ArticleInfection and immunity2010
Outer membrane protein X (Ail) contributes to Yersinia pestis virulence in pneumonic plague and its activity is dependent on the lipopolysaccharide core length.
Article in Infection and immunity, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 75 citations in OpenAlex.
- Structure-activity of outer membrane proteins in native bacterial membrane vesicles by solid-state NMR.bioRxiv : the preprint server for biology · 2026Article
- Unveiling the role of outer membrane proteins (OMPs) in biofilm formation and Harnessing them for targeting biofilm-forming bacterial infections.World journal of microbiology & biotechnology · 2026Review
- Synthetic and natural antimicrobials as a control against food borne pathogens: A review.Heliyon · 2023Review
- Yersinia pestis ΔApplied and environmental microbiology · 2023Article
- Article
- Contributions of Yersinia pestis outer membrane protein Ail to plague pathogenesis.Current opinion in infectious diseases · 2022Review
- Polylysine for skin regeneration: A review of recent advances and future perspectives.Bioengineering & translational medicine · 2022Review
- Roles of OmpA in Type III Secretion System-Mediated Virulence of EnterohemorrhagicPathogens (Basel, Switzerland) · 2021Article
- Deletion of Yersinia pestisJournal of bacteriology · 2021Article
- Lipopolysaccharide of theBiomolecules · 2021Review
- Roles of OmpX, an Outer Membrane Protein, on Virulence and Flagellar Expression in Uropathogenic Escherichia coli.Infection and immunity · 2021Article
- Correlating the Structure and Activity of Y. pestis Ail in a Bacterial Cell Envelope.Biophysical journal · 2021Article
- Mutually constructive roles of Ail and LPS in Yersinia pestis serum survival.Molecular microbiology · 2020Article
- Tn-Seq Analysis Identifies Genes Important for Yersinia pestis Adherence during Primary Pneumonic Plague.mSphere · 2020Article
- Article
- Activation of Heme Oxygenase Expression by Cobalt Protoporphyrin Treatment Prevents Pneumonic Plague Caused by Inhalation ofAntimicrobial agents and chemotherapy · 2020Article
- Proteomic profiling ofBioImpacts : BI · 2020Article
- Ail provides multiple mechanisms of serum resistance to Yersinia pestis.Molecular microbiology · 2019Article
- Overexpression of Outer Membrane Protein X (OmpX) Compensates for the Effect of TolC Inactivation on Biofilm Formation and Curli Production in Extraintestinal PathogenicFrontiers in cellular and infection microbiology · 2018Article
- Structural Insights into the Yersinia pestis Outer Membrane Protein Ail in Lipid Bilayers.The journal of physical chemistry. B · 2017Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Yersinia pestis, the causative agent of plague, is one of the most virulent microorganisms known. The outer membrane protein X (OmpX) in Y. pestis KIM is required for efficient bacterial adherence to and internalization by cultured HEp-2 cells and confers resistance to human serum. Here, we tested the contribution of OmpX to disease progression in the fully virulent Y. pestis CO92 strain by engineering a deletion mutant and comparing its ability in mediating pneumonic plague to that of the wild type in two animal models. The deletion of OmpX delayed the time to death up to 48 h in a mouse model and completely attenuated virulence in a rat model of disease. All rats challenged with 1 × 10(8) CFU of the ompX mutant survived, compared to the 50% lethal dose (LD50) of 1.2 × 10(3) CFU for the wild-type strain. Because murine serum is not bactericidal for the ompX mutant, the mechanism underlying the delay in time to death in mice was attributed to loss of adhesion/internalization properties but not serum resistance. The rat model, which is most similar to humans, highlighted the critical role of serum resistance in disease. To resolve conflicting evidence for the role of Y. pestis lipopolysaccharide (LPS) and OmpX in serum resistance, ompX was cloned into Escherichia coli D21 and three isogenic derivatives engineered to have progressively truncated LPS core saccharides. OmpX-mediated serum resistance, adhesiveness, and invasiveness, although dependent on LPS core length, displayed these functions in E. coli, independently of other Yersinia proteins and/or LPS. Also, autoaggregation was required for efficient OmpX-mediated adhesiveness and internalization but not serum resistance.
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Registered trials
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