MIKYSKOVÁ, Michaela, Filip MELICHER a Michaela WIMMEROVÁ. Structural characterization of the jacalin-related lectin from the mushroom Calocera viscosa. In XXVIIth Biochemistry congress. 2023. ISBN 978-80-8240-047-5.
Další formáty:   BibTeX LaTeX RIS
Základní údaje
Originální název Structural characterization of the jacalin-related lectin from the mushroom Calocera viscosa
Název česky Strukturní charakterizace jacalinu-podobného lektinu z houby krásnorůžek lepkavý
Autoři MIKYSKOVÁ, Michaela (203 Česká republika, domácí), Filip MELICHER (703 Slovensko, domácí) a Michaela WIMMEROVÁ (203 Česká republika, garant).
Vydání XXVIIth Biochemistry congress, 2023.
Další údaje
Originální jazyk angličtina
Typ výsledku Prezentace na konferencích
Obor 10608 Biochemistry and molecular biology
Stát vydavatele Slovensko
Utajení není předmětem státního či obchodního tajemství
Kód RIV RIV/00216224:14310/23:00133257
Organizační jednotka Přírodovědecká fakulta
ISBN 978-80-8240-047-5
Klíčová slova česky lektiny; Calocera viscosa; krásnorůžek lepkavý; jacalinové lektiny; houby
Klíčová slova anglicky lectins; Calocera viscosa; yellow stagshorn; jacalin-related lectins; fungi
Změnil Změnila: Mgr. Michaela Mikysková, učo 478218. Změněno: 26. 1. 2024 16:25.
Anotace
The research is focused on the properties and the structural analysis of the new lectin - saccharide binding protein - from the mushroom Calocera viscosa (CalVL). Mushroom lectins have been variously explored and studied for their potential in biomedicine. Based on lectin-glycan interactions, they exhibit mitogenic, antiproliferative and antimicrobial effects. Various methods were employed to characterize different properties of this lectin. Initial predictions suggested that the CalVL belongs to the family of jacalin-related lectins (JRLs) with a beta-prism fold. JRLs are known for their specificity to D-galactose and D-mannose. The CalVL was produced in E. coli expression system, and purified by affinity chromatography on mannose-agarose resin. Later it was shown by hemagglutination assay that the CalVL can agglutinate erythrocytes due to the interaction with their surface saccharides. Thermostability was determined by Differential Scanning Fluorimetry, homogeneity and the oligomeric state of the protein by Dynamic Light Scattering and Analytical Ultracentrifugation. Crystallization in various screens was performed using the vapour diffusion method, specifically the sitting drop technique. Data collection from obtained crystals was performed on synchrotron PETRAIII. The structure of the CalVL with D-mannose was solved by molecular replacement, where the CalVL without ligand was used as a model. This confirms the prediction of the CalVL being a member of the JRLs family.
Návaznosti
LM2023042, projekt VaVNázev: Česká infrastruktura pro integrativní strukturní biologii
Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, CIISB - Česká infrastruktura pro integrativní strukturní biologii
VytisknoutZobrazeno: 1. 9. 2024 14:33