Novel two-domain lectin from bacterium Photorhabdus laumondii
| Authors | |
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| Year of publication | 2023 |
| Type | Appeared in Conference without Proceedings |
| MU Faculty or unit | |
| Citation | |
| Description | Lectins, saccharide binding proteins, play a key role in the pathogenic processes of diverse bacteria. High interaction specificity enables the recognition of the host cell and adhesion to it. Rather low binding affinity is compensated by a quite strong avidity effect, as lectins are usually polyvalent. Photorhabdus spp., entomopathogenic bacteria, produce various lectins, a few of which have been already characterized. In my work, I focus on producing and characterizing a novel two-domain lectin from Photorhabdus laumondii. First of all, bioinformatical analysis was performed. A synthetic gene was inserted into a production vector and the recombinant protein was produced by E. coli. After production optimization, several methods were used to characterize the binding properties of the recombinant protein, e. g. batch method, and hemagglutination. |
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