Hetero-Multivalency of Pseudomonas aeruginosa Lectin LecA Binding to Model Membranes View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2018-12

AUTHORS

Nolan C. Worstell, Akshi Singla, Panatda Saenkham, Thushara Galbadage, Preeti Sule, Dongheon Lee, Alec Mohr, Joseph Sang-Il Kwon, Jeffrey D. Cirillo, Hung-Jen Wu

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 modeled LecA's two-step binding process with membranes using a kinetic Monte Carlo simulation. The simulation identified the frequency of low-affinity ligand encounters with bound LecA and the bound LecA's retention of the low-affinity ligand as essential parameters for triggering hetero-multivalent binding, agreeing with experimental observations. The hetero-multivalency can alter lectin binding properties, including avidities, capacities, and kinetics, and therefore, it likely occurs in various multivalent binding systems. Using hetero-multivalency concept, we also offered a new strategy to design high-affinity drug carriers for targeted drug delivery. More... »

PAGES

8419

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41598-018-26643-7

DOI

http://dx.doi.org/10.1038/s41598-018-26643-7

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1104216300

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/29849092


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