ArticlePLoS pathogens2008
HpaC controls substrate specificity of the Xanthomonas type III secretion system.
Article in PLoS pathogens, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- On the role of the sorting platform in hierarchical type III secretion regulation in enteropathogenicJournal of bacteriology · 2025Article
- Recognition of a translocation motif in the regulator HpaA fromFrontiers in plant science · 2022Article
- Article
- A conserved motif promotes HpaB-regulated export of type III effectors from Xanthomonas.Molecular plant pathology · 2018Article
- HpaB-Dependent Secretion of Type III Effectors in the Plant Pathogens Ralstonia solanacearum and Xanthomonas campestris pv. vesicatoria.Scientific reports · 2017Article
- The Predicted Lytic Transglycosylase HpaH from Xanthomonas campestris pv. vesicatoria Associates with the Type III Secretion System and Promotes Effector Protein Translocation.Infection and immunity · 2017Article
- Type III-Dependent Translocation of HrpB2 by a Nonpathogenic hpaABC Mutant of the Plant-Pathogenic Bacterium Xanthomonas campestris pv. vesicatoria.Applied and environmental microbiology · 2016Article
- HrcU and HrpP are pathogenicity factors in the fire blight pathogen Erwinia amylovora required for the type III secretion of DspA/E.BMC microbiology · 2016Article
- Type Three Secretion System in Attaching and Effacing Pathogens.Frontiers in cellular and infection microbiology · 2016Review
- A Salmonella type three secretion effector/chaperone complex adopts a hexameric ring-like structure.Journal of bacteriology · 2015Article
- HpaP modulates type III effector secretion in Ralstonia solanacearum and harbours a substrate specificity switch domain essential for virulence.Molecular plant pathology · 2014Article
- Type III chaperones & Co in bacterial plant pathogens: a set of specialized bodyguards mediating effector delivery.Frontiers in plant science · 2013Review
- The periplasmic HrpB1 protein from Xanthomonas spp. binds to peptidoglycan and to components of the type III secretion system.Applied and environmental microbiology · 2013Article
- Genetically engineered frameshifted YopN-TyeA chimeras influence type III secretion system function in Yersinia pseudotuberculosis.PloS one · 2013Article
- Role of EscP (Orf16) in injectisome biogenesis and regulation of type III protein secretion in enteropathogenic Escherichia coli.Journal of bacteriology · 2012Article
- Protein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant- and animal-pathogenic bacteria.Microbiology and molecular biology reviews : MMBR · 2012Review
- HrcQ provides a docking site for early and late type III secretion substrates from Xanthomonas.PloS one · 2012Article
- Functional characterization of the type III secretion substrate specificity switch protein HpaC from Xanthomonas campestris pv. vesicatoria.Infection and immunity · 2011Article
- Structure-function analysis of the HrpB2-HrcU interaction in the Xanthomonas citri type III secretion system.PloS one · 2011Article
- Secretion of early and late substrates of the type III secretion system from Xanthomonas is controlled by HpaC and the C-terminal domain of HrcU.Molecular microbiology · 2011Article
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6 authors.
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Abstract
The Gram-negative bacterial plant pathogen Xanthomonas campestris pv. vesicatoria employs a type III secretion (T3S) system to inject bacterial effector proteins into the host cell cytoplasm. One essential pathogenicity factor is HrpB2, which is secreted by the T3S system. We show that secretion of HrpB2 is suppressed by HpaC, which was previously identified as a T3S control protein. Since HpaC promotes secretion of translocon and effector proteins but inhibits secretion of HrpB2, HpaC presumably acts as a T3S substrate specificity switch protein. Protein-protein interaction studies revealed that HpaC interacts with HrpB2 and the C-terminal domain of HrcU, a conserved inner membrane component of the T3S system. However, no interaction was observed between HpaC and the full-length HrcU protein. Analysis of HpaC deletion derivatives revealed that the binding site for the C-terminal domain of HrcU is essential for HpaC function. This suggests that HpaC binding to the HrcU C terminus is key for the control of T3S. The C terminus of HrcU also provides a binding site for HrpB2; however, no interaction was observed with other T3S substrates including pilus, translocon and effector proteins. This is in contrast to HrcU homologs from animal pathogenic bacteria suggesting evolution of distinct mechanisms in plant and animal pathogenic bacteria for T3S substrate recognition.
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