Zoeken
Zoeken kan via de modus 'eenvoudig zoeken' (één veld) of uitgebreid via 'geavanceerd zoeken' (meerdere velden). Zo kan je bv. zoeken op een combinatie van een auteursnaam (auteur), een jaartal (jaar) en een documenttype.
Boekenmand
Nuttige resultaten kan je aanvinken en toevoegen aan een mandje. De inhoud hiervan kan je exporteren of afdrukken (naar bv. PDF).
RSS
Op de hoogte blijven van nieuw toegevoegde publicaties binnen uw interessegebied? Dit kan door een RSS-feed (?) te maken van jouw zoekopdracht.
nieuwe zoekopdracht
Mannose-specific lectins from marine algae: diverse structural scaffolds associated to common virucidal and anti-cancer properties
Barre, A.; Simplicien, M.; Benoist, H.; Van Damme, E.J.M.; Rougé, P. (2019). Mannose-specific lectins from marine algae: diverse structural scaffolds associated to common virucidal and anti-cancer properties. Mar. Drugs 17(8): 440. https://dx.doi.org/10.3390/md17080440
In: Marine Drugs. Molecular Diversity Preservation International (MDPI): Basel. ISSN 1660-3397; e-ISSN 1660-3397
|   |
| Trefwoorden |
Rhodophyta [WoRMS]
Marien/Kust |
| Author keywords |
lectin; seaweed; red algae; mannose-binding specificity;structure-function relationships; diagnostic tool; therapeutic drugs;anti-cancer properties; anti-HIV-1 properties |
| Auteurs | | Top |
- Barre, A.
- Simplicien, M.
- Benoist, H.
|
- Van Damme, E.J.M.
- Rougé, P.
|
|
| Abstract |
To date, a number of mannose-specific lectins have been isolated and characterized from seaweeds, especially from red algae. In fact, man-specific seaweed lectins consist of different structural scaffolds harboring a single or a few carbohydrate-binding sites which specifically recognize mannose-containing glycans. Depending on the structural scaffold, man-specific seaweed lectins belong to five distinct structurally-related lectin families, namely (1) the griffithsin lectin family (β-prism I scaffold); (2) the Oscillatoria agardhii agglutinin homolog (OAAH) lectin family (β-barrel scaffold); (3) the legume lectin-like lectin family (β-sandwich scaffold); (4) the Galanthus nivalis agglutinin (GNA)-like lectin family (β-prism II scaffold); and, (5) the MFP2-like lectin family (MFP2-like scaffold). Another algal lectin from Ulva pertusa, has been inferred to the methanol dehydrogenase related lectin family, because it displays a rather different GlcNAc-specificity. In spite of these structural discrepancies, all members from the five lectin families share a common ability to specifically recognize man-containing glycans and, especially, high-mannose type glycans. Because of their mannose-binding specificity, these lectins have been used as valuable tools for deciphering and characterizing the complex mannose-containing glycans from the glycocalyx covering both normal and transformed cells, and as diagnostic tools and therapeutic drugs that specifically recognize the altered high-mannose N-glycans occurring at the surface of various cancer cells. In addition to these anti-cancer properties, man-specific seaweed lectins have been widely used as potent human immunodeficiency virus (HIV-1)-inactivating proteins, due to their capacity to specifically interact with the envelope glycoprotein gp120 and prevent the virion infectivity of HIV-1 towards the host CD4+ T-lymphocyte cells in vitro. |
IMIS is ontwikkeld en wordt gehost door het VLIZ.
