Mannose-Specific Lectins from Marine Algae: Diverse Structural Scaffolds Associated to Common Virucidal and Anti-Cancer Properties
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-con...
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creator | Barre, A Simplicien, M Benoist, H Van Damme, Els Rougé, P |
description | 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 (beta-prism I scaffold); (2) the Oscillatoria agardhii agglutinin homolog (OAAH) lectin family (beta-barrel scaffold); (3) the legume lectin-like lectin family (beta-sandwich scaffold); (4) the Galanthus nivalis agglutinin (GNA)-like lectin family (beta-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. |
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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 (beta-prism I scaffold); (2) the Oscillatoria agardhii agglutinin homolog (OAAH) lectin family (beta-barrel scaffold); (3) the legume lectin-like lectin family (beta-sandwich scaffold); (4) the Galanthus nivalis agglutinin (GNA)-like lectin family (beta-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.</description><identifier>ISSN: 1660-3397</identifier><identifier>EISSN: 1660-3397</identifier><language>eng</language><publisher>MDPI</publisher><subject>anti-cancer properties ; anti-HIV-1 properties ; Biology and Life Sciences ; diagnostic tool ; lectin ; mannose-binding specificity ; red algae ; seaweed ; structure-function relationships ; therapeutic drugs</subject><creationdate>2019</creationdate><rights>Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) info:eu-repo/semantics/openAccess</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,315,780,784,4024,27860</link.rule.ids></links><search><creatorcontrib>Barre, A</creatorcontrib><creatorcontrib>Simplicien, M</creatorcontrib><creatorcontrib>Benoist, H</creatorcontrib><creatorcontrib>Van Damme, Els</creatorcontrib><creatorcontrib>Rougé, P</creatorcontrib><title>Mannose-Specific Lectins from Marine Algae: Diverse Structural Scaffolds Associated to Common Virucidal and Anti-Cancer Properties</title><description>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 (beta-prism I scaffold); (2) the Oscillatoria agardhii agglutinin homolog (OAAH) lectin family (beta-barrel scaffold); (3) the legume lectin-like lectin family (beta-sandwich scaffold); (4) the Galanthus nivalis agglutinin (GNA)-like lectin family (beta-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.</description><subject>anti-cancer properties</subject><subject>anti-HIV-1 properties</subject><subject>Biology and Life Sciences</subject><subject>diagnostic tool</subject><subject>lectin</subject><subject>mannose-binding specificity</subject><subject>red algae</subject><subject>seaweed</subject><subject>structure-function relationships</subject><subject>therapeutic drugs</subject><issn>1660-3397</issn><issn>1660-3397</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>ADGLB</sourceid><recordid>eNqdjs1KxDAUhYMoOP68w32BQjU2zrgrVXHhwEDFbbiT3nSupMlwk_oAPrkVXLh2dT4434FzolY3xtSV1pv70z98ri5y_qhr3aw3dyv1tcUYU6aqP5Jjzw5eyRWOGbykCbYoHAnaMCI9wCN_kmSCvsjsyiwYoHfofQpDhjbn5BgLDVASdGmaUoR3XkweFhHjAG0sXHUYHQnsJB1JClO-UmceQ6br37xUt89Pb91LNR4oFht4L-Sw2IRsUdxhOWHn8afak10b0-jG6H-NvgHVpF9M</recordid><startdate>2019</startdate><enddate>2019</enddate><creator>Barre, A</creator><creator>Simplicien, M</creator><creator>Benoist, H</creator><creator>Van Damme, Els</creator><creator>Rougé, P</creator><general>MDPI</general><scope>ADGLB</scope></search><sort><creationdate>2019</creationdate><title>Mannose-Specific Lectins from Marine Algae: Diverse Structural Scaffolds Associated to Common Virucidal and Anti-Cancer Properties</title><author>Barre, A ; Simplicien, M ; Benoist, H ; Van Damme, Els ; Rougé, P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-ghent_librecat_oai_archive_ugent_be_86653563</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>anti-cancer properties</topic><topic>anti-HIV-1 properties</topic><topic>Biology and Life Sciences</topic><topic>diagnostic tool</topic><topic>lectin</topic><topic>mannose-binding specificity</topic><topic>red algae</topic><topic>seaweed</topic><topic>structure-function relationships</topic><topic>therapeutic drugs</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Barre, A</creatorcontrib><creatorcontrib>Simplicien, M</creatorcontrib><creatorcontrib>Benoist, H</creatorcontrib><creatorcontrib>Van Damme, Els</creatorcontrib><creatorcontrib>Rougé, P</creatorcontrib><collection>Ghent University Academic Bibliography</collection></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Barre, A</au><au>Simplicien, M</au><au>Benoist, H</au><au>Van Damme, Els</au><au>Rougé, P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mannose-Specific Lectins from Marine Algae: Diverse Structural Scaffolds Associated to Common Virucidal and Anti-Cancer Properties</atitle><date>2019</date><risdate>2019</risdate><issn>1660-3397</issn><eissn>1660-3397</eissn><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 (beta-prism I scaffold); (2) the Oscillatoria agardhii agglutinin homolog (OAAH) lectin family (beta-barrel scaffold); (3) the legume lectin-like lectin family (beta-sandwich scaffold); (4) the Galanthus nivalis agglutinin (GNA)-like lectin family (beta-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.</abstract><pub>MDPI</pub><oa>free_for_read</oa></addata></record> |
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subjects | anti-cancer properties anti-HIV-1 properties Biology and Life Sciences diagnostic tool lectin mannose-binding specificity red algae seaweed structure-function relationships therapeutic drugs |
title | Mannose-Specific Lectins from Marine Algae: Diverse Structural Scaffolds Associated to Common Virucidal and Anti-Cancer Properties |
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