1 results match your criteria: "Syracuse University 1-014 Center of Science and Technology[Affiliation]"
Chemical control over Asialo-GM1: A dual ligand for pili and Lectin A that activates swarming motility and facilitates adherence of Pseudomonas aeruginosa.
Colloids Surf B Biointerfaces
July 2022
Department of Chemistry, Syracuse University 1-014 Center of Science and Technology, Syracuse, NY 13244, USA. Electronic address:
Article Synopsis
- Glycolipid asialo-GM1 on mammalian cells is recognized by both type IV pili and Lectin A (LecA) proteins of Pseudomonas aeruginosa, impacting bacterial motility and adherence.
- Research shows that asialo-GM1 enhances swarming and twitching on gel surfaces while promoting adherence on solid surfaces, indicating its role in modulating bacterial activities through different signaling pathways.
- Treatment with pili or LecA proteins can inhibit asialo-GM1 mediated swarming and cause leakage from liposomes, suggesting a complex interaction that affects bacterial adherence and motility.