ArticleJournal of bacteriology2005
An amino-terminal secretion signal is required for YplA export by the Ysa, Ysc, and flagellar type III secretion systems of Yersinia enterocolitica biovar 1B.
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 21 papers.
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Who cites it
21 citing papers in PubMed, 31 citations in OpenAlex.
- Selective Inhibition ofPharmaceutics · 2025Article
- Temperature Adaptive Biofilm Formation inAntibiotics (Basel, Switzerland) · 2025Article
- Bacterial Flagellar Filament: A Supramolecular Multifunctional Nanostructure.International journal of molecular sciences · 2021Review
- Computational prediction of secreted proteins in gram-negative bacteria.Computational and structural biotechnology journal · 2021Review
- A quantitative proteomic screen of the Campylobacter jejuni flagellar-dependent secretome.Journal of proteomics · 2017Article
- Type III Secretion in the Melioidosis PathogenFrontiers in cellular and infection microbiology · 2017Review
- Type III secretion systems: the bacterial flagellum and the injectisome.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015Review
- Flagellar biosynthesis exerts temporal regulation of secretion of specific Campylobacter jejuni colonization and virulence determinants.Molecular microbiology · 2014Article
- Comparative analysis of the secretion capability of early and late flagellar type III secretion substrates.Molecular microbiology · 2014Article
- Two residues predominantly dictate functional difference in motility between Shewanella oneidensis flagellins FlaA and FlaB.The Journal of biological chemistry · 2014Article
- 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
- Identification of potential type III secretion proteins via heterologous expression of Vibrio parahaemolyticus DNA.Applied and environmental microbiology · 2012Article
- Vp1659 is a Vibrio parahaemolyticus type III secretion system 1 protein that contributes to translocation of effector proteins needed to induce cytolysis, autophagy, and disruption of actin structure in HeLa cells.Journal of bacteriology · 2010Article
- Application of a short, disordered N-terminal flagellin segment, a fully functional flagellar type III export signal, to expression of secreted proteins.Applied and environmental microbiology · 2010Article
- Inactivation of the fliY gene encoding a flagellar motor switch protein attenuates mobility and virulence of Leptospira interrogans strain Lai.BMC microbiology · 2009Article
- Identification of a Campylobacter jejuni-secreted protein required for maximal invasion of host cells.Molecular microbiology · 2009Article
- YspM, a newly identified Ysa type III secreted protein of Yersinia enterocolitica.Journal of bacteriology · 2008Article
- Involvement of a phospholipase C in the hemolytic activity of a clinical strain of Pseudomonas fluorescens.BMC microbiology · 2008Article
- An inhibitor of gram-negative bacterial virulence protein secretion.Cell host & microbe · 2008Article
- Diminished LcrV secretion attenuates Yersinia pseudotuberculosis virulence.Journal of bacteriology · 2007Article
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
Yersinia enterocolitica biovar 1B maintains three distinct type III secretion (TTS) systems, which independently operate to target proteins to extracellular sites. The Ysa and Ysc systems are prototypical contact-dependent TTS systems that translocate toxic effectors to the cytosols of targeted eukaryotic host cells during infection. The flagellar TTS system is utilized during the assembly of the flagellum and is required for secretion of the virulence-associated phospholipase YplA to the bacterial milieu. When ectopically produced, YplA is also a secretion substrate for the Ysa and Ysc TTS systems. In this study, we define elements that allow YplA recognition and export by the Ysa, Ysc, and flagellar TTS systems. Fusion of various amino-terminal regions of YplA to Escherichia coli alkaline phosphatase (PhoA) lacking its native secretion signal demonstrated that the first 20 amino acids or corresponding mRNA codons of YplA were sufficient for export of YplA-PhoA chimeras by each TTS system. Export of native YplA by each of the three TTS systems was also found to depend on the integrity of its amino terminus. Introduction of a frameshift mutation or deletion of yplA sequences encoding the amino-terminal 20 residues negatively impacted YplA secretion. Deletion of other yplA regions was tolerated, including that resulting in the removal of amino acid residues 30 through 40 of the polypeptide and removal of the 5' untranslated region of the mRNA. This work supports a model in which independent and distantly related TTS systems of Y. enterocolitica recognize protein substrates by a similar mechanism.
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