cDNA cloning and structural characterization of a lectin from the mussel Crenomytilus grayanus with a unique amino acid sequence and antibacterial activity
An amino acid sequence of GalNAc/Gal-specific lectin from the mussel Crenomytilus grayanus (CGL) was determined by cDNA sequencing. CGL consists of 150 amino acid residues, contains three tandem repeats with high sequence similarities to each other (up to 73%) and does not belong to any known lectin...
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Veröffentlicht in: | Fish & shellfish immunology 2013-10, Vol.35 (4), p.1320-1324 |
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container_title | Fish & shellfish immunology |
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creator | Kovalchuk, Svetlana N Chikalovets, Irina V Chernikov, Oleg V Molchanova, Valentina I Li, Wei Rasskazov, Valery A Lukyanov, Pavel A |
description | An amino acid sequence of GalNAc/Gal-specific lectin from the mussel Crenomytilus grayanus (CGL) was determined by cDNA sequencing. CGL consists of 150 amino acid residues, contains three tandem repeats with high sequence similarities to each other (up to 73%) and does not belong to any known lectins family. According to circular dichroism results CGL is a β/α-protein with the predominance of β-structure. CGL was predicted to adopt a ß-trefoil fold. The lectin exhibits antibacterial activity and might be involved in the recognition and clearance of bacterial pathogens in the shellfish. |
doi_str_mv | 10.1016/j.fsi.2013.07.011 |
format | Article |
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CGL consists of 150 amino acid residues, contains three tandem repeats with high sequence similarities to each other (up to 73%) and does not belong to any known lectins family. According to circular dichroism results CGL is a β/α-protein with the predominance of β-structure. CGL was predicted to adopt a ß-trefoil fold. 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All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c301t-125b97bf7aa74b56dad6b539afecc6ad52e680cfe63ddddac251702deb3f95f13</citedby><cites>FETCH-LOGICAL-c301t-125b97bf7aa74b56dad6b539afecc6ad52e680cfe63ddddac251702deb3f95f13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23886951$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kovalchuk, Svetlana N</creatorcontrib><creatorcontrib>Chikalovets, Irina V</creatorcontrib><creatorcontrib>Chernikov, Oleg V</creatorcontrib><creatorcontrib>Molchanova, Valentina I</creatorcontrib><creatorcontrib>Li, Wei</creatorcontrib><creatorcontrib>Rasskazov, Valery A</creatorcontrib><creatorcontrib>Lukyanov, Pavel A</creatorcontrib><title>cDNA cloning and structural characterization of a lectin from the mussel Crenomytilus grayanus with a unique amino acid sequence and antibacterial activity</title><title>Fish & shellfish immunology</title><addtitle>Fish Shellfish Immunol</addtitle><description>An amino acid sequence of GalNAc/Gal-specific lectin from the mussel Crenomytilus grayanus (CGL) was determined by cDNA sequencing. CGL consists of 150 amino acid residues, contains three tandem repeats with high sequence similarities to each other (up to 73%) and does not belong to any known lectins family. According to circular dichroism results CGL is a β/α-protein with the predominance of β-structure. CGL was predicted to adopt a ß-trefoil fold. The lectin exhibits antibacterial activity and might be involved in the recognition and clearance of bacterial pathogens in the shellfish.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Anti-Bacterial Agents - chemistry</subject><subject>Anti-Bacterial Agents - metabolism</subject><subject>Bacteria - drug effects</subject><subject>Bacteria - growth & development</subject><subject>Base Sequence</subject><subject>Circular Dichroism</subject><subject>Cloning, Molecular</subject><subject>DNA, Complementary - genetics</subject><subject>DNA, Complementary - metabolism</subject><subject>Lectins - chemistry</subject><subject>Lectins - genetics</subject><subject>Lectins - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Mytilidae - genetics</subject><subject>Mytilidae - metabolism</subject><subject>Mytilidae - microbiology</subject><subject>Phylogeny</subject><subject>Polymerase Chain Reaction</subject><subject>RNA, Messenger - genetics</subject><subject>RNA, Messenger - metabolism</subject><subject>Sequence Alignment</subject><issn>1050-4648</issn><issn>1095-9947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kU1v1DAQhi0Eoh_wA7ggH7kk2HHsrI_V8ilV7aU9WxNn3PUqsYvtUC1_hT-Lly3MZV6N5p13pIeQd5y1nHH1cd-67NuOcdGyoWWcvyDnnGnZaN0PL49asqZX_eaMXOS8Z4wpodhrctaJzUZpyc_Jb_vp5oraOQYfHiiEieaSVlvWBDO1O0hgCyb_C4qPgUZHgc5oiw_UpbjQskO6rDnjTLcJQ1wOxc9rpg8JDhCqePJlVz1r8D9WpLD4EClYX2OwDoLFv5kQih9PSTW2Cv_Tl8Mb8srBnPHtc78k918-322_Nde3X79vr64bKxgvDe_kqIfRDQBDP0o1waRGKTQ4tFbBJDtUG2YdKjHVAttJPrBuwlE4LR0Xl-TD6e5jivWpXMzis8V5hoBxzYb3gndaanVc5adVm2LOCZ15TH6BdDCcmSMTszeViTkyMWwwlUn1vH8-v44LTv8d_yCIP1uIjao</recordid><startdate>20131001</startdate><enddate>20131001</enddate><creator>Kovalchuk, Svetlana N</creator><creator>Chikalovets, Irina V</creator><creator>Chernikov, Oleg V</creator><creator>Molchanova, Valentina I</creator><creator>Li, Wei</creator><creator>Rasskazov, Valery A</creator><creator>Lukyanov, Pavel A</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20131001</creationdate><title>cDNA cloning and structural characterization of a lectin from the mussel Crenomytilus grayanus with a unique amino acid sequence and antibacterial activity</title><author>Kovalchuk, Svetlana N ; 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subjects | Amino Acid Sequence Animals Anti-Bacterial Agents - chemistry Anti-Bacterial Agents - metabolism Bacteria - drug effects Bacteria - growth & development Base Sequence Circular Dichroism Cloning, Molecular DNA, Complementary - genetics DNA, Complementary - metabolism Lectins - chemistry Lectins - genetics Lectins - metabolism Molecular Sequence Data Mytilidae - genetics Mytilidae - metabolism Mytilidae - microbiology Phylogeny Polymerase Chain Reaction RNA, Messenger - genetics RNA, Messenger - metabolism Sequence Alignment |
title | cDNA cloning and structural characterization of a lectin from the mussel Crenomytilus grayanus with a unique amino acid sequence and antibacterial activity |
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