MIKYSKOVÁ, Michaela, Filip MELICHER and 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.
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Basic information
Original name Structural characterization of the jacalin-related lectin from the mushroom Calocera viscosa
Name in Czech Strukturní charakterizace jacalinu-podobného lektinu z houby krásnorůžek lepkavý
Authors MIKYSKOVÁ, Michaela (203 Czech Republic, belonging to the institution), Filip MELICHER (703 Slovakia, belonging to the institution) and Michaela WIMMEROVÁ (203 Czech Republic, guarantor).
Edition XXVIIth Biochemistry congress, 2023.
Other information
Original language English
Type of outcome Presentations at conferences
Field of Study 10608 Biochemistry and molecular biology
Country of publisher Slovakia
Confidentiality degree is not subject to a state or trade secret
RIV identification code RIV/00216224:14310/23:00133257
Organization unit Faculty of Science
ISBN 978-80-8240-047-5
Keywords (in Czech) lektiny; Calocera viscosa; krásnorůžek lepkavý; jacalinové lektiny; houby
Keywords in English lectins; Calocera viscosa; yellow stagshorn; jacalin-related lectins; fungi
Changed by Changed by: Mgr. Michaela Mikysková, učo 478218. Changed: 26/1/2024 16:25.
Abstract
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.
Links
LM2023042, research and development projectName: Česká infrastruktura pro integrativní strukturní biologii
Investor: Ministry of Education, Youth and Sports of the CR, CIISB - Czech Infrastructure for Integrative Structural Biology
PrintDisplayed: 13/7/2024 10:19