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 a Michaela WIMMEROVÁ

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

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

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

Anotace

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.

Návaznosti

LM2023042, projekt VaV

Název: Česká infrastruktura pro integrativní strukturní biologii

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, CIISB - Česká infrastruktura pro integrativní strukturní biologii

Citovat

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.

@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 a 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.

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