Publication details
When LecB Is Not Alone: Structural and Functional Analysis of a Two-Domain Lectin
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| Year of publication | 2026 |
| Type | Appeared in Conference without Proceedings |
| MU Faculty or unit | |
| Citation | |
| Description | LecB (PA-IIL) is a well-characterized lectin from the opportunistic pathogen Pseudomonas aeruginosa that plays a central role in host colonization and biofilm formation, particularly in immunocompromised patients such as those with cystic fibrosis [1]. Homologous lectins have also been identified in other pathogenic bacteria, including Burkholderia cenocepacia [2]. Notably, several uncharacterized LecB-like proteins contain an additional N-terminal domain of unknown function, suggesting functional diversification within this lectin family. In this project, we study a putative two-domain lectin comprising a canonical LecB-like carbohydrate-binding domain fused to an N-terminal accessory domain. A candidate gene from an insect pathogen was identified through bioinformatic analysis, cloned, and recombinantly expressed in E. coli. Full-length protein and individual domains were purified and characterized using biophysical methods (nanoDSF, AUC, DLS), confirming stable and well-defined oligomeric states. The N-terminal domain structure has been largely determined by molecular replacement and is currently under refinement. Crystallization of both the LecB-like domain and the full-length construct is being optimized. Structural comparison with canonical LecB and AlphaFold predictions suggests alterations in the putative carbohydrate-binding region that may affect ligand specificity. Together, these results highlight structural diversity within LecB-like lectins and provide a basis for understanding their functional evolution and potential functional specialization. |
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