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listera ovata/mannose

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StraipsniaiKlinikiniai tyrimaiPatentai
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The Orchidaceae species Listera ovata and Epipactis helleborine contain two types of mannose-binding proteins. Using a combination of affinity chromatography on mannose-Sepharose-4B and ion exchange chromatography on a Mono-S column eight different mannose-binding proteins were isolated from the

Leaves of the Orchid Twayblade (Listera ovata) Contain a Mannose-Specific Lectin.

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A new lectin was isolated from leaves of the twayblade (Listera ovata). It is a dimeric protein built up of two subunits of M(r) 12,500. This lectin, which is the first to be isolated from a species of the family Orchidaceae, exhibits exclusive specificity towards mannose.
Mannose-binding lectins were purified from the leaves of three Orchidaceae species, namely Listera ovata (twayblade), Epipactis helleborine (broad-leaved helleborine) and Cymbidium hybrid, using affinity chromatography on Mannose - Sepharose-4B. Apparently, the Orchidaceae lectins are dimeric
The alpha-(1-3)-D-mannose- and alpha-(1-6)-D-mannose-specific agglutinins (lectins) from Galanthus nivalis, Hippeastrum hybrid, Narcissus pseudonarcissus, and Listera ovata inhibited infection of MT-4 cells by human immunodeficiency virus types 1 and 2 (HIV-1 and HIV-2) and simian immunodeficiency
A series of four mannose(Man)-, three N-acetylglucosamine (GlcNAc)n-, ten N-acetylgalactosamine/galactose(GalNAc/Gal)-, one 5-acetylneuraminic acid (alpha-2,3-Gal/GalNAc)- and one 5-acetylneuroaminic acid(alpha-2,6-Gal/Gal-NAc)-specific plant agglutinins were evaluated for their antiviral activity
The carbohydrate-binding specificity of an alpha-D-mannose-specific lectin isolated from leaves of the orchid twayblade (Listera ovata) was elucidated by quantitative precipitation of mannose-containing polysaccharides and glycoproteins, hapten inhibition, and affinity chromatography on the

Current lead natural products for the chemotherapy of human immunodeficiency virus (HIV) infection.

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A large variety of natural products have been described as anti-HIV agents, and for a portion thereof the target of interaction has been identified. Cyanovirin-N, a 11-kDa protein from Cyanobacterium (blue-green alga) irreversibly inactivates HIV and also aborts cell-to-cell fusion and transmission
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