ArticlePloS one2011
Pseudomonas aeruginosa PilY1 binds integrin in an RGD- and calcium-dependent manner.
Article in PloS one, 2011. 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.
- Cx43 levels guide apicobasal polarity in regenerating airway epithelial cells.Communications biology · 2026Article
- PilY proteins: bimodular drivers of type IV pilus versatility.Trends in microbiology · 2026Review
- Diversity, classification, and evolution of myxobacterial PilY1 proteins.Frontiers in microbiology · 2026Article
- Article
- Separation ofmBio · 2025Article
- Tad pili with adaptable tips mediate contact-dependent killing during bacterial predation.Nature communications · 2025Article
- Mechanical forces and ligand binding modulateLife science alliance · 2025Article
- Bacterial adhesion strategies and countermeasures in urinary tract infection.Nature microbiology · 2025Review
- Saccharibacteria deploy two distinct type IV pili, driving episymbiosis, host competition, and twitching motility.The ISME journal · 2025Article
- Respiratory processes of early-evolved hyperthermophiles in sulfidic and low-oxygen geothermal microbial communities.Nature communications · 2025Article
- Saccharibacteria deploy two distinct Type IV pili, driving episymbiosis, host competition, and twitching motility.bioRxiv : the preprint server for biology · 2024Article
- PilY1 regulates the dynamic architecture of the type IV pilus machine in Pseudomonas aeruginosa.Nature communications · 2024Article
- Engagement of αFrontiers in microbiology · 2024Article
- Feature architecture aware phylogenetic profiling indicates a functional diversification of type IVa pili in the nosocomial pathogen Acinetobacter baumannii.PLoS genetics · 2023Article
- Mechanism of assembly of type 4 filaments: everything you always wanted to know (but were afraid to ask).Microbiology (Reading, England) · 2023Review
- The differential expression of PilY1 proteins by the HsfBA phosphorelay allows twitching motility in the absence of exopolysaccharides.PLoS genetics · 2022Article
- Kingella kingae PilC1 and PilC2 are adhesive multifunctional proteins that promote bacterial adherence, twitching motility, DNA transformation, and pilus biogenesis.PLoS pathogens · 2022Article
- A noncanonical cytochromeProceedings of the National Academy of Sciences of the United States of America · 2022Article
- PilB fromProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
PilY1 is a type IV pilus (tfp)-associated protein from the opportunistic pathogen Pseudomonas aeruginosa that shares functional similarity with related proteins in infectious Neisseria and Kingella species. Previous data have shown that PilY1 acts as a calcium-dependent pilus biogenesis factor necessary for twitching motility with a specific calcium binding site located at amino acids 850-859 in the 1,163 residue protein. In addition to motility, PilY1 is also thought to play an important role in the adhesion of P. aeruginosa tfp to host epithelial cells. Here, we show that PilY1 contains an integrin binding arginine-glycine-aspartic acid (RGD) motif located at residues 619-621 in the PilY1 from the PAK strain of P. aeruginosa; this motif is conserved in the PilY1s from the other P. aeruginosa strains of known sequence. We demonstrate that purified PilY1 binds integrin in vitro in an RGD-dependent manner. Furthermore, we identify a second calcium binding site (amino acids 600-608) located ten residues upstream of the RGD. Eliminating calcium binding from this site using a D608A mutation abolished integrin binding; in contrast, a calcium binding mimic (D608K) preserved integrin binding. Finally, we show that the previously established PilY1 calcium binding site at 851-859 also impacts the protein's association with integrin. Taken together, these data indicate that PilY1 binds to integrin in an RGD- and calcium-dependent manner in vitro. As such, P. aeruginosa may employ these interactions to mediate host epithelial cell binding in vivo.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.