Solving the mysteries of novel two-domain lectins

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F24%3A00138789" target="_blank" >RIV/00216224:14310/24:00138789 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Solving the mysteries of novel two-domain lectins
Original language 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 patients with immune deficiencies (e.g. cystic fibrosis patients) [1]. In the past, several LecB homologs were described, including lectins produced by Burkholderia cenocepacia, Ralstonia solanacearum, and Chromobacterium violaceum [2,3,4]. Nevertheless, there are still uncharacterized LecB-like proteins in the pathogenic bacteria, some of which contain an additional domain of unknown function. Their characterization could provide insights into the mechanism of infections and lead to the development of novel approaches to disease treatment. The objective of the presented project is to characterize three potential two-domain lectins containing a LecB-like domain with an emphasis on their binding properties. The genes encoding these hypothetical carbohydrate-specific proteins were identified through bioinformatic analysis. Synthetic genes were cloned into expression vectors and expressed in E. coli. The properties of the proteins were examined using a variety of methods.
Czech name
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Czech description
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Project
<a href="/en/project/LM2023042" target="_blank" >LM2023042: Czech Infrastructure for Integrative Structural Biology</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach

Publication year
2024
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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