Hetero-Multivalency of Pseudomonas aeruginosa Lectin LecA Binding to Model Membranes.

ABSTRACT: A single glycan-lectin interaction is often weak and semi-specific. Multiple binding domains in a single lectin can bind with multiple glycan molecules simultaneously, making it difficult for the classic "lock-and-key" model to explain these interactions. We demonstrated that hetero-multivalency, a homo-oligomeric protein simultaneously binding to at least two types of ligands, influences LecA (a Pseudomonas aeruginosa adhesin)-glycolipid recognition. We also observed enhanced binding between P. aeruginosa and mixed glycolipid liposomes. Interestingly, strong ligands could activate weaker binding ligands leading to higher LecA binding capacity. This hetero-multivalency is probably mediated via a simple mechanism, Reduction of Dimensionality (RD). To understand the influence of RD, we also

SUBMITTER: Worstell NC 

PROVIDER: S-EPMC5976636 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature