Publication details
Studies of mutant lectin binding behaviour by microcalorimetry
| Authors | |
|---|---|
| Year of publication | 2014 |
| Type | Conference abstract |
| MU Faculty or unit | |
| Citation | |
| Description | Bacterial lectins help pathogens in adhesion to sugar moieties presented on the host cell surface. Therefore, lectins from pathogenic bacteria and their adhesion modes are the subject of intense study. On the other hand, understanding of the basic principles of the lectin-carbohydrate binding process is still important task and can be helpful for further lectin engineering by targeted mutagenesis methods. Lectins with tuned affinity can offer interesting perspectives in biomedical or biotechnology. Our work is focused on the engineering of previously well studied lectins PA-IIL [1], CV-IIL [2], RS-IIL [3] and BC2L-A [4] from the PA-IIL lectin family. Effects of the mutations on the individual lectin binding behaviour were studied by isothermal titration microcalorimetry method (ITC). |
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