(Strept)avidin Binds Glycoconjugates
Fluorescently labeled and conjugated (strept)avidins are widely used for imaging biotinylated molecules in immunological assays and histochemistry. We showed that besides biotin, these proteins bind glycans, including fragments of mammalian glycoproteins and glycolipids, in particular, ABO blood gro...
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Veröffentlicht in: | Biochemistry (Moscow) 2024-11, Vol.89 (11), p.2023-2027 |
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container_title | Biochemistry (Moscow) |
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creator | Shilova, Nadezhda V. Polyakova, Svetlana M. Nokel, Alexey Yu Lipatnikov, Alexander D. Gordeeva, Elena A. Lavrenteva, Marina V. Bovin, Nicolai V. |
description | Fluorescently labeled and conjugated (strept)avidins are widely used for imaging biotinylated molecules in immunological assays and histochemistry. We showed that besides biotin, these proteins bind glycans, including fragments of mammalian glycoproteins and glycolipids, in particular, ABO blood group antigens, oligolactosamines, and 6-
O
-sulfated oligosaccharides. This interaction is inhibited in a dose-dependent manner by micromolar concentrations of polymeric, but not monomeric, glycan conjugates (i.e., requires polyvalence). Taking into account the cluster organization of cell glycans (glycoproteins and glycolipids), the ability of (strept)avidins to bind glycans might be a source of errors in the analysis of carbohydrate-containing samples, which can be prevented by avoiding a large excess of (strept)avidin in analytical systems. |
doi_str_mv | 10.1134/S0006297924110142 |
format | Article |
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O
-sulfated oligosaccharides. This interaction is inhibited in a dose-dependent manner by micromolar concentrations of polymeric, but not monomeric, glycan conjugates (i.e., requires polyvalence). Taking into account the cluster organization of cell glycans (glycoproteins and glycolipids), the ability of (strept)avidins to bind glycans might be a source of errors in the analysis of carbohydrate-containing samples, which can be prevented by avoiding a large excess of (strept)avidin in analytical systems.</description><identifier>ISSN: 0006-2979</identifier><identifier>ISSN: 1608-3040</identifier><identifier>EISSN: 1608-3040</identifier><identifier>DOI: 10.1134/S0006297924110142</identifier><identifier>PMID: 39647829</identifier><language>eng</language><publisher>Moscow: Pleiades Publishing</publisher><subject>ABO system ; Animals ; Antigens ; Avidin ; Avidin - chemistry ; Avidin - metabolism ; Biochemistry ; Biomedical and Life Sciences ; Biomedicine ; Bioorganic Chemistry ; Biotin ; Biotin - chemistry ; Biotin - metabolism ; Blood groups ; Carbohydrates ; Glycan ; Glycoconjugates ; Glycoconjugates - chemistry ; Glycoconjugates - metabolism ; Glycolipids ; Glycolipids - chemistry ; Glycolipids - metabolism ; Glycoproteins ; Glycoproteins - chemistry ; Glycoproteins - metabolism ; Histochemistry ; Humans ; Humidity ; Immunology ; Integrated circuits ; Internet resources ; Life Sciences ; Ligands ; Microbiology ; Oligosaccharides ; Polysaccharides ; Polysaccharides - chemistry ; Polysaccharides - metabolism ; Protein Binding</subject><ispartof>Biochemistry (Moscow), 2024-11, Vol.89 (11), p.2023-2027</ispartof><rights>Pleiades Publishing, Ltd. 2024</rights><rights>Copyright Springer Nature B.V. Nov 2024</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1134/S0006297924110142$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1134/S0006297924110142$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/39647829$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shilova, Nadezhda V.</creatorcontrib><creatorcontrib>Polyakova, Svetlana M.</creatorcontrib><creatorcontrib>Nokel, Alexey Yu</creatorcontrib><creatorcontrib>Lipatnikov, Alexander D.</creatorcontrib><creatorcontrib>Gordeeva, Elena A.</creatorcontrib><creatorcontrib>Lavrenteva, Marina V.</creatorcontrib><creatorcontrib>Bovin, Nicolai V.</creatorcontrib><title>(Strept)avidin Binds Glycoconjugates</title><title>Biochemistry (Moscow)</title><addtitle>Biochemistry Moscow</addtitle><addtitle>Biochemistry (Mosc)</addtitle><description>Fluorescently labeled and conjugated (strept)avidins are widely used for imaging biotinylated molecules in immunological assays and histochemistry. We showed that besides biotin, these proteins bind glycans, including fragments of mammalian glycoproteins and glycolipids, in particular, ABO blood group antigens, oligolactosamines, and 6-
O
-sulfated oligosaccharides. This interaction is inhibited in a dose-dependent manner by micromolar concentrations of polymeric, but not monomeric, glycan conjugates (i.e., requires polyvalence). Taking into account the cluster organization of cell glycans (glycoproteins and glycolipids), the ability of (strept)avidins to bind glycans might be a source of errors in the analysis of carbohydrate-containing samples, which can be prevented by avoiding a large excess of (strept)avidin in analytical systems.</description><subject>ABO system</subject><subject>Animals</subject><subject>Antigens</subject><subject>Avidin</subject><subject>Avidin - chemistry</subject><subject>Avidin - metabolism</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Bioorganic Chemistry</subject><subject>Biotin</subject><subject>Biotin - chemistry</subject><subject>Biotin - metabolism</subject><subject>Blood groups</subject><subject>Carbohydrates</subject><subject>Glycan</subject><subject>Glycoconjugates</subject><subject>Glycoconjugates - chemistry</subject><subject>Glycoconjugates - metabolism</subject><subject>Glycolipids</subject><subject>Glycolipids - chemistry</subject><subject>Glycolipids - metabolism</subject><subject>Glycoproteins</subject><subject>Glycoproteins - chemistry</subject><subject>Glycoproteins - metabolism</subject><subject>Histochemistry</subject><subject>Humans</subject><subject>Humidity</subject><subject>Immunology</subject><subject>Integrated circuits</subject><subject>Internet resources</subject><subject>Life Sciences</subject><subject>Ligands</subject><subject>Microbiology</subject><subject>Oligosaccharides</subject><subject>Polysaccharides</subject><subject>Polysaccharides - chemistry</subject><subject>Polysaccharides - metabolism</subject><subject>Protein Binding</subject><issn>0006-2979</issn><issn>1608-3040</issn><issn>1608-3040</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNplkE1Lw0AQhhdRbK3-AC9S0EM9RHd3NrPZoxatQsFD9Rw2u5uSkC-zidB_b0Irgp6G4Xl4mXkJuWT0jjEQ9xtKKXIlFReMUSb4EZkypFEAVNBjMh1xMPIJOfM-H1ZOFZySCSgUMuJqSm4Wm651TXervzKbVfPHrLJ-vip2pjZ1lfdb3Tl_Tk5SXXh3cZgz8vH89L58CdZvq9flwzpoGAIEoXVgUCRCKYoGIy1UIqVhJrEpJmnolLASjUCl0jA1yK2mnKchGAFSRwAzstjnNm392TvfxWXmjSsKXbm69zEwgWHEQchBvf6j5nXfVsN1o8UwQhaOgVcHq09KZ-OmzUrd7uKf_weB7wU_oGrr2t8YRuOx5PhfyfANf8VpRA</recordid><startdate>20241101</startdate><enddate>20241101</enddate><creator>Shilova, Nadezhda V.</creator><creator>Polyakova, Svetlana M.</creator><creator>Nokel, Alexey Yu</creator><creator>Lipatnikov, Alexander D.</creator><creator>Gordeeva, Elena A.</creator><creator>Lavrenteva, Marina V.</creator><creator>Bovin, Nicolai V.</creator><general>Pleiades Publishing</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QL</scope><scope>7TM</scope><scope>7U9</scope><scope>C1K</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>7X8</scope></search><sort><creationdate>20241101</creationdate><title>(Strept)avidin Binds Glycoconjugates</title><author>Shilova, Nadezhda V. ; 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We showed that besides biotin, these proteins bind glycans, including fragments of mammalian glycoproteins and glycolipids, in particular, ABO blood group antigens, oligolactosamines, and 6-
O
-sulfated oligosaccharides. This interaction is inhibited in a dose-dependent manner by micromolar concentrations of polymeric, but not monomeric, glycan conjugates (i.e., requires polyvalence). Taking into account the cluster organization of cell glycans (glycoproteins and glycolipids), the ability of (strept)avidins to bind glycans might be a source of errors in the analysis of carbohydrate-containing samples, which can be prevented by avoiding a large excess of (strept)avidin in analytical systems.</abstract><cop>Moscow</cop><pub>Pleiades Publishing</pub><pmid>39647829</pmid><doi>10.1134/S0006297924110142</doi><tpages>5</tpages></addata></record> |
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subjects | ABO system Animals Antigens Avidin Avidin - chemistry Avidin - metabolism Biochemistry Biomedical and Life Sciences Biomedicine Bioorganic Chemistry Biotin Biotin - chemistry Biotin - metabolism Blood groups Carbohydrates Glycan Glycoconjugates Glycoconjugates - chemistry Glycoconjugates - metabolism Glycolipids Glycolipids - chemistry Glycolipids - metabolism Glycoproteins Glycoproteins - chemistry Glycoproteins - metabolism Histochemistry Humans Humidity Immunology Integrated circuits Internet resources Life Sciences Ligands Microbiology Oligosaccharides Polysaccharides Polysaccharides - chemistry Polysaccharides - metabolism Protein Binding |
title | (Strept)avidin Binds Glycoconjugates |
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