ArticleProceedings of the National Academy of Sciences of the United States of America2013
Structural basis for the specific recognition of dual receptors by the homopolymeric pH 6 antigen (Psa) fimbriae of Yersinia pestis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 41 citations in OpenAlex.
- The role of adhesins ofGut microbes · 2026Review
- Discovery of Trypanosoma brucei inhibitors enabled by a unified synthesis of diverse sulfonyl fluorides.Communications chemistry · 2024Article
- Diversity in Genetic Regulation of Bacterial Fimbriae Assembled by the Chaperone Usher Pathway.International journal of molecular sciences · 2022Review
- Use of magnetic nanotrap particles in capturing Yersinia pestis virulence factors, nucleic acids and bacteria.Journal of nanobiotechnology · 2021Article
- Phosphorylation of Extracellular Proteins inFrontiers in microbiology · 2021Article
- Chaperone-tip adhesin complex is vital for synergistic activation of CFA/I fimbriae biogenesis.PLoS pathogens · 2020Article
- Classical chaperone-usher (CU) adhesive fimbriome: uropathogenic Escherichia coli (UPEC) and urinary tract infections (UTIs).Folia microbiologica · 2020Review
- Sulfated Lewis A trisaccharide on oviduct membrane glycoproteins binds bovine sperm and lengthens sperm lifespan.The Journal of biological chemistry · 2019Article
- Yersinia pestis and plague: an updated view on evolution, virulence determinants, immune subversion, vaccination, and diagnostics.Genes and immunity · 2019Review
- The invasin D protein fromThe Journal of biological chemistry · 2018Article
- Structural basis forProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Structural and functional studies on Pseudomonas aeruginosa DspI: implications for its role in DSF biosynthesis.Scientific reports · 2018Article
- Structure-Function Relationship of Aminopeptidase P fromFrontiers in microbiology · 2017Article
- Crystal structure and analysis of HdaB: The enteroaggregative Escherichia coli AAF/IV pilus tip protein.Protein science : a publication of the Protein Society · 2016Article
- Structural Insight into Archaic and Alternative Chaperone-Usher Pathways Reveals a Novel Mechanism of Pilus Biogenesis.PLoS pathogens · 2015Article
- Sulfonyl fluorides as privileged warheads in chemical biology.Chemical science · 2015Article
- Structural and functional insight into the carbohydrate receptor binding of F4 fimbriae-producing enterotoxigenic Escherichia coli.The Journal of biological chemistry · 2015Article
- Structural insight into host recognition by aggregative adherence fimbriae of enteroaggregative Escherichia coli.PLoS pathogens · 2014Article
- Preliminary X-ray diffraction analysis of CfaA, a molecular chaperone essential for the assembly of CFA/I fimbriae of human enterotoxigenic Escherichia coli.Acta crystallographica. Section F, Structural biology communications · 2014Article
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8 authors at 4 institutions in 1 country.
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Abstract
The pH 6 antigen (Psa) of Yersinia pestis consists of fimbriae that bind to two receptors: β1-linked galactosyl residues in glycosphingolipids and the phosphocholine group in phospholipids. Despite the ubiquitous presence of either moiety on the surface of many mammalian cells, Y. pestis appears to prefer interacting with certain types of human cells, such as macrophages and alveolar epithelial cells of the lung. The molecular mechanism of this apparent selectivity is not clear. Site-directed mutagenesis of the consensus choline-binding motif in the sequence of PsaA, the subunit of the Psa fimbrial homopolymer, identified residues that abolish galactosylceramide binding, phosphatidylcholine binding, or both. The crystal structure of PsaA in complex with both galactose and phosphocholine reveals separate receptor binding sites that share a common structural motif, thus suggesting a potential interaction between the two sites. Mutagenesis of this shared structural motif identified Tyr126, which is part of the choline-binding consensus sequence but is found in direct contact with the galactose in the structure of PsaA, important for both receptor binding. Thus, this structure depicts a fimbrial subunit that forms a polymeric adhesin with a unique arrangement of dual receptor binding sites. These findings move the field forward by providing insights into unique types of multiple receptor-ligand interactions and should steer research into the synthesis of dual receptor inhibitor molecules to slow down the rapid progression of plague.
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