Glycan‐based high‐affinity ligands for toxins and pathogen receptors
Identifieur interne : 001615 ( Istex/Corpus ); précédent : 001614; suivant : 001616Glycan‐based high‐affinity ligands for toxins and pathogen receptors
Auteurs : Ashish A. Kulkarni ; Alison A. Weiss ; Suri S. IyerSource :
- Medicinal Research Reviews [ 0198-6325 ] ; 2010-03.
Abstract
Glycans decorate over 95% of the mammalian cell surface in the form of glycolipids and glycoproteins. Several toxins and pathogens bind to these glycans to enter the cells. Understanding the fundamentals of the complex interplay between microbial pathogens and their glycan receptors at the molecular level could lead to the development of novel therapeutics and diagnostics. Using Shiga toxin and influenza virus as examples, we describe the complex biological interface between host glycans and these infectious agents, and recent strategies to develop glycan‐based high‐affinity ligands. These molecules are expected to ultimately be incorporated into diagnostics and therapeutics, and can be used as probes to study important biological processes. Additionally, by focusing on the specific glycans that microbial pathogens target, we can begin to decipher the “glycocode” and how these glycans participate in normal and aberrant cellular communication. © 2010 Wiley Periodicals, Inc. Med Res Rev, 30, No. 2, 327–393, 2010
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DOI: 10.1002/med.20196
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<ref target="http://www.tei-c.org/">We use TEI</ref></desc></application></appInfo></encodingDesc><profileDesc><abstract xml:lang="en" style="main"><head>Abstract</head><p>Glycans decorate over 95% of the mammalian cell surface in the form of glycolipids and glycoproteins. Several toxins and pathogens bind to these glycans to enter the cells. Understanding the fundamentals of the complex interplay between microbial pathogens and their glycan receptors at the molecular level could lead to the development of novel therapeutics and diagnostics. Using Shiga toxin and influenza virus as examples, we describe the complex biological interface between host glycans and these infectious agents, and recent strategies to develop glycan‐based high‐affinity ligands. These molecules are expected to ultimately be incorporated into diagnostics and therapeutics, and can be used as probes to study important biological processes. Additionally, by focusing on the specific glycans that microbial pathogens target, we can begin to decipher the “glycocode” and how these glycans participate in normal and aberrant cellular communication. © 2010 Wiley Periodicals, Inc. Med Res Rev, 30, No. 2, 327–393, 2010</p></abstract><textClass><keywords xml:lang="en"><term xml:id="kwd1">shiga</term><term xml:id="kwd2">glycan</term><term xml:id="kwd3">recognition</term><term xml:id="kwd4">influenza</term><term xml:id="kwd5">protein–glycan specificity</term></keywords></textClass><langUsage><language ident="en"></language></langUsage></profileDesc><revisionDesc><change when="2019-12-20" who="#istex" xml:id="pub2tei">formatting</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/WNG-CT8FZ6Q6-V/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component version="2.0" type="serialArticle" xml:lang="en"><header><publicationMeta level="product"><publisherInfo><publisherName>Wiley Subscription Services, Inc., A Wiley Company</publisherName><publisherLoc>Hoboken</publisherLoc></publisherInfo><doi registered="yes">10.1002/(ISSN)1098-1128</doi><issn type="print">0198-6325</issn><issn type="electronic">1098-1128</issn><idGroup><id type="product" value="MED"></id></idGroup><titleGroup><title type="main" xml:lang="en" sort="MEDICINAL RESEARCH REVIEWS">Medicinal Research Reviews</title><title type="short">Med. 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Rev.</title></titleGroup></publicationMeta><publicationMeta level="part" position="20"><doi origin="wiley" registered="yes">10.1002/med.v30:2</doi><titleGroup><title type="specialIssueTitle">Special Issue on Carbohydrate Recognition and Applications</title></titleGroup><numberingGroup><numbering type="journalVolume" number="30">30</numbering><numbering type="journalIssue">2</numbering></numberingGroup><creators><creator xml:id="sped1" creatorRole="sponsoringEditor"><personName><givenNames>Xue‐Long</givenNames><familyName>Sun</familyName></personName></creator></creators><coverDate startDate="2010-03">March 2010</coverDate></publicationMeta><publicationMeta level="unit" type="reviewArticle" position="6" status="forIssue"><doi origin="wiley" registered="yes">10.1002/med.20196</doi><idGroup><id type="unit" value="MED20196"></id></idGroup><countGroup><count type="pageTotal" number="67"></count></countGroup><copyright ownership="publisher">© 2010 Wiley Periodicals, Inc.</copyright><eventGroup><event type="publishedOnlineEarlyUnpaginated" date="2010-02-04"></event><event type="firstOnline" date="2010-02-04"></event><event type="publishedOnlineFinalForm" date="2010-02-18"></event><event type="xmlConverted" agent="Converter:JWSART34_TO_WML3G version:2.3.2 mode:FullText source:FullText result:FullText mathml2tex" date="2010-03-04"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.8.8" date="2014-02-02"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.1.7 mode:FullText,remove_FC" date="2014-10-31"></event></eventGroup><numberingGroup><numbering type="pageFirst">327</numbering><numbering type="pageLast">393</numbering></numberingGroup><correspondenceTo>UC Chemical and Biosensors Group, Department of Chemistry, Cincinnati, OH 45221‐0172</correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:MED.MED20196.pdf"></link></linkGroup></publicationMeta><contentMeta><countGroup><count type="figureTotal" number="9"></count><count type="tableTotal" number="6"></count><count type="referenceTotal" number="309"></count></countGroup><titleGroup><title type="main" xml:lang="en">Glycan‐based high‐affinity ligands for toxins and pathogen receptors</title><title type="short" xml:lang="en">GLYCAN‐BASED HIGH‐AFFINITY LIGANDS</title></titleGroup><creators><creator xml:id="au1" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Ashish A.</givenNames><familyName>Kulkarni</familyName></personName></creator><creator xml:id="au2" creatorRole="author" affiliationRef="#af2"><personName><givenNames>Alison A.</givenNames><familyName>Weiss</familyName></personName></creator><creator xml:id="au3" creatorRole="author" affiliationRef="#af1" corresponding="yes"><personName><givenNames>Suri S.</givenNames><familyName>Iyer</familyName></personName><contactDetails><email>suri.iyer@uc.edu</email></contactDetails></creator></creators><affiliationGroup><affiliation xml:id="af1" countryCode="US" type="organization"><unparsedAffiliation>UC Chemical and Biosensors Group, Department of Chemistry, University of Cincinnati, Cincinnati, Ohio</unparsedAffiliation></affiliation><affiliation xml:id="af2" countryCode="US" type="organization"><unparsedAffiliation>Department of Molecular Genetics, Biochemistry and Microbiology, University of Cincinnati, Cincinnati, Ohio</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en" type="author"><keyword xml:id="kwd1">shiga</keyword><keyword xml:id="kwd2">glycan</keyword><keyword xml:id="kwd3">recognition</keyword><keyword xml:id="kwd4">influenza</keyword><keyword xml:id="kwd5">protein–glycan specificity</keyword></keywordGroup><fundingInfo><fundingAgency>NSF</fundingAgency><fundingNumber>CAREER CHE‐0845005</fundingNumber></fundingInfo><fundingInfo><fundingAgency>UC Nanotechnology Institute</fundingAgency></fundingInfo><fundingInfo><fundingAgency>NIAID</fundingAgency><fundingNumber>U01‐AI075498</fundingNumber></fundingInfo><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>Glycans decorate over 95% of the mammalian cell surface in the form of glycolipids and glycoproteins. Several toxins and pathogens bind to these glycans to enter the cells. Understanding the fundamentals of the complex interplay between microbial pathogens and their glycan receptors at the molecular level could lead to the development of novel therapeutics and diagnostics. Using Shiga toxin and influenza virus as examples, we describe the complex biological interface between host glycans and these infectious agents, and recent strategies to develop glycan‐based high‐affinity ligands. These molecules are expected to ultimately be incorporated into diagnostics and therapeutics, and can be used as probes to study important biological processes. Additionally, by focusing on the specific glycans that microbial pathogens target, we can begin to decipher the “glycocode” and how these glycans participate in normal and aberrant cellular communication. © 2010 Wiley Periodicals, Inc. Med Res Rev, 30, No. 2, 327–393, 2010</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Glycan‐based high‐affinity ligands for toxins and pathogen receptors</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>GLYCAN‐BASED HIGH‐AFFINITY LIGANDS</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Glycan‐based high‐affinity ligands for toxins and pathogen receptors</title></titleInfo><name type="personal"><namePart type="given">Ashish A.</namePart><namePart type="family">Kulkarni</namePart><affiliation>UC Chemical and Biosensors Group, Department of Chemistry, University of Cincinnati, Cincinnati, Ohio</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Alison A.</namePart><namePart type="family">Weiss</namePart><affiliation>Department of Molecular Genetics, Biochemistry and Microbiology, University of Cincinnati, Cincinnati, Ohio</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Suri S.</namePart><namePart type="family">Iyer</namePart><affiliation>UC Chemical and Biosensors Group, Department of Chemistry, University of Cincinnati, Cincinnati, Ohio</affiliation><affiliation>E-mail: suri.iyer@uc.edu</affiliation><affiliation>Correspondence address: UC Chemical and Biosensors Group, Department of Chemistry, Cincinnati, OH 45221‐0172</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="review-article" displayLabel="reviewArticle" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-L5L7X3NF-P">review-article</genre><originInfo><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><place><placeTerm type="text">Hoboken</placeTerm></place><dateIssued encoding="w3cdtf">2010-03</dateIssued><copyrightDate encoding="w3cdtf">2010</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><extent unit="figures">9</extent><extent unit="tables">6</extent><extent unit="references">309</extent></physicalDescription><abstract lang="en">Glycans decorate over 95% of the mammalian cell surface in the form of glycolipids and glycoproteins. Several toxins and pathogens bind to these glycans to enter the cells. Understanding the fundamentals of the complex interplay between microbial pathogens and their glycan receptors at the molecular level could lead to the development of novel therapeutics and diagnostics. Using Shiga toxin and influenza virus as examples, we describe the complex biological interface between host glycans and these infectious agents, and recent strategies to develop glycan‐based high‐affinity ligands. These molecules are expected to ultimately be incorporated into diagnostics and therapeutics, and can be used as probes to study important biological processes. Additionally, by focusing on the specific glycans that microbial pathogens target, we can begin to decipher the “glycocode” and how these glycans participate in normal and aberrant cellular communication. © 2010 Wiley Periodicals, Inc. Med Res Rev, 30, No. 2, 327–393, 2010</abstract><note type="funding">NSF - No. CAREER CHE‐0845005; </note><note type="funding">UC Nanotechnology Institute</note><note type="funding">NIAID - No. U01‐AI075498; </note><subject lang="en"><genre>keywords</genre><topic>shiga</topic><topic>glycan</topic><topic>recognition</topic><topic>influenza</topic><topic>protein–glycan specificity</topic></subject><relatedItem type="host"><titleInfo><title>Medicinal Research Reviews</title></titleInfo><titleInfo type="abbreviated"><title>Med. Res. 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