{"refrec":{"BRefID":323035,"RR":"<b>Barre, A.; Simplicien, M.; Benoist, H.; Van Damme, E.J.M.; Rougé, P.</b> (2019). Mannose-specific lectins from marine algae: diverse structural scaffolds associated to common virucidal and anti-cancer properties. <i>Mar. Drugs 17(8)</i>: 440. <a href=\"https://dx.doi.org/10.3390/md17080440\" target=\"_blank\">https://dx.doi.org/10.3390/md17080440</a>","BEntID":316506,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":0,"RefStringPartII":". <i>Mar. Drugs 17(8)</i>: 440. <a href=\"https://dx.doi.org/10.3390/md17080440\" target=\"_blank\">https://dx.doi.org/10.3390/md17080440</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Barre, A.; Simplicien, M.; Benoist, H.; Van Damme, E.J.M.; Rougé, P.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Barre, A. <i>et al.</i>","Englishabstract":"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 <span class=\"html-italic\">Oscillatoria agardhii</span> agglutinin homolog (OAAH) lectin family (β-barrel scaffold); (3) the legume lectin-like lectin family (β-sandwich scaffold); (4) the <span class=\"html-italic\">Galanthus nivalis</span> agglutinin (GNA)-like lectin family (β-prism II scaffold); and, (5) the MFP2-like lectin family (MFP2-like scaffold). Another algal lectin from <span class=\"html-italic\">Ulva pertusa</span>, 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 <span class=\"html-italic\">N</span>-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.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Mannose-specific lectins from marine algae: diverse structural scaffolds associated to common virucidal and anti-cancer properties","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2026-04-19 01:32:05.188672","timezone_type":1,"timezone":"+02:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"lectin; seaweed; red algae; mannose-binding specificity;structure-function relationships; diagnostic tool; therapeutic drugs;anti-cancer properties; anti-HIV-1 properties","OtherDescriptors":null,"Notes":null,"AnaPub":2019,"MonPub":null,"DateUpdate":"2020-04-08","DateCreate":"2020-04-07","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000484403200043","VABBcode":null,"OpenAcc":1,"DOI":"10.3390/md17080440"},"refs":null,"anarec":{"AnaID":323035,"PubliDate":2019,"Pagination":"440","XtraPublOfAnaID":null,"ISBN":null,"Volume":"17","Issue":"8","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":113252,"SerRR":"Marine Drugs. 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