Characterization of a novel lectin from pathogenic fungus Microsporum canis

RIEVAJOVÁ, Martina, Lenka MALINOVSKÁ, Hana BEREZŇÁKOVÁ, Jan KOMÁREK a Michaela WIMMEROVÁ. Characterization of a novel lectin from pathogenic fungus Microsporum canis. In 29. kongres Československé společnosti mikrobiologické s mezinárodní účastí. 2022. ISBN 978-80-88379-18-8.

Základní údaje

• Originální název: Characterization of a novel lectin from pathogenic fungus Microsporum canis
• Autoři: RIEVAJOVÁ, Martina, Lenka MALINOVSKÁ, Hana BEREZŇÁKOVÁ, Jan KOMÁREK a Michaela WIMMEROVÁ.
• Vydání: 29. kongres Československé společnosti mikrobiologické s mezinárodní účastí, 2022.

Další údaje

• Originální jazyk: angličtina
• Typ výsledku: Konferenční abstrakt
• Stát vydavatele: Česká republika
• Utajení: není předmětem státního či obchodního tajemství
• WWW: URL
• Organizační jednotka: Přírodovědecká fakulta
• ISBN: 978-80-88379-18-8
• Klíčová slova česky: lektin; Microsporum canis
• Klíčová slova anglicky: lectin; Microsporum canis

Anotace

Microsporum canis is a pathogenic fungus that infects the upper layers of skin and creates inflamed lesions often associated with itchiness, scaling, and hair loss. Its primary hosts are cats and dogs, but it can also infect humans through contact with an infected animal. The infection is often recurring, and the rate of treatment failure is relatively high due to the growing resistance of the pathogen. Adhesion of fungal pathogens in the early stages of infection can be mediated by lectins through the interaction of these saccharide binding proteins with surface glycans of the host cells. This work is focused on characterization of lectin from M. canis – Microsporum canis lectin (MCL) as it might be involved in the adhesion of the pathogen, which makes it a potential target for antiadhesion therapy. The characterization of MCL is greatly hindered by problems with solubility and instability of the protein. However, we managed to obtain basic information about the secondary structure of the protein by circular dichroism and information about thermal stability by nano differential scanning fluorimetry. Also, several potential saccharide inhibitors have been tested by hemagglutination inhibition assay. From the results we can conclude that this thermally stable lectin is specific for L-fucose and its derivates are potential inhibitory agents. The future resesearch will be focused on optimization of production of the recombinant protein, its characteriziation and search for multivalent inhibitors of this lectin with potential role in prevention and therapy