Structural characterization of the jacalin-related lectin from
the mushroom Calocera viscosa

k 2023

Structural characterization of the jacalin-related lectin from the mushroom Calocera viscosa

MIKYSKOVÁ, Michaela, Filip MELICHER and Michaela WIMMEROVÁ

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

Language

English

Type of outcome

Prezentace na konferencích

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

Slovakia

Confidentiality degree

není předmětem státního či obchodního tajemství

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

Změněno: 26/1/2024 16:25, Mgr. Michaela Mikysková

Abstract

V originále

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 project

Name: Česká infrastruktura pro integrativní strukturní biologii

Investor: Ministry of Education, Youth and Sports of the CR, CIISB - Czech Infrastructure for Integrative Structural Biology

Citovat

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.

@proceedings{2366058,
   author = {Mikysková, Michaela and Melicher, Filip and Wimmerová, Michaela},
   booktitle = {XXVIIth Biochemistry congress},
   keywords = {lectins; Calocera viscosa; yellow stagshorn; jacalin-related lectins; fungi},
   language = {eng},
   isbn = {978-80-8240-047-5},
   title = {Structural characterization of the jacalin-related lectin from the mushroom Calocera viscosa},
   year = {2023}
}

TY  - CONF
ID  - 2366058
AU  - Mikysková, Michaela - Melicher, Filip - Wimmerová, Michaela
PY  - 2023
TI  - Structural characterization of the jacalin-related lectin from the mushroom Calocera viscosa
SN  - 9788082400475
KW  - lectins
KW  - Calocera viscosa
KW  - yellow stagshorn
KW  - jacalin-related lectins
KW  - fungi
N2  - 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.
ER  -

MIKYSKOVÁ, Michaela, Filip MELICHER and Michaela WIMMEROVÁ. Structural characterization of the jacalin-related lectin from the mushroom Calocera viscosa. In \textit{XXVIIth Biochemistry congress}. 2023. ISBN~978-80-8240-047-5.

Detailed Information on Publication Record