specific Systemic and Mucosal IgA Antibody Responses toFrontiers in immunology · 2021Trial
- Four New Sequence Types and Molecular Characteristics of Multidrug-ResistantAntibiotics (Basel, Switzerland) · 2024Article
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- Membrane translocation process revealed by in situ structures of type II secretion system secretins.Nature communications · 2023Article
- Genomic diversity of non-diarrheagenic fecal Escherichia coli from children in sub-Saharan Africa and south Asia and their relatedness to diarrheagenic E. coli.Nature communications · 2023Article
- Phylogenetic relationship and virulence composition ofFrontiers in microbiology · 2023Article
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- Escherichia marmotae-a Human Pathogen Easily Misidentified as Escherichia coli.Microbiology spectrum · 2022Article
- Functional Analysis of Hypothetical Proteins ofBioinformatics and biology insights · 2022Article
- Porcine Enterotoxigenic Escherichia coli Strains Differ in Their Capacity To Secrete Enterotoxins through Varying YghG Levels.Applied and environmental microbiology · 2020Article
- Human Mucosal IgA Immune Responses against EnterotoxigenicPathogens (Basel, Switzerland) · 2020Review
- Bacterial secretins: Mechanisms of assembly and membrane targeting.Protein science : a publication of the Protein Society · 2020Review
- Structure and assembly of pilotin-dependent and -independent secretins of the type II secretion system.PLoS pathogens · 2019Article
- Architecture, Function, and Substrates of the Type II Secretion System.EcoSal Plus · 2019Review
- SslE (YghJ), a Cell-Associated and Secreted Lipoprotein of Neonatal Septicemic Escherichia coli, Induces Toll-Like Receptor 2-Dependent Macrophage Activation and Proinflammation through NF-κB and MAP Kinase Signaling.Infection and immunity · 2018Article
- Structural insight into the assembly of the type II secretion system pilotin-secretin complex from enterotoxigenic Escherichia coli.Nature microbiology · 2018Article
- M60-like metalloprotease domain of the Escherichia coli YghJ protein forms amyloid fibrils.PloS one · 2018Article
- Genomic and transcriptomic landscape of Escherichia coli BL21(DE3).Nucleic acids research · 2017Article
- Expanding Role of Type II Secretion in Bacterial Pathogenesis and Beyond.Infection and immunity · 2017Review
- Electron Acceptors Induce Secretion of Enterotoxigenic Escherichia coli Heat-Labile Enterotoxin under Anaerobic Conditions through Promotion of GspD Assembly.Infection and immunity · 2016Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The enterotoxigenic Escherichia coli (ETEC) pathotype, characterized by the prototypical strain H10407, is a leading cause of morbidity and mortality in the developing world. A major virulence factor of ETEC is the type II secretion system (T2SS) responsible for secretion of the diarrheagenic heat-labile enterotoxin (LT). In this study, we have characterized the two type II secretion systems, designated alpha (T2SS(α)) and beta (T2SS(β)), encoded in the H10407 genome and describe the prevalence of both systems in other E. coli pathotypes. Under laboratory conditions, the T2SS(β) is assembled and functional in the secretion of LT into culture supernatant, whereas the T2SS(α) is not. Insertional inactivation of the three genes located upstream of gspC(β) (yghJ, pppA, and yghG) in the atypical T2SS(β) operon revealed that YghJ is not required for assembly of the GspD(β) secretin or secretion of LT, that PppA is likely the prepilin peptidase required for the function of T2SS(β), and that YghG is required for assembly of the GspD(β) secretin and thus function of the T2SS(β). Mutational and physiological analysis further demonstrated that YghG (redesignated GspS(β)) is a novel outer membrane pilotin protein that is integral for assembly of the T2SS(β) by localizing GspD(β) to the outer membrane, whereupon GspD(β) forms the macromolecular secretin multimer through which T2SS(β) substrates are translocated.
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