ReviewFrontiers in cellular and infection microbiology2012
Yersinia infection tools-characterization of structure and function of adhesins.
Review in Frontiers in cellular and infection microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed.
- Cooperation between Adh and OR5M11 contributes to the lung pathogenicity of Actinobacillus pleuropneumoniae by facilitating the NLRP3-mediated inflammatory response.Veterinary research · 2026Article
- Engineered Escherichia coli as a microbial cell factory for intracellular protein delivery: strains, vectors, mechanisms, and therapeutic applications.Microbial cell factories · 2026Review
- Anti-infective compounds forSustainable microbiology · 2026Review
- Size-dependent ability of AtaA to immobilize cells in Acinetobacter sp. Tol 5.Scientific reports · 2024Article
- Progress on the research and development of plague vaccines with a call to action.NPJ vaccines · 2024Review
- Macrophage innate immune responses delineate between defective translocon assemblies produced byVirulence · 2023Article
- Chronic Leptin Deficiency Improves Tolerance of Physiological Damage and Host-Pathogen Cooperation during Yersinia pseudotuberculosis Infection.Infection and immunity · 2022Article
- Case report: a genomics-guided reclassification of a blood culture isolate misassigned by MALDI-TOF asAccess microbiology · 2022Article
- Lipopolysaccharide of theBiomolecules · 2021Review
- Development of IMBs-qPCR detection method for Yersinia enterocolitica based on the foxA gene.Archives of microbiology · 2021Article
- Structural Modeling of the Treponema pallidum Outer Membrane Protein Repertoire: a Road Map for Deconvolution of Syphilis Pathogenesis and Development of a Syphilis Vaccine.Journal of bacteriology · 2021Article
- Dynamic relocalization of cytosolic type III secretion system components prevents premature protein secretion at low external pH.Nature communications · 2021Article
- A NovelFrontiers in cellular and infection microbiology · 2021Article
- Tn-Seq Analysis Identifies Genes Important for Yersinia pestis Adherence during Primary Pneumonic Plague.mSphere · 2020Article
- Interaction with the host: the role of fibronectin and extracellular matrix proteins in the adhesion of Gram-negative bacteria.Medical microbiology and immunology · 2020Review
- Inhibition of Neutrophil Primary Granule Release during Yersinia pestis Pulmonary Infection.mBio · 2019Article
- The Yersinia pseudotuberculosis Cpx envelope stress system contributes to transcriptional activation of rovM.Virulence · 2019Article
- Assay development for the discovery of small-molecule inhibitors of YadA adhesion to collagen.Cell surface (Amsterdam, Netherlands) · 2019Article
- Reversible Gene Expression Control in Yersinia pestis by Using an Optimized CRISPR Interference System.Applied and environmental microbiology · 2019Article
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3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Among the seventeen species of the Gram-negative genus Yersinia, three have been shown to be virulent and pathogenic to humans and animals-Y. enterocolitica, Y. pseudotuberculosis, and Y. pestis. In order to be so, they are armoured with various factors that help them adhere to tissues and organelles, cross the cellular barrier and escape the immune system during host invasion. The group of proteins that mediate pathogen-host interactions constitute adhesins. Invasin, Ail, YadA, YadB, YadC, Pla, and pH 6 antigen belong to the most prominent and best-known Yersinia adhesins. They act at different times and stages of infection complementing each other by their ability to bind a variety of host molecules such as collagen, fibronectin, laminin, β1 integrins, and complement regulators. All the proteins are anchored in the bacterial outer membrane (OM), often forming rod-like or fimbrial-like structures that protrude to the extracellular milieu. Structural studies have shown that the anchor region forms a β-barrel composed of 8, 10, or 12 antiparallel β-strands. Depending on the protein, the extracellular part can be composed of several domains belonging to the immunoglobulin fold superfamily, or form a coiled-coil structure with globular head domain at the end, or just constitute several loops connecting individual β-strands in the β-barrel. Those extracellular regions define the activity of each adhesin. This review focuses on the structure and function of these important molecules, and their role in pathogenesis.
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