Detailed Information on Publication Record
2022
Characterization of a novel lectin from pathogenic fungus Microsporum canis
RIEVAJOVÁ, Martina, Lenka MALINOVSKÁ, Hana BEREZŇÁKOVÁ, Jan KOMÁREK, Michaela WIMMEROVÁ et. al.Basic information
Original name
Characterization of a novel lectin from pathogenic fungus Microsporum canis
Authors
Edition
29. kongres Československé společnosti mikrobiologické s mezinárodní účastí, 2022
Other information
Language
English
Type of outcome
Konferenční abstrakt
Country of publisher
Czech Republic
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Organization unit
Faculty of Science
ISBN
978-80-88379-18-8
Keywords (in Czech)
lektin; Microsporum canis;
Keywords in English
lectin; Microsporum canis;
Změněno: 29/5/2023 12:02, Mgr. Martina Rievajová
Abstract
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