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

Scientific Reports
Nolan C WorstellHung-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, an...Continue Reading

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Citations

Mar 3, 2019·Glycobiology·Hyun-Kyu ChoiHung-Jen Wu
Dec 19, 2019·Molecular & Cellular Proteomics : MCP·Brian B Haab, Zachary Klamer
Apr 24, 2020·Chemical Communications : Chem Comm·Manuel González-CuestaJosé M García Fernández
Sep 6, 2020·Nature Communications·Melissa RinaldinDaniela J Kraft
Jun 18, 2020·Scientific Reports·Thomas SchubertWinfried Römer
Jan 17, 2021·Molecular & Cellular Proteomics : MCP·Brian B Haab, Zachary Klamer
Mar 6, 2021·The Cell Surface·Paula Parreira, M Cristina L Martins

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Methods Mentioned

BETA
saturation binding
Surface Plasmon Resonance

Software Mentioned

kMC
JSmol

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