Probing the conformational and dynamical effects of O‐glycosylation within the immunodominant region of a MUC1 peptide tumor antigen
Identifieur interne : 000811 ( Istex/Corpus ); précédent : 000810; suivant : 000812Probing the conformational and dynamical effects of O‐glycosylation within the immunodominant region of a MUC1 peptide tumor antigen
Auteurs : J. Schuman ; A. P. Campbell ; R. R. Koganty ; B. M. LongeneckerSource :
- The Journal of Peptide Research [ 1397-002X ] ; 2003-03.
Abstract
Abstract: MUC1 mucin is a large transmembrane glycoprotein, the extracellular domain of which is formed by a repeating 20 amino acid sequence, GVTSAPDTRPAPGSTAPPAH. In normal breast epithelial cells, the extracellular domain is densely covered with highly branched complex carbohydrate structures. However, in neoplastic breast tissue, the extracellular domain is under‐glycosylated, resulting in the exposure of a highly immunogenic core peptide epitope (PDTRP in bold above), as well as in the exposure of normally cryptic core Tn (GalNAc), STn (sialyl α2–6 GalNAc) and TF (Gal β1–3 GalNAc) carbohydrates. Here, we report the results of 1H NMR structural studies, natural abundance 13C NMR relaxation measurements and distance‐restrained MD simulations designed to probe the structural and dynamical effects of Tn‐glycosylation within the PDTRP core peptide epitope. Two synthetic peptides were studied: a nine‐residue MUC1 peptide of the sequence, Thr1‐Ser2‐Ala3‐Pro4‐Asp5‐Thr6‐Arg7‐Pro8‐Ala9, and a Tn‐glycosylated version of this peptide, Thr1‐Ser2‐Ala3‐Pro4‐Asp5‐Thr6(αGalNAc)‐Arg7‐Pro8‐Ala9. The results of these studies show that a type I β‐turn conformation is adopted by residues PDTR within the PDTRP region of the unglycosylated MUC1 sequence. The existence of a similar β‐turn within the PDTRP core peptide epitope of the under‐glycosylated cancer‐associated MUC1 mucin protein might explain the immunodominance of this region in vivo, as the presence of defined secondary structure within peptide epitope regions has been correlated with increased immunogenicity in other systems. Our results have also shown that Tn glycosylation at the central threonine within the PDTRP core epitope region shifts the conformational equilibrium away from the type I β‐turn conformation and toward a more rigid and extended state. The significance of these results are discussed in relation to the possible roles that peptide epitope secondary structure and glycosylation state may play in MUC1 tumor immunogenicity.
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DOI: 10.1034/j.1399-3011.2003.00031.x
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<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Probing the conformational and dynamical effects of O‐glycosylation within the immunodominant region of a MUC1 peptide tumor antigen</title><author><name sortKey="Schuman, J" sort="Schuman, J" uniqKey="Schuman J" first="J." last="Schuman">J. Schuman</name><affiliation><mods:affiliation>Department of Medicinal Chemistry, School of Pharmacy, University of Washington, Seattle, USA.</mods:affiliation></affiliation></author><author><name sortKey="Campbell, A P" sort="Campbell, A P" uniqKey="Campbell A" first="A. P." last="Campbell">A. P. Campbell</name><affiliation><mods:affiliation>Department of Medicinal Chemistry, School of Pharmacy, University of Washington, Seattle, USA.</mods:affiliation></affiliation></author><author><name sortKey="Koganty, R R" sort="Koganty, R R" uniqKey="Koganty R" first="R. R." last="Koganty">R. R. 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Longenecker</name><affiliation><mods:affiliation>Biomira Inc., Edmonton, Canada.</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:DCA1BD36E323CD65E77A2DE79D090E336A6E0908</idno><date when="2003" year="2003">2003</date><idno type="doi">10.1034/j.1399-3011.2003.00031.x</idno><idno type="url">https://api.istex.fr/ark:/67375/WNG-VLV2BX4F-0/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000811</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000811</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main">Probing the conformational and dynamical effects of O‐glycosylation within the immunodominant region of a MUC1 peptide tumor antigen</title><author><name sortKey="Schuman, J" sort="Schuman, J" uniqKey="Schuman J" first="J." last="Schuman">J. Schuman</name><affiliation><mods:affiliation>Department of Medicinal Chemistry, School of Pharmacy, University of Washington, Seattle, USA.</mods:affiliation></affiliation></author><author><name sortKey="Campbell, A P" sort="Campbell, A P" uniqKey="Campbell A" first="A. P." last="Campbell">A. P. Campbell</name><affiliation><mods:affiliation>Department of Medicinal Chemistry, School of Pharmacy, University of Washington, Seattle, USA.</mods:affiliation></affiliation></author><author><name sortKey="Koganty, R R" sort="Koganty, R R" uniqKey="Koganty R" first="R. R." last="Koganty">R. R. Koganty</name><affiliation><mods:affiliation>Biomira Inc., Edmonton, Canada.</mods:affiliation></affiliation></author><author><name sortKey="Longenecker, B M" sort="Longenecker, B M" uniqKey="Longenecker B" first="B. M." last="Longenecker">B. M. Longenecker</name><affiliation><mods:affiliation>Biomira Inc., Edmonton, Canada.</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">The Journal of Peptide Research</title><title level="j" type="alt">JOURNAL OF PEPTIDE RESEARCH</title><idno type="ISSN">1397-002X</idno><idno type="eISSN">1399-3011</idno><imprint><biblScope unit="vol">61</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="91">91</biblScope><biblScope unit="page" to="108">108</biblScope><biblScope unit="page-count">18</biblScope><publisher>Munksgaard International Publishers</publisher><pubPlace>Oxford, UK</pubPlace><date type="published" when="2003-03">2003-03</date></imprint><idno type="ISSN">1397-002X</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1397-002X</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: MUC1 mucin is a large transmembrane glycoprotein, the extracellular domain of which is formed by a repeating 20 amino acid sequence, GVTSAPDTRPAPGSTAPPAH. In normal breast epithelial cells, the extracellular domain is densely covered with highly branched complex carbohydrate structures. However, in neoplastic breast tissue, the extracellular domain is under‐glycosylated, resulting in the exposure of a highly immunogenic core peptide epitope (PDTRP in bold above), as well as in the exposure of normally cryptic core Tn (GalNAc), STn (sialyl α2–6 GalNAc) and TF (Gal β1–3 GalNAc) carbohydrates. Here, we report the results of 1H NMR structural studies, natural abundance 13C NMR relaxation measurements and distance‐restrained MD simulations designed to probe the structural and dynamical effects of Tn‐glycosylation within the PDTRP core peptide epitope. Two synthetic peptides were studied: a nine‐residue MUC1 peptide of the sequence, Thr1‐Ser2‐Ala3‐Pro4‐Asp5‐Thr6‐Arg7‐Pro8‐Ala9, and a Tn‐glycosylated version of this peptide, Thr1‐Ser2‐Ala3‐Pro4‐Asp5‐Thr6(αGalNAc)‐Arg7‐Pro8‐Ala9. The results of these studies show that a type I β‐turn conformation is adopted by residues PDTR within the PDTRP region of the unglycosylated MUC1 sequence. The existence of a similar β‐turn within the PDTRP core peptide epitope of the under‐glycosylated cancer‐associated MUC1 mucin protein might explain the immunodominance of this region in vivo, as the presence of defined secondary structure within peptide epitope regions has been correlated with increased immunogenicity in other systems. Our results have also shown that Tn glycosylation at the central threonine within the PDTRP core epitope region shifts the conformational equilibrium away from the type I β‐turn conformation and toward a more rigid and extended state. The significance of these results are discussed in relation to the possible roles that peptide epitope secondary structure and glycosylation state may play in MUC1 tumor immunogenicity.</div></front></TEI><istex><corpusName>wiley</corpusName><keywords><teeft><json:string>muc1</json:string><json:string>peptide</json:string><json:string>unglycosylated</json:string><json:string>glycosylation</json:string><json:string>thr6</json:string><json:string>asp5</json:string><json:string>epitope</json:string><json:string>mucin</json:string><json:string>arg7</json:string><json:string>muc1 peptide</json:string><json:string>pdtrp</json:string><json:string>chem</json:string><json:string>galnac</json:string><json:string>glycosylated</json:string><json:string>conformation</json:string><json:string>immunogenicity</json:string><json:string>biol</json:string><json:string>noesy</json:string><json:string>connectivity</json:string><json:string>carbohydrate</json:string><json:string>3jna</json:string><json:string>conformational equilibrium</json:string><json:string>receptor</json:string><json:string>peptide backbone</json:string><json:string>glycopeptide</json:string><json:string>dihedral</json:string><json:string>ddha</json:string><json:string>datum</json:string><json:string>pro8</json:string><json:string>temperature coefficient</json:string><json:string>chemical shift</json:string><json:string>noesy spectrum</json:string><json:string>ddca</json:string><json:string>pro4</json:string><json:string>trans</json:string><json:string>conformational</json:string><json:string>steric</json:string><json:string>biochemistry</json:string><json:string>isomer</json:string><json:string>dqfcosy</json:string><json:string>ala3</json:string><json:string>fontenot</json:string><json:string>proline</json:string><json:string>threonine</json:string><json:string>unglycosylated muc1 peptide</json:string><json:string>relaxation datum</json:string><json:string>hydrogen bond</json:string><json:string>pdtrp region</json:string><json:string>dihedral space</json:string><json:string>muc1 mucin</json:string><json:string>side chain</json:string><json:string>natural abundance</json:string><json:string>relaxation time</json:string><json:string>random coil</json:string><json:string>standard deviation</json:string><json:string>random coil value</json:string><json:string>proton</json:string><json:string>schuman</json:string><json:string>pdtrp core peptide epitope</json:string><json:string>trans isomer</json:string><json:string>pdtrp core epitope region</json:string><json:string>solvent shielding</json:string><json:string>dqfcosy spectrum</json:string><json:string>crystal structure</json:string><json:string>side chain mobility</json:string><json:string>extracellular domain</json:string><json:string>residue</json:string><json:string>backbone</json:string><json:string>simulation</json:string><json:string>amino</json:string><json:string>glycosylation shift</json:string><json:string>muc1 tumor immunogenicity</json:string><json:string>second residue</json:string><json:string>glycosylation state</json:string><json:string>datum set</json:string><json:string>backbone dynamic</json:string><json:string>glycosylation site</json:string><json:string>relaxation measurement</json:string><json:string>ddca value</json:string><json:string>chemical shift deviation</json:string><json:string>protein structure</json:string><json:string>strong corresponding</json:string><json:string>final structure</json:string><json:string>sialyl galnac</json:string><json:string>receptor binding</json:string><json:string>natl acad</json:string><json:string>muc1 tandem</json:string><json:string>local effect</json:string><json:string>muc1 figure</json:string><json:string>dynamical effect</json:string><json:string>secondary structure</json:string></teeft></keywords><author><json:item><name>J. Schuman</name><affiliations><json:string>Department of Medicinal Chemistry, School of Pharmacy, University of Washington, Seattle, USA.</json:string></affiliations></json:item><json:item><name>A.P. Campbell</name><affiliations><json:string>Department of Medicinal Chemistry, School of Pharmacy, University of Washington, Seattle, USA.</json:string></affiliations></json:item><json:item><name>R.R. Koganty</name><affiliations><json:string>Biomira Inc., Edmonton, Canada.</json:string></affiliations></json:item><json:item><name>B.M. Longenecker</name><affiliations><json:string>Biomira Inc., Edmonton, Canada.</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>cancer</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>epitope</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>glycosylation</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>MD</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>mucin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>MUC1</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>NMR</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>peptide</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>tumor</value></json:item></subject><articleId><json:string>CBDD031</json:string></articleId><arkIstex>ark:/67375/WNG-VLV2BX4F-0</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>article</json:string></originalGenre><abstract>Abstract: MUC1 mucin is a large transmembrane glycoprotein, the extracellular domain of which is formed by a repeating 20 amino acid sequence, GVTSAPDTRPAPGSTAPPAH. In normal breast epithelial cells, the extracellular domain is densely covered with highly branched complex carbohydrate structures. However, in neoplastic breast tissue, the extracellular domain is under‐glycosylated, resulting in the exposure of a highly immunogenic core peptide epitope (PDTRP in bold above), as well as in the exposure of normally cryptic core Tn (GalNAc), STn (sialyl α2–6 GalNAc) and TF (Gal β1–3 GalNAc) carbohydrates. Here, we report the results of 1H NMR structural studies, natural abundance 13C NMR relaxation measurements and distance‐restrained MD simulations designed to probe the structural and dynamical effects of Tn‐glycosylation within the PDTRP core peptide epitope. Two synthetic peptides were studied: a nine‐residue MUC1 peptide of the sequence, Thr1‐Ser2‐Ala3‐Pro4‐Asp5‐Thr6‐Arg7‐Pro8‐Ala9, and a Tn‐glycosylated version of this peptide, Thr1‐Ser2‐Ala3‐Pro4‐Asp5‐Thr6(αGalNAc)‐Arg7‐Pro8‐Ala9. The results of these studies show that a type I β‐turn conformation is adopted by residues PDTR within the PDTRP region of the unglycosylated MUC1 sequence. The existence of a similar β‐turn within the PDTRP core peptide epitope of the under‐glycosylated cancer‐associated MUC1 mucin protein might explain the immunodominance of this region in vivo, as the presence of defined secondary structure within peptide epitope regions has been correlated with increased immunogenicity in other systems. Our results have also shown that Tn glycosylation at the central threonine within the PDTRP core epitope region shifts the conformational equilibrium away from the type I β‐turn conformation and toward a more rigid and extended state. The significance of these results are discussed in relation to the possible roles that peptide epitope secondary structure and glycosylation state may play in MUC1 tumor immunogenicity.</abstract><qualityIndicators><score>10</score><pdfWordCount>9831</pdfWordCount><pdfCharCount>62816</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>18</pdfPageCount><pdfPageSize>595 x 782 pts</pdfPageSize><pdfWordsPerPage>546</pdfWordsPerPage><pdfText>true</pdfText><refBibsNative>true</refBibsNative><abstractWordCount>278</abstractWordCount><abstractCharCount>2015</abstractCharCount><keywordCount>9</keywordCount></qualityIndicators><title>Probing the conformational and dynamical effects of O‐glycosylation within the immunodominant region of a MUC1 peptide tumor antigen</title><pmid><json:string>12558945</json:string></pmid><genre><json:string>article</json:string></genre><host><title>The Journal of Peptide Research</title><language><json:string>unknown</json:string></language><doi><json:string>10.1111/(ISSN)1399-3011</json:string></doi><issn><json:string>1397-002X</json:string></issn><eissn><json:string>1399-3011</json:string></eissn><publisherId><json:string>CBDD</json:string></publisherId><volume>61</volume><issue>3</issue><pages><first>91</first><last>108</last><total>18</total></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>3750</json:string><json:string>2003</json:string></date><geogName></geogName><orgName><json:string>Army Breast Cancer Grant</json:string><json:string>University of Alberta</json:string><json:string>University of Washington</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName><json:string>R. Boyko</json:string><json:string>Kirnarsky</json:string><json:string>A. Patricia</json:string><json:string>Dr Brian</json:string><json:string>A.P. 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Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Biochemistry</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences medicales</json:string></inist></categories><publicationDate>2003</publicationDate><copyrightDate>2003</copyrightDate><doi><json:string>10.1034/j.1399-3011.2003.00031.x</json:string></doi><id>DCA1BD36E323CD65E77A2DE79D090E336A6E0908</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/WNG-VLV2BX4F-0/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/WNG-VLV2BX4F-0/bundle.zip</uri></json:item><istex:fulltextTEI 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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"><p><hi rend="bold">Abstract:</hi> MUC1 mucin is a large transmembrane glycoprotein, the extracellular domain of which is formed by a repeating 20 amino acid sequence, GVTSA<hi rend="bold">PDTRP</hi>APGSTAPPAH. In normal breast epithelial cells, the extracellular domain is densely covered with highly branched complex carbohydrate structures. However, in neoplastic breast tissue, the extracellular domain is under‐glycosylated, resulting in the exposure of a highly immunogenic core peptide epitope (PDTRP in bold above), as well as in the exposure of normally cryptic core Tn (GalNAc), STn (sialyl α2–6 GalNAc) and TF (Gal β1–3 GalNAc) carbohydrates. Here, we report the results of <hi rend="superscript">1</hi>H NMR structural studies, natural abundance <hi rend="superscript">13</hi>C NMR relaxation measurements and distance‐restrained MD simulations designed to probe the structural and dynamical effects of Tn‐glycosylation within the PDTRP core peptide epitope. Two synthetic peptides were studied: a nine‐residue MUC1 peptide of the sequence, Thr1‐Ser2‐Ala3‐Pro4‐Asp5‐Thr6‐Arg7‐Pro8‐Ala9, and a Tn‐glycosylated version of this peptide, Thr1‐Ser2‐Ala3‐Pro4‐Asp5‐Thr6(αGalNAc)‐Arg7‐Pro8‐Ala9. The results of these studies show that a type I β‐turn conformation is adopted by residues PDTR within the PDTRP region of the unglycosylated MUC1 sequence. The existence of a similar β‐turn within the PDTRP core peptide epitope of the under‐glycosylated cancer‐associated MUC1 mucin protein might explain the immunodominance of this region <hi rend="italic">in vivo</hi>, as the presence of defined secondary structure within peptide epitope regions has been correlated with increased immunogenicity in other systems. Our results have also shown that Tn glycosylation at the central threonine within the PDTRP core epitope region shifts the conformational equilibrium away from the type I β‐turn conformation and toward a more rigid and extended state. The significance of these results are discussed in relation to the possible roles that peptide epitope secondary structure and glycosylation state may play in MUC1 tumor immunogenicity.</p></abstract><textClass><keywords xml:lang="en"><term xml:id="k1">cancer</term><term xml:id="k2">epitope</term><term xml:id="k3">glycosylation</term><term xml:id="k4">MD</term><term xml:id="k5">mucin</term><term xml:id="k6">MUC1</term><term xml:id="k7">NMR</term><term xml:id="k8">peptide</term><term xml:id="k9">tumor</term></keywords><keywords rend="tocHeading1"><term>Original Articles</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-VLV2BX4F-0/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>Munksgaard International Publishers</publisherName><publisherLoc>Oxford, UK</publisherLoc></publisherInfo><doi origin="wiley" registered="yes">10.1111/(ISSN)1399-3011</doi><issn type="print">1397-002X</issn><issn type="electronic">1399-3011</issn><idGroup><id type="product" value="CBDD"></id><id type="publisherDivision" value="ST"></id></idGroup><titleGroup><title type="main" sort="JOURNAL OF PEPTIDE RESEARCH">The Journal of Peptide Research</title></titleGroup></publicationMeta><publicationMeta level="part" position="03003"><doi origin="wiley">10.1111/jpp.2003.61.issue-3</doi><numberingGroup><numbering type="journalVolume" number="61">61</numbering><numbering type="journalIssue" number="3">3</numbering></numberingGroup><coverDate startDate="2003-03">March 2003</coverDate></publicationMeta><publicationMeta level="unit" type="article" position="0009100" status="forIssue"><doi origin="wiley">10.1034/j.1399-3011.2003.00031.x</doi><idGroup><id type="unit" value="CBDD031"></id></idGroup><countGroup><count type="pageTotal" number="18"></count></countGroup><titleGroup><title type="tocHeading1">Original Articles</title></titleGroup><eventGroup><event type="firstOnline" date="2003-02-04"></event><event type="publishedOnlineFinalForm" date="2008-12-05"></event><event type="xmlConverted" agent="Converter:BPG_TO_WML3G version:2.3.15 mode:FullText source:FullText result:FullText" date="2010-07-21"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.8.8" date="2014-01-08"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.1.7 mode:FullText,remove_FC" date="2014-11-04"></event></eventGroup><numberingGroup><numbering type="pageFirst" number="91">91</numbering><numbering type="pageLast" number="108">108</numbering></numberingGroup><correspondenceTo>
Asst. Professor <i>A. Patricia Campbell</i>
Department of Medicinal Chemistry
School of Pharmacy
University of Washington
Seattle
WA 98195
USA
Tel.: 1‐206‐685‐2468
Fax: 1‐206‐685‐3252
E‐mail: <email normalForm="apc@u.washington.edu">apc@u.washington.edu</email></correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:CBDD.CBDD031.pdf"></link></linkGroup></publicationMeta><contentMeta><unparsedEditorialHistory><b>Dates:</b>Received 28 June 2002 Revised 27 August 2002 Accepted 12 October 2002</unparsedEditorialHistory><countGroup><count type="figureTotal" number="10"></count><count type="tableTotal" number="6"></count><count type="formulaTotal" number="0"></count><count type="referenceTotal" number="72"></count><count type="wordTotal" number="8483"></count><count type="linksPubMed" number="0"></count><count type="linksCrossRef" number="0"></count></countGroup><titleGroup><title type="main">Probing the conformational and dynamical effects of <i>O</i>‐glycosylation within the immunodominant region of a MUC1 peptide tumor antigen</title><title type="shortAuthors">Schuman <i>et al</i></title><title type="short">Effects of MUC1 <i>O</i>‐glycosylation</title></titleGroup><creators><creator creatorRole="author" xml:id="cr1" affiliationRef="#a1"><personName><givenNames>J.</givenNames><familyName>Schuman</familyName></personName></creator><creator creatorRole="author" xml:id="cr2" affiliationRef="#a1"><personName><givenNames>A.P.</givenNames><familyName>Campbell</familyName></personName></creator><creator creatorRole="author" xml:id="cr3" affiliationRef="#a2"><personName><givenNames>R.R.</givenNames><familyName>Koganty</familyName></personName></creator><creator creatorRole="author" xml:id="cr4" affiliationRef="#a2"><personName><givenNames>B.M.</givenNames><familyName>Longenecker</familyName></personName></creator></creators><affiliationGroup><affiliation xml:id="a1" countryCode="US"><unparsedAffiliation>Department of Medicinal Chemistry, School of Pharmacy, University of Washington, Seattle, USA.</unparsedAffiliation></affiliation><affiliation xml:id="a2" countryCode="CA"><unparsedAffiliation>Biomira Inc., Edmonton, Canada.</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en"><keyword xml:id="k1">cancer</keyword><keyword xml:id="k2">epitope</keyword><keyword xml:id="k3">glycosylation</keyword><keyword xml:id="k4">MD</keyword><keyword xml:id="k5">mucin</keyword><keyword xml:id="k6">MUC1</keyword><keyword xml:id="k7">NMR</keyword><keyword xml:id="k8">peptide</keyword><keyword xml:id="k9">tumor</keyword></keywordGroup><supportingInformation><supportingInfoItem><mediaResource alt="supporting info item" href="urn-x:wiley:1397002X:media:cbdd031:CBDD_031_sm_Tables"></mediaResource><caption>Supporting info item</caption></supportingInfoItem></supportingInformation><abstractGroup><abstract type="main" xml:lang="en"><p><b>Abstract:</b> MUC1 mucin is a large transmembrane glycoprotein, the extracellular domain of which is formed by a repeating 20 amino acid sequence, GVTSA<b>PDTRP</b>APGSTAPPAH. In normal breast epithelial cells, the extracellular domain is densely covered with highly branched complex carbohydrate structures. However, in neoplastic breast tissue, the extracellular domain is under‐glycosylated, resulting in the exposure of a highly immunogenic core peptide epitope (PDTRP in bold above), as well as in the exposure of normally cryptic core Tn (GalNAc), STn (sialyl α2–6 GalNAc) and TF (Gal β1–3 GalNAc) carbohydrates. Here, we report the results of <sup>1</sup>H NMR structural studies, natural abundance <sup>13</sup>C NMR relaxation measurements and distance‐restrained MD simulations designed to probe the structural and dynamical effects of Tn‐glycosylation within the PDTRP core peptide epitope. Two synthetic peptides were studied: a nine‐residue MUC1 peptide of the sequence, Thr1‐Ser2‐Ala3‐Pro4‐Asp5‐Thr6‐Arg7‐Pro8‐Ala9, and a Tn‐glycosylated version of this peptide, Thr1‐Ser2‐Ala3‐Pro4‐Asp5‐Thr6(αGalNAc)‐Arg7‐Pro8‐Ala9. The results of these studies show that a type I β‐turn conformation is adopted by residues PDTR within the PDTRP region of the unglycosylated MUC1 sequence. The existence of a similar β‐turn within the PDTRP core peptide epitope of the under‐glycosylated cancer‐associated MUC1 mucin protein might explain the immunodominance of this region <i>in vivo</i>, as the presence of defined secondary structure within peptide epitope regions has been correlated with increased immunogenicity in other systems. Our results have also shown that Tn glycosylation at the central threonine within the PDTRP core epitope region shifts the conformational equilibrium away from the type I β‐turn conformation and toward a more rigid and extended state. The significance of these results are discussed in relation to the possible roles that peptide epitope secondary structure and glycosylation state may play in MUC1 tumor immunogenicity.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Probing the conformational and dynamical effects of O‐glycosylation within the immunodominant region of a MUC1 peptide tumor antigen</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>Effects of MUC1 O‐glycosylation</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Probing the conformational and dynamical effects of O‐glycosylation within the immunodominant region of a MUC1 peptide tumor antigen</title></titleInfo><name type="personal"><namePart type="given">J.</namePart><namePart type="family">Schuman</namePart><affiliation>Department of Medicinal Chemistry, School of Pharmacy, University of Washington, Seattle, USA.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">A.P.</namePart><namePart type="family">Campbell</namePart><affiliation>Department of Medicinal Chemistry, School of Pharmacy, University of Washington, Seattle, USA.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">R.R.</namePart><namePart type="family">Koganty</namePart><affiliation>Biomira Inc., Edmonton, Canada.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">B.M.</namePart><namePart type="family">Longenecker</namePart><affiliation>Biomira Inc., Edmonton, Canada.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-6N5SZHKN-D">article</genre><originInfo><publisher>Munksgaard International Publishers</publisher><place><placeTerm type="text">Oxford, UK</placeTerm></place><dateIssued encoding="w3cdtf">2003-03</dateIssued><edition>Dates:Received 28 June 2002 Revised 27 August 2002 Accepted 12 October 2002</edition><copyrightDate encoding="w3cdtf">2003</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><extent unit="figures">10</extent><extent unit="tables">6</extent><extent unit="formulas">0</extent><extent unit="references">72</extent><extent unit="linksCrossRef">0</extent><extent unit="words">8483</extent></physicalDescription><abstract lang="en">Abstract: MUC1 mucin is a large transmembrane glycoprotein, the extracellular domain of which is formed by a repeating 20 amino acid sequence, GVTSAPDTRPAPGSTAPPAH. In normal breast epithelial cells, the extracellular domain is densely covered with highly branched complex carbohydrate structures. However, in neoplastic breast tissue, the extracellular domain is under‐glycosylated, resulting in the exposure of a highly immunogenic core peptide epitope (PDTRP in bold above), as well as in the exposure of normally cryptic core Tn (GalNAc), STn (sialyl α2–6 GalNAc) and TF (Gal β1–3 GalNAc) carbohydrates. Here, we report the results of 1H NMR structural studies, natural abundance 13C NMR relaxation measurements and distance‐restrained MD simulations designed to probe the structural and dynamical effects of Tn‐glycosylation within the PDTRP core peptide epitope. Two synthetic peptides were studied: a nine‐residue MUC1 peptide of the sequence, Thr1‐Ser2‐Ala3‐Pro4‐Asp5‐Thr6‐Arg7‐Pro8‐Ala9, and a Tn‐glycosylated version of this peptide, Thr1‐Ser2‐Ala3‐Pro4‐Asp5‐Thr6(αGalNAc)‐Arg7‐Pro8‐Ala9. The results of these studies show that a type I β‐turn conformation is adopted by residues PDTR within the PDTRP region of the unglycosylated MUC1 sequence. The existence of a similar β‐turn within the PDTRP core peptide epitope of the under‐glycosylated cancer‐associated MUC1 mucin protein might explain the immunodominance of this region in vivo, as the presence of defined secondary structure within peptide epitope regions has been correlated with increased immunogenicity in other systems. Our results have also shown that Tn glycosylation at the central threonine within the PDTRP core epitope region shifts the conformational equilibrium away from the type I β‐turn conformation and toward a more rigid and extended state. The significance of these results are discussed in relation to the possible roles that peptide epitope secondary structure and glycosylation state may play in MUC1 tumor immunogenicity.</abstract><note type="additional physical form">Supporting info item</note><subject lang="en"><genre>keywords</genre><topic>cancer</topic><topic>epitope</topic><topic>glycosylation</topic><topic>MD</topic><topic>mucin</topic><topic>MUC1</topic><topic>NMR</topic><topic>peptide</topic><topic>tumor</topic></subject><relatedItem type="host"><titleInfo><title>The Journal of Peptide Research</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><identifier type="ISSN">1397-002X</identifier><identifier type="eISSN">1399-3011</identifier><identifier type="DOI">10.1111/(ISSN)1399-3011</identifier><identifier type="PublisherID">CBDD</identifier><part><date>2003</date><detail type="volume"><caption>vol.</caption><number>61</number></detail><detail type="issue"><caption>no.</caption><number>3</number></detail><extent unit="pages"><start>91</start><end>108</end><total>18</total></extent></part></relatedItem><relatedItem type="references" displayLabel="cit1"><titleInfo><title>MUC1 and cancer</title></titleInfo><name type="personal"><namePart type="given">J.</namePart><namePart type="family">Taylor‐Papadimitriou</namePart><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">J.</namePart><namePart type="family">Burchell</namePart><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">D.W.</namePart><namePart type="family">Miles</namePart><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">M.</namePart><namePart type="family">Dalziel</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Taylor‐Papadimitriou, J., Burchell, J., Miles, D.W. & Dalziel, M. (1999) MUC1 and cancer. Biochim. Biophys. Acta 1455, 301–313.</note><part><date>1999</date><detail type="volume"><caption>vol.</caption><number>1455</number></detail><extent unit="pages"><start>301</start><end>313</end></extent></part><relatedItem type="host"><titleInfo><title>Biochim. Biophys. 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