ArticleMolecular microbiology2019
Ail provides multiple mechanisms of serum resistance to Yersinia pestis.
Article in Molecular microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 29 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
- Proteins of the SubB family provide multiple mechanisms of serum resistance inEmerging microbes & infections · 2025Article
- The Gene Ail for the Attachment-Invasion Locus Protein ofInternational journal of molecular sciences · 2025Article
- Pathogenicity and virulence ofVirulence · 2024Review
- Determinants of bacterial survival and proliferation in blood.FEMS microbiology reviews · 2024Review
- Outer membrane protein OMP76 ofVirulence · 2023Article
- Yersinia pestis ΔApplied and environmental microbiology · 2023Article
- Article
- Edwardsiella tarda TraT is an anti-complement factor and a cellular infection promoter.Communications biology · 2022Article
- Contributions of Yersinia pestis outer membrane protein Ail to plague pathogenesis.Current opinion in infectious diseases · 2022Review
- Engineering a HyperstableJournal of the American Chemical Society · 2022Article
- Correlating the Structure and Activity of Y. pestis Ail in a Bacterial Cell Envelope.Biophysical journal · 2021Article
- Interactions Between PathogenicFrontiers in cellular and infection microbiology · 2021Review
- Yersinia pestis: the Natural History of Plague.Clinical microbiology reviews · 2020Review
- 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
- Yersinia pestis and plague: an updated view on evolution, virulence determinants, immune subversion, vaccination, and diagnostics.Genes and immunity · 2019Review
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Ail, a multifunctional outer membrane protein of Yersinia pestis, confers cell binding, Yop delivery and serum resistance activities. Resistance to complement proteins in serum is critical for the survival of Y. pestis during the septicemic stage of plague infections. Bacteria employ a variety of tactics to evade the complement system, including recruitment of complement regulatory factors, such as factor H, C4b-binding protein (C4BP) and vitronectin (Vn). Y. pestis Ail interacts with the regulatory factors Vn and C4BP, and Ail homologs from Y. enterocolitica and Y. pseudotuberculosis recruit factor H. Using co-sedimentation assays, we demonstrate that two surface-exposed amino acids, F80 and F130, are required for the interaction of Y. pestis Ail with Vn, factor H and C4BP. However, although Ail-F80A/F130A fails to interact with these complement regulatory proteins, it still confers 10,000-fold more serum resistance than a Δail strain and prevents C9 polymerization, potentially by directly interfering with MAC assembly. Using site-directed mutagenesis, we further defined this additional mechanism of complement evasion conferred by Ail. Finally, we find that at Y. pestis concentrations reflective of early-stage septicemic plague, Ail weakly recruits Vn and fails to recruit factor H, suggesting that this alternative mechanism of serum resistance may be essential during plague infection.
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