Aspergillus fumigatus lectin ? a new procedure for studying highly complex interactions of multivalent lectins with their ligands
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F11%3A00050064" target="_blank" >RIV/00216224:14310/11:00050064 - isvavai.cz</a>
Result on the web
—
DOI - Digital Object Identifier
—
Alternative languages
Result language
angličtina
Original language name
Aspergillus fumigatus lectin ? a new procedure for studying highly complex interactions of multivalent lectins with their ligands
Original language description
Lectins are proteins or glycoproteins of non-immune origin which recognize and bind reversibly to diverse sugar structures. They are involved in recognition events in a variety of physiological and pathological processes. One of the most interesting biological function of these sugar-specific proteins is their involvement in host-pathogen interactions. Wide range of pathogenic bacteria and viruses use their surface lectins (called adhesins) for recognition and adhesion to host tissues ? in the the crucial step for initiation of infection. Inhibition of these lectins by suitable carbohydrates or their analogs might prevent attachment of pathogens to host cells and prevent the disease outbreak. Aspergillus fumigatus is an ubiquitous saprophytic mold andopportunistic pathogen responsible for severe infections in immuno-compromised individuals. The project is focused on a detailed characterization of L-fucose specific lectin AFL from A. fumigatus.
Czech name
—
Czech description
—
Classification
Type
O - Miscellaneous
CEP classification
CE - Biochemistry
OECD FORD branch
—
Result continuities
Project
<a href="/en/project/GA303%2F09%2F1168" target="_blank" >GA303/09/1168: Lectins from human pathogens - structure, function, engineering</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach
Others
Publication year
2011
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů