Identification of murine cytotoxic T-lymphocyte epitopes of bovine herpesvirus 1
Identifieur interne : 000474 ( Istex/Corpus ); précédent : 000473; suivant : 000475Identification of murine cytotoxic T-lymphocyte epitopes of bovine herpesvirus 1
Auteurs : Douglas S. Zatechka Jr. ; Nagendra R. Hegde ; Kandasamy Hariharan ; S. SrikumaranSource :
- Vaccine [ 0264-410X ] ; 1999.
English descriptors
- Teeft :
- Adjuvant, Allele, Aspms, Assay, Bovine, Bovine herpesvirus, Cell epitopes, Ctls, Cytotoxic, Cytotoxicity assay, Epitope, Error bars, Glycoprotein, Herpesvirus, Immunization, Immunol, Individual peptides, Lymphocyte, Lysed, Lysis, Maximum release, Molecule, Murine, Native peptides, Particular class, Peptide, Peptide motif, Peptide motifs, Recombinant, Spontaneous release, Standard deviations, Syngeneic, Synthetic peptides, Target cells, Vaccine, Viral, Viral immunol, Viral peptides, Virol, Zatechka.
Abstract
Abstract: Major histocompatibility complex (MHC) class I molecules present endogenously derived viral peptides to CD8+ cytotoxic T-lymphocytes (CTLs). The objective of this study was to identify the H-2Dd- and H-2Kd-restricted CTL epitopes of bovine herpesvirus 1 (BHV-1), based on the allele-specific peptide motifs (ASPMs) of the above class I molecules. Nine sequences conforming to the H-2Dd and H-2Kd ASPMs were identified on BHV-1 proteins, and the respective peptides were synthesized. Five of these peptides exhibited moderate to strong binding to the Dd molecule. CTLs generated by BALB/c mice immunized with BHV-1 proteins emulsified in a suitable adjuvant effectively lysed peptide-pulsed syngeneic targets, indicating that these epitopes were generated in vivo. Mice immunized with these peptides emulsified in a suitable adjuvant also developed anti-BHV-1 CTLs. These CTLs identified three veritable CTL epitopes among the “potential epitopes” synthesized based on the ASPMs. The elucidation of the CTL epitopes of BHV-1 should aid in the development of efficacious vaccines against this virus.
Url:
DOI: 10.1016/S0264-410X(98)00251-5
Links to Exploration step
ISTEX:DFF0F9A5B5E7DDFB9AF6408CCA95D8659945BC6FLe document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title>Identification of murine cytotoxic T-lymphocyte epitopes of bovine herpesvirus 1</title><author><name sortKey="Zatechka Jr, Douglas S" sort="Zatechka Jr, Douglas S" uniqKey="Zatechka Jr D" first="Douglas S." last="Zatechka Jr.">Douglas S. Zatechka Jr.</name><affiliation><mods:affiliation>Department of Veterinary and Biomedical Sciences, University of Nebraska-Lincoln, Fair Street and East Campus Loop, Lincoln, NE 68583-0905, USA</mods:affiliation></affiliation></author><author><name sortKey="Hegde, Nagendra R" sort="Hegde, Nagendra R" uniqKey="Hegde N" first="Nagendra R." last="Hegde">Nagendra R. Hegde</name><affiliation><mods:affiliation>Department of Veterinary and Biomedical Sciences, University of Nebraska-Lincoln, Fair Street and East Campus Loop, Lincoln, NE 68583-0905, USA</mods:affiliation></affiliation></author><author><name sortKey="Hariharan, Kandasamy" sort="Hariharan, Kandasamy" uniqKey="Hariharan K" first="Kandasamy" last="Hariharan">Kandasamy Hariharan</name><affiliation><mods:affiliation>IDEC Pharmaceuticals Corporation, San Diego, CA 92121, USA</mods:affiliation></affiliation></author><author><name sortKey="Srikumaran, S" sort="Srikumaran, S" uniqKey="Srikumaran S" first="S." last="Srikumaran">S. Srikumaran</name><affiliation><mods:affiliation>Department of Veterinary and Biomedical Sciences, University of Nebraska-Lincoln, Fair Street and East Campus Loop, Lincoln, NE 68583-0905, USA</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:DFF0F9A5B5E7DDFB9AF6408CCA95D8659945BC6F</idno><date when="1999" year="1999">1999</date><idno type="doi">10.1016/S0264-410X(98)00251-5</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-JBNNRNX8-2/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000474</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000474</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Identification of murine cytotoxic T-lymphocyte epitopes of bovine herpesvirus 1</title><author><name sortKey="Zatechka Jr, Douglas S" sort="Zatechka Jr, Douglas S" uniqKey="Zatechka Jr D" first="Douglas S." last="Zatechka Jr.">Douglas S. Zatechka Jr.</name><affiliation><mods:affiliation>Department of Veterinary and Biomedical Sciences, University of Nebraska-Lincoln, Fair Street and East Campus Loop, Lincoln, NE 68583-0905, USA</mods:affiliation></affiliation></author><author><name sortKey="Hegde, Nagendra R" sort="Hegde, Nagendra R" uniqKey="Hegde N" first="Nagendra R." last="Hegde">Nagendra R. Hegde</name><affiliation><mods:affiliation>Department of Veterinary and Biomedical Sciences, University of Nebraska-Lincoln, Fair Street and East Campus Loop, Lincoln, NE 68583-0905, USA</mods:affiliation></affiliation></author><author><name sortKey="Hariharan, Kandasamy" sort="Hariharan, Kandasamy" uniqKey="Hariharan K" first="Kandasamy" last="Hariharan">Kandasamy Hariharan</name><affiliation><mods:affiliation>IDEC Pharmaceuticals Corporation, San Diego, CA 92121, USA</mods:affiliation></affiliation></author><author><name sortKey="Srikumaran, S" sort="Srikumaran, S" uniqKey="Srikumaran S" first="S." last="Srikumaran">S. Srikumaran</name><affiliation><mods:affiliation>Department of Veterinary and Biomedical Sciences, University of Nebraska-Lincoln, Fair Street and East Campus Loop, Lincoln, NE 68583-0905, USA</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Vaccine</title><title level="j" type="abbrev">JVAC</title><idno type="ISSN">0264-410X</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1999">1999</date><biblScope unit="volume">17</biblScope><biblScope unit="issue">7–8</biblScope><biblScope unit="page" from="686">686</biblScope><biblScope unit="page" to="694">694</biblScope></imprint><idno type="ISSN">0264-410X</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0264-410X</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Adjuvant</term><term>Allele</term><term>Aspms</term><term>Assay</term><term>Bovine</term><term>Bovine herpesvirus</term><term>Cell epitopes</term><term>Ctls</term><term>Cytotoxic</term><term>Cytotoxicity assay</term><term>Epitope</term><term>Error bars</term><term>Glycoprotein</term><term>Herpesvirus</term><term>Immunization</term><term>Immunol</term><term>Individual peptides</term><term>Lymphocyte</term><term>Lysed</term><term>Lysis</term><term>Maximum release</term><term>Molecule</term><term>Murine</term><term>Native peptides</term><term>Particular class</term><term>Peptide</term><term>Peptide motif</term><term>Peptide motifs</term><term>Recombinant</term><term>Spontaneous release</term><term>Standard deviations</term><term>Syngeneic</term><term>Synthetic peptides</term><term>Target cells</term><term>Vaccine</term><term>Viral</term><term>Viral immunol</term><term>Viral peptides</term><term>Virol</term><term>Zatechka</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Major histocompatibility complex (MHC) class I molecules present endogenously derived viral peptides to CD8+ cytotoxic T-lymphocytes (CTLs). The objective of this study was to identify the H-2Dd- and H-2Kd-restricted CTL epitopes of bovine herpesvirus 1 (BHV-1), based on the allele-specific peptide motifs (ASPMs) of the above class I molecules. Nine sequences conforming to the H-2Dd and H-2Kd ASPMs were identified on BHV-1 proteins, and the respective peptides were synthesized. Five of these peptides exhibited moderate to strong binding to the Dd molecule. CTLs generated by BALB/c mice immunized with BHV-1 proteins emulsified in a suitable adjuvant effectively lysed peptide-pulsed syngeneic targets, indicating that these epitopes were generated in vivo. Mice immunized with these peptides emulsified in a suitable adjuvant also developed anti-BHV-1 CTLs. These CTLs identified three veritable CTL epitopes among the “potential epitopes” synthesized based on the ASPMs. The elucidation of the CTL epitopes of BHV-1 should aid in the development of efficacious vaccines against this virus.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>epitope</json:string><json:string>ctls</json:string><json:string>peptide</json:string><json:string>cytotoxic</json:string><json:string>lymphocyte</json:string><json:string>viral</json:string><json:string>murine</json:string><json:string>vaccine</json:string><json:string>lysed</json:string><json:string>glycoprotein</json:string><json:string>immunol</json:string><json:string>virol</json:string><json:string>aspms</json:string><json:string>syngeneic</json:string><json:string>recombinant</json:string><json:string>herpesvirus</json:string><json:string>lysis</json:string><json:string>zatechka</json:string><json:string>allele</json:string><json:string>bovine herpesvirus</json:string><json:string>synthetic peptides</json:string><json:string>adjuvant</json:string><json:string>assay</json:string><json:string>maximum release</json:string><json:string>peptide motifs</json:string><json:string>bovine</json:string><json:string>standard deviations</json:string><json:string>cell epitopes</json:string><json:string>target cells</json:string><json:string>error bars</json:string><json:string>individual peptides</json:string><json:string>immunization</json:string><json:string>native peptides</json:string><json:string>peptide motif</json:string><json:string>spontaneous release</json:string><json:string>cytotoxicity assay</json:string><json:string>viral peptides</json:string><json:string>viral immunol</json:string><json:string>particular class</json:string><json:string>molecule</json:string></teeft></keywords><author><json:item><name>Douglas S. Zatechka, Jr.</name><affiliations><json:string>Department of Veterinary and Biomedical Sciences, University of Nebraska-Lincoln, Fair Street and East Campus Loop, Lincoln, NE 68583-0905, USA</json:string></affiliations></json:item><json:item><name>Nagendra R. Hegde</name><affiliations><json:string>Department of Veterinary and Biomedical Sciences, University of Nebraska-Lincoln, Fair Street and East Campus Loop, Lincoln, NE 68583-0905, USA</json:string></affiliations></json:item><json:item><name>Kandasamy Hariharan</name><affiliations><json:string>IDEC Pharmaceuticals Corporation, San Diego, CA 92121, USA</json:string></affiliations></json:item><json:item><name>S. Srikumaran</name><affiliations><json:string>Department of Veterinary and Biomedical Sciences, University of Nebraska-Lincoln, Fair Street and East Campus Loop, Lincoln, NE 68583-0905, USA</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Allele-specific peptide motif</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>BHV-1</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>CTL epitope</value></json:item></subject><arkIstex>ark:/67375/6H6-JBNNRNX8-2</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: Major histocompatibility complex (MHC) class I molecules present endogenously derived viral peptides to CD8+ cytotoxic T-lymphocytes (CTLs). The objective of this study was to identify the H-2Dd- and H-2Kd-restricted CTL epitopes of bovine herpesvirus 1 (BHV-1), based on the allele-specific peptide motifs (ASPMs) of the above class I molecules. Nine sequences conforming to the H-2Dd and H-2Kd ASPMs were identified on BHV-1 proteins, and the respective peptides were synthesized. Five of these peptides exhibited moderate to strong binding to the Dd molecule. CTLs generated by BALB/c mice immunized with BHV-1 proteins emulsified in a suitable adjuvant effectively lysed peptide-pulsed syngeneic targets, indicating that these epitopes were generated in vivo. Mice immunized with these peptides emulsified in a suitable adjuvant also developed anti-BHV-1 CTLs. These CTLs identified three veritable CTL epitopes among the “potential epitopes” synthesized based on the ASPMs. The elucidation of the CTL epitopes of BHV-1 should aid in the development of efficacious vaccines against this virus.</abstract><qualityIndicators><score>8.908</score><pdfWordCount>5414</pdfWordCount><pdfCharCount>34207</pdfCharCount><pdfVersion>1.2</pdfVersion><pdfPageCount>9</pdfPageCount><pdfPageSize>595 x 842 pts (A4)</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>159</abstractWordCount><abstractCharCount>1107</abstractCharCount><keywordCount>3</keywordCount></qualityIndicators><title>Identification of murine cytotoxic T-lymphocyte epitopes of bovine herpesvirus 1</title><pmid><json:string>10067674</json:string></pmid><pii><json:string>S0264-410X(98)00251-5</json:string></pii><genre><json:string>research-article</json:string></genre><host><title>Vaccine</title><language><json:string>unknown</json:string></language><publicationDate>1999</publicationDate><issn><json:string>0264-410X</json:string></issn><pii><json:string>S0264-410X(00)X0073-4</json:string></pii><volume>17</volume><issue>7–8</issue><pages><first>686</first><last>694</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1999</json:string></date><geogName></geogName><orgName><json:string>Department of Veterinary and Biomedical Sciences</json:string><json:string>Jackson Laboratory, Bar Harbor, ME</json:string><json:string>University of Nebraska Agricultural Research Division</json:string><json:string>Scripps Laboratories</json:string><json:string>CytRx Corporation</json:string><json:string>Use Committee of the University of Nebraska-Lincoln</json:string><json:string>IDEC Pharmaceuticals Corporation, San Diego</json:string><json:string>Elsevier Science Ltd.</json:string><json:string>University of Nebraska-Lincoln</json:string><json:string>Veterinary Diagnostic Center</json:string><json:string>American Type Culture Collection</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName><json:string>Ruben Donis</json:string><json:string>Irvine Scienti</json:string><json:string>To</json:string><json:string>La Jolla</json:string><json:string>L. 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[20]</json:string><json:string>[49]</json:string><json:string>[50, 51]</json:string><json:string>[31]</json:string><json:string>[46, 47]</json:string><json:string>[5]</json:string><json:string>[48]</json:string><json:string>[52]</json:string><json:string>[7]</json:string><json:string>[36]</json:string><json:string>[42, 43]</json:string><json:string>[2]</json:string><json:string>[46]</json:string><json:string>[19]</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-JBNNRNX8-2</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - medicine, research & experimental</json:string><json:string>2 - immunology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - virology</json:string></scienceMetrix><scopus><json:string>1 - Health Sciences</json:string><json:string>2 - Medicine</json:string><json:string>3 - Infectious Diseases</json:string><json:string>1 - Health Sciences</json:string><json:string>2 - Medicine</json:string><json:string>3 - Public Health, Environmental and Occupational Health</json:string><json:string>1 - Health Sciences</json:string><json:string>2 - Veterinary</json:string><json:string>3 - General Veterinary</json:string><json:string>1 - Life Sciences</json:string><json:string>2 - Immunology and Microbiology</json:string><json:string>3 - General Immunology and Microbiology</json:string><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Molecular Medicine</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 biologiques fondamentales et appliquees. psychologie</json:string><json:string>4 - microbiologie</json:string></inist></categories><publicationDate>1999</publicationDate><copyrightDate>1999</copyrightDate><doi><json:string>10.1016/S0264-410X(98)00251-5</json:string></doi><id>DFF0F9A5B5E7DDFB9AF6408CCA95D8659945BC6F</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-JBNNRNX8-2/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-JBNNRNX8-2/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-JBNNRNX8-2/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a">Identification of murine cytotoxic T-lymphocyte epitopes of bovine herpesvirus 1</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>©1999 Elsevier Science Ltd</p></licence><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</p></availability><date>1999</date></publicationStmt><notesStmt><note type="research-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</note><note type="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note><note type="content">Fig. 1: The ability of the synthetic peptides to bind class I molecules. BALB/3T3 cells were treated with citrate–phosphate buffer, pH 3.3, for 20 s. Dissociation of the native peptides (stripping) was monitored by flow cytometry using antibodies that bind H-2d molecules only in the presence of bound peptides (TIB-126) or irrespective of peptide binding (HB87). The ability of the synthetic peptides to individually reconstitute the TIB-126 epitope was tested by incubating the stripped cells with peptides, in the presence of human β2-microglobulin. Results are expressed as fluorescence index (FI) calculated as follows: FI=(Mean sample fluorescence−Mean background fluorescence)/(Mean background fluorescence)×100, where background refers to peptide-stripped cells and sample refers to peptide-pulsed cells. The error bars indicate standard deviations of the means.</note><note type="content">Fig. 2: Immunization of mice with BHV-1 protein or peptides induces BHV-1-specific CTLs. Mice were immunized and boosted with protein (Panel A) or peptides (Panel B), in PROVAX™ or TiterMax, and lymphocytes were harvested from spleen (Panel A) or popliteal lymph nodes (Panel B), respectively. In vitro restimulated effectors were tested against syngeneic targets either pulsed with a cocktail of peptides or not pulsed with the peptides, at the indicated E:T ratios, in a standard 51Cr-release assay. The results are presented as % specific lysis, calculated as follows: % specific lysis=(Sample 51Cr release−Spontaneous 51Cr release)/(Maximum 51Cr release−Spontaneous 51Cr release) where spontaneous and maximum release refer to no effector and Triton X-100-treated samples, respectively. Spontaneous release was less than 20% of maximum release in all cases. The error bars indicate standard deviations of the means.</note><note type="content">Fig. 3: Identification of H-2Dd-restricted CTL epitopes of BHV-1. CTLs derived as described in Fig. 2B, were tested in a 51Cr-release assay using syngeneic cells pulsed with individual peptides at the indicated E:T ratios. The negative control peptide was a nonamer from BVDV gp53. The spontaneous release was less than 18% of maximum release in all cases. The error bars indicate standard deviations of the means. The means were statistically significant when no antigen was compared individually with peptides 1, 6 and 7, but not significant between no antigen and peptide (p<0.05).</note><note type="content">Fig. 4: BHV-1-specific CTLs are H-2Dd-restricted. CTLs obtained as described in Fig. 2, were tested in a 51Cr-release assay using targets pulsed with a pool of peptides 1, 6 and 7. The results are presented as described in Fig. 2. Spontaneous release was less than 12% of maximum release in all cases. (A) CTLs are class I-restricted. BALB/3T3 cells that do not express class II molecules were used as targets. (B) CTLs are H-2Dd-restricted. Syngeneic (P815, H-2d) and allogeneic (EL-4, H-2b) targets were used. The error bars indicate standard deviations of the means.</note><note type="content">Table 1: The allele-specific peptide motifs (ASPMs) of the MHC class I products utilized</note><note type="content">Table 2: Peptides synthesized in this study</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Identification of murine cytotoxic T-lymphocyte epitopes of bovine herpesvirus 1</title><author xml:id="author-0000"><persName><forename type="first">Douglas S.</forename><surname>Zatechka, Jr.</surname></persName><affiliation>Department of Veterinary and Biomedical Sciences, University of Nebraska-Lincoln, Fair Street and East Campus Loop, Lincoln, NE 68583-0905, USA</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Nagendra R.</forename><surname>Hegde</surname></persName><affiliation>Department of Veterinary and Biomedical Sciences, University of Nebraska-Lincoln, Fair Street and East Campus Loop, Lincoln, NE 68583-0905, USA</affiliation></author><author xml:id="author-0002"><persName><forename type="first">Kandasamy</forename><surname>Hariharan</surname></persName><affiliation>IDEC Pharmaceuticals Corporation, San Diego, CA 92121, USA</affiliation></author><author xml:id="author-0003"><persName><forename type="first">S.</forename><surname>Srikumaran</surname></persName><note type="correspondence"><p>Corresponding author. Tel.: +1-402-472-3319; fax: +1-402-472-9690</p></note><affiliation>Department of Veterinary and Biomedical Sciences, University of Nebraska-Lincoln, Fair Street and East Campus Loop, Lincoln, NE 68583-0905, USA</affiliation></author><idno type="istex">DFF0F9A5B5E7DDFB9AF6408CCA95D8659945BC6F</idno><idno type="ark">ark:/67375/6H6-JBNNRNX8-2</idno><idno type="DOI">10.1016/S0264-410X(98)00251-5</idno><idno type="PII">S0264-410X(98)00251-5</idno></analytic><monogr><title level="j">Vaccine</title><title level="j" type="abbrev">JVAC</title><idno type="pISSN">0264-410X</idno><idno type="PII">S0264-410X(00)X0073-4</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1999"></date><biblScope unit="volume">17</biblScope><biblScope unit="issue">7–8</biblScope><biblScope unit="page" from="686">686</biblScope><biblScope unit="page" to="694">694</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1999</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: Major histocompatibility complex (MHC) class I molecules present endogenously derived viral peptides to CD8+ cytotoxic T-lymphocytes (CTLs). The objective of this study was to identify the H-2Dd- and H-2Kd-restricted CTL epitopes of bovine herpesvirus 1 (BHV-1), based on the allele-specific peptide motifs (ASPMs) of the above class I molecules. Nine sequences conforming to the H-2Dd and H-2Kd ASPMs were identified on BHV-1 proteins, and the respective peptides were synthesized. Five of these peptides exhibited moderate to strong binding to the Dd molecule. CTLs generated by BALB/c mice immunized with BHV-1 proteins emulsified in a suitable adjuvant effectively lysed peptide-pulsed syngeneic targets, indicating that these epitopes were generated in vivo. Mice immunized with these peptides emulsified in a suitable adjuvant also developed anti-BHV-1 CTLs. These CTLs identified three veritable CTL epitopes among the “potential epitopes” synthesized based on the ASPMs. The elucidation of the CTL epitopes of BHV-1 should aid in the development of efficacious vaccines against this virus.</p></abstract><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>Allele-specific peptide motif</term></item><item><term>BHV-1</term></item><item><term>CTL epitope</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1998-06-22">Modified</change><change when="1999">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-JBNNRNX8-2/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: ce:floats; body; tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"><istex:entity SYSTEM="gr1" NDATA="IMAGE" name="gr1"></istex:entity><istex:entity SYSTEM="gr2" NDATA="IMAGE" name="gr2"></istex:entity><istex:entity SYSTEM="gr3" NDATA="IMAGE" name="gr3"></istex:entity><istex:entity SYSTEM="gr4" NDATA="IMAGE" name="gr4"></istex:entity></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>JVAC</jid><aid>1220</aid><ce:pii>S0264-410X(98)00251-5</ce:pii><ce:doi>10.1016/S0264-410X(98)00251-5</ce:doi><ce:copyright year="1999" type="full-transfer">Elsevier Science Ltd</ce:copyright></item-info><head><ce:title>Identification of murine cytotoxic T-lymphocyte epitopes of bovine herpesvirus 1</ce:title><ce:author-group><ce:author><ce:given-name>Douglas S.</ce:given-name><ce:surname>Zatechka</ce:surname><ce:suffix>Jr.</ce:suffix><ce:cross-ref refid="AFF1">a</ce:cross-ref></ce:author><ce:author><ce:given-name>Nagendra R.</ce:given-name><ce:surname>Hegde</ce:surname><ce:cross-ref refid="AFF1">a</ce:cross-ref></ce:author><ce:author><ce:given-name>Kandasamy</ce:given-name><ce:surname>Hariharan</ce:surname><ce:cross-ref refid="AFF2">b</ce:cross-ref></ce:author><ce:author><ce:given-name>S.</ce:given-name><ce:surname>Srikumaran</ce:surname><ce:cross-ref refid="AFF1">a</ce:cross-ref><ce:cross-ref refid="CORR1">*</ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>Department of Veterinary and Biomedical Sciences, University of Nebraska-Lincoln, Fair Street and East Campus Loop, Lincoln, NE 68583-0905, USA</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>IDEC Pharmaceuticals Corporation, San Diego, CA 92121, USA</ce:textfn></ce:affiliation><ce:correspondence id="CORR1"><ce:label>*</ce:label><ce:text>Corresponding author. Tel.: +1-402-472-3319; fax: +1-402-472-9690</ce:text></ce:correspondence></ce:author-group><ce:date-received day="2" month="4" year="1998"></ce:date-received><ce:date-revised day="22" month="6" year="1998"></ce:date-revised><ce:date-accepted day="22" month="6" year="1998"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Major histocompatibility complex (MHC) class I molecules present endogenously derived viral peptides to CD8<ce:sup>+</ce:sup> cytotoxic T-lymphocytes (CTLs). The objective of this study was to identify the H-2D<ce:sup>d</ce:sup>- and H-2K<ce:sup>d</ce:sup>-restricted CTL epitopes of bovine herpesvirus 1 (BHV-1), based on the allele-specific peptide motifs (ASPMs) of the above class I molecules. Nine sequences conforming to the H-2D<ce:sup>d</ce:sup> and H-2K<ce:sup>d</ce:sup> ASPMs were identified on BHV-1 proteins, and the respective peptides were synthesized. Five of these peptides exhibited moderate to strong binding to the D<ce:sup>d</ce:sup> molecule. CTLs generated by BALB/c mice immunized with BHV-1 proteins emulsified in a suitable adjuvant effectively lysed peptide-pulsed syngeneic targets, indicating that these epitopes were generated in vivo. Mice immunized with these peptides emulsified in a suitable adjuvant also developed anti-BHV-1 CTLs. These CTLs identified three veritable CTL epitopes among the “potential epitopes” synthesized based on the ASPMs. The elucidation of the CTL epitopes of BHV-1 should aid in the development of efficacious vaccines against this virus.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords class="keyword"><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>Allele-specific peptide motif</ce:text></ce:keyword><ce:keyword><ce:text>BHV-1</ce:text></ce:keyword><ce:keyword><ce:text>CTL epitope</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Identification of murine cytotoxic T-lymphocyte epitopes of bovine herpesvirus 1</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Identification of murine cytotoxic T-lymphocyte epitopes of bovine herpesvirus 1</title></titleInfo><name type="personal"><namePart type="given">Douglas S.</namePart><namePart type="family">Zatechka, Jr.</namePart><affiliation>Department of Veterinary and Biomedical Sciences, University of Nebraska-Lincoln, Fair Street and East Campus Loop, Lincoln, NE 68583-0905, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Nagendra R.</namePart><namePart type="family">Hegde</namePart><affiliation>Department of Veterinary and Biomedical Sciences, University of Nebraska-Lincoln, Fair Street and East Campus Loop, Lincoln, NE 68583-0905, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Kandasamy</namePart><namePart type="family">Hariharan</namePart><affiliation>IDEC Pharmaceuticals Corporation, San Diego, CA 92121, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">S.</namePart><namePart type="family">Srikumaran</namePart><affiliation>Department of Veterinary and Biomedical Sciences, University of Nebraska-Lincoln, Fair Street and East Campus Loop, Lincoln, NE 68583-0905, USA</affiliation><description>Corresponding author. Tel.: +1-402-472-3319; fax: +1-402-472-9690</description><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1999</dateIssued><dateModified encoding="w3cdtf">1998-06-22</dateModified><copyrightDate encoding="w3cdtf">1999</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: Major histocompatibility complex (MHC) class I molecules present endogenously derived viral peptides to CD8+ cytotoxic T-lymphocytes (CTLs). The objective of this study was to identify the H-2Dd- and H-2Kd-restricted CTL epitopes of bovine herpesvirus 1 (BHV-1), based on the allele-specific peptide motifs (ASPMs) of the above class I molecules. Nine sequences conforming to the H-2Dd and H-2Kd ASPMs were identified on BHV-1 proteins, and the respective peptides were synthesized. Five of these peptides exhibited moderate to strong binding to the Dd molecule. CTLs generated by BALB/c mice immunized with BHV-1 proteins emulsified in a suitable adjuvant effectively lysed peptide-pulsed syngeneic targets, indicating that these epitopes were generated in vivo. Mice immunized with these peptides emulsified in a suitable adjuvant also developed anti-BHV-1 CTLs. These CTLs identified three veritable CTL epitopes among the “potential epitopes” synthesized based on the ASPMs. The elucidation of the CTL epitopes of BHV-1 should aid in the development of efficacious vaccines against this virus.</abstract><note type="content">Fig. 1: The ability of the synthetic peptides to bind class I molecules. BALB/3T3 cells were treated with citrate–phosphate buffer, pH 3.3, for 20 s. Dissociation of the native peptides (stripping) was monitored by flow cytometry using antibodies that bind H-2d molecules only in the presence of bound peptides (TIB-126) or irrespective of peptide binding (HB87). The ability of the synthetic peptides to individually reconstitute the TIB-126 epitope was tested by incubating the stripped cells with peptides, in the presence of human β2-microglobulin. Results are expressed as fluorescence index (FI) calculated as follows: FI=(Mean sample fluorescence−Mean background fluorescence)/(Mean background fluorescence)×100, where background refers to peptide-stripped cells and sample refers to peptide-pulsed cells. The error bars indicate standard deviations of the means.</note><note type="content">Fig. 2: Immunization of mice with BHV-1 protein or peptides induces BHV-1-specific CTLs. Mice were immunized and boosted with protein (Panel A) or peptides (Panel B), in PROVAX™ or TiterMax, and lymphocytes were harvested from spleen (Panel A) or popliteal lymph nodes (Panel B), respectively. In vitro restimulated effectors were tested against syngeneic targets either pulsed with a cocktail of peptides or not pulsed with the peptides, at the indicated E:T ratios, in a standard 51Cr-release assay. The results are presented as % specific lysis, calculated as follows: % specific lysis=(Sample 51Cr release−Spontaneous 51Cr release)/(Maximum 51Cr release−Spontaneous 51Cr release) where spontaneous and maximum release refer to no effector and Triton X-100-treated samples, respectively. Spontaneous release was less than 20% of maximum release in all cases. The error bars indicate standard deviations of the means.</note><note type="content">Fig. 3: Identification of H-2Dd-restricted CTL epitopes of BHV-1. CTLs derived as described in Fig. 2B, were tested in a 51Cr-release assay using syngeneic cells pulsed with individual peptides at the indicated E:T ratios. The negative control peptide was a nonamer from BVDV gp53. The spontaneous release was less than 18% of maximum release in all cases. The error bars indicate standard deviations of the means. The means were statistically significant when no antigen was compared individually with peptides 1, 6 and 7, but not significant between no antigen and peptide (p<0.05).</note><note type="content">Fig. 4: BHV-1-specific CTLs are H-2Dd-restricted. CTLs obtained as described in Fig. 2, were tested in a 51Cr-release assay using targets pulsed with a pool of peptides 1, 6 and 7. The results are presented as described in Fig. 2. Spontaneous release was less than 12% of maximum release in all cases. (A) CTLs are class I-restricted. BALB/3T3 cells that do not express class II molecules were used as targets. (B) CTLs are H-2Dd-restricted. Syngeneic (P815, H-2d) and allogeneic (EL-4, H-2b) targets were used. The error bars indicate standard deviations of the means.</note><note type="content">Table 1: The allele-specific peptide motifs (ASPMs) of the MHC class I products utilized</note><note type="content">Table 2: Peptides synthesized in this study</note><subject><genre>Keywords</genre><topic>Allele-specific peptide motif</topic><topic>BHV-1</topic><topic>CTL epitope</topic></subject><relatedItem type="host"><titleInfo><title>Vaccine</title></titleInfo><titleInfo type="abbreviated"><title>JVAC</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><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1999</dateIssued></originInfo><identifier type="ISSN">0264-410X</identifier><identifier type="PII">S0264-410X(00)X0073-4</identifier><part><date>1999</date><detail type="volume"><number>17</number><caption>vol.</caption></detail><detail type="issue"><number>7–8</number><caption>no.</caption></detail><extent unit="issue-pages"><start>617</start><end>1014</end></extent><extent unit="pages"><start>686</start><end>694</end></extent></part></relatedItem><identifier type="istex">DFF0F9A5B5E7DDFB9AF6408CCA95D8659945BC6F</identifier><identifier type="ark">ark:/67375/6H6-JBNNRNX8-2</identifier><identifier type="DOI">10.1016/S0264-410X(98)00251-5</identifier><identifier type="PII">S0264-410X(98)00251-5</identifier><accessCondition type="use and reproduction" contentType="copyright">©1999 Elsevier Science Ltd</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource><recordOrigin>Elsevier Science Ltd, ©1999</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-JBNNRNX8-2/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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