Mysteries of Lectins in Opportunistic Pathogens: Two Domains – One Purpose?
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| Year of publication | 2025 |
| Type | Conference abstract |
| MU Faculty or unit | |
| Citation | |
| Description | LecB (PA-IIL) is one of two characterized lectins (saccharide-binding proteins) from the bacterium Pseudomonas aeruginosa. Both proteins (LecA and LecB) play a significant role in bacterial infection and biofilm formation in immunocompromised patients, such as those with cystic fibrosis.1 Several LecB homologs have been described, including lectins produced by Burkholderia cenocepacia.2 Nevertheless, there remain uncharacterized LecB-like proteins in the pathogenic bacteria, some of which contain an additional domain of unknown function. Characterizing these proteins could provide insight into infection mechanisms and lead to the development of novel disease treatment approaches. This project aims to structurally and functionally characterize two potential two-domain lectins that contain a LecB-like domain with an emphasis on their binding properties. The genes encoding these hypothetical carbohydrate-specific proteins originating in opportunistic human pathogens were identified by bioinformatic analysis. The genes were then cloned into expression vectors and expressed in Escherichia coli. Additionally, new gene constructs were prepared to characterize each domain separately. The examined proteins (whole proteins, as well as separate domains) are undergoing production and purification optimization. Various methods are being used to investigate the thermostability, homogeneity, and binding properties of the purified proteins. The contribution focuses on the current state of knowledge regarding those two-domain proteins. |
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