a 2022

Characterization of a novel lectin from pathogenic fungus Microsporum canis

RIEVAJOVÁ, Martina, Lenka MALINOVSKÁ, Hana BEREZŇÁKOVÁ, Jan KOMÁREK, Michaela WIMMEROVÁ et. al.

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

Jazyk

angličtina

Typ výsledku

Konferenční abstrakt

Stát vydavatele

Česká republika

Utajení

není předmětem státního či obchodního tajemství

Odkazy

Organizační jednotka

Přírodovědecká fakulta

ISBN

978-80-88379-18-8

Klíčová slova česky

lektin; Microsporum canis;

Klíčová slova anglicky

lectin; Microsporum canis;
Změněno: 29. 5. 2023 12:02, Mgr. Martina Rievajová

Anotace

V originále

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