2024
Solving the mysteries of novel two-domain lectins
BURÁŇOVÁ, Tereza; Eva PAULENOVÁ a Michaela WIMMEROVÁZákladní údaje
Originální název
Solving the mysteries of novel two-domain lectins
Autoři
BURÁŇOVÁ, Tereza (203 Česká republika, domácí); Eva PAULENOVÁ (203 Česká republika, domácí) a Michaela WIMMEROVÁ (203 Česká republika, garant, domácí)
Vydání
XXIII. Setkání biochemiků a molekulárních biologů, 2024
Další údaje
Jazyk
angličtina
Typ výsledku
Konferenční abstrakt
Obor
10608 Biochemistry and molecular biology
Stát vydavatele
Česká republika
Utajení
není předmětem státního či obchodního tajemství
Kód RIV
RIV/00216224:14310/24:00138789
Organizační jednotka
Přírodovědecká fakulta
ISBN
978-80-280-0621-1
Klíčová slova česky
lektiny; dvoudoménové proteiny; rekombinantní proteiny
Klíčová slova anglicky
lectins; two-domain proteins; recombinant proteins
Změněno: 5. 2. 2025 16:32, Mgr. Tereza Buráňová
Anotace
V originále
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.
Návaznosti
| LM2023042, projekt VaV |
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