Antigenic differences between European and American isolates of porcine reproductive and respiratory syndrome virus (PRRSV) are encoded by the carboxyterminal portion of viral open reading frame 3
Identifieur interne : 000340 ( Istex/Corpus ); précédent : 000339; suivant : 000341Antigenic differences between European and American isolates of porcine reproductive and respiratory syndrome virus (PRRSV) are encoded by the carboxyterminal portion of viral open reading frame 3
Auteurs : Jonathan B. Katz ; Amy L. Shafer ; Kenneth A. Eernisse ; John G. Landgraf ; Eric A. NelsonSource :
- Veterinary Microbiology [ 0378-1135 ] ; 1995.
English descriptors
- Teeft :
- American prrs viruses, American swine, Amino, Amino acids, Antigenic, Antigenic differences, Antiserum, Baculovirus, Boehringer mannheim, Carboxyterminal portion, Cell cultures, Differentially reactive, Equine arteritis virus, Experimental reproduction, German sera, Glycosylation, Gnotobiotic, Gnotobiotic lelystad, Gnotobiotic swine, Hyperimmune rabbit serum, Immunoblot, Ipma, Katz, Lactate dehydrogenase, Lelystad, Lelystad virus, Microbiology, Molecular mass markers, Monoclonal antibodies, More reactive, Native protein, Nucleocapsid protein, Orfs, Porcine, Porcine epidemic abortion, Protein products, Prrs, Prrsv, Rabbits inoculated, Radioimmunoprecipitation assay, Reactive, Reading frame, Recombinant, Recombinant baculovirus, Recombinant fusion protein, Recombinant protein, Respiratory syndrome, Respiratory syndrome virus, Ripa, Serologic, Serologic analysis, Serologic differences, Simian hemorrhagic fever virus, Structural proteins, Swine, Swine infertility, Swine pratt, Syndrome, Veterinary microbiology, Viral, Viral antigen, Viral antigens, Virus, Wensvoort, Western immunoblot, Western immunoblotting.
Abstract
Abstract: Antigenic differences between European and American isolates of porcine reproductive and respiratory syndrome virus (PRRSV) were revealed by serologic analysis of a recombinant protein derived from PRRSV open reading frame 3 (ORF 3). The hydrophilic carboxyterminal 199 amino acids encoded by the ORF 3 of a European (Lelystad) isolate of PRRSV were expressed as a recombinant fusion protein (BP03-P) in a baculovirus gene expression system. Sera from gnotobiotic swine exposed to prototypic reference European and American isolates of PRRSV and sera from conventionally reared European and American swine convalescing from naturally acquired PRRSV infections were used to characterize the BP03-P protein. Sera from gnotobiotic and conventionally reared swine exposed to European isolates of PRRSV were significantly more reactive (P < 0.01) with BP03-P than were the corresponding American PRRSV antisera using the indirect immunoperoxidase monolayer assay (IPMA). Prototypic European, but not American, PRRSV antisera also recognized BP03-P using western immunoblotting and radioimmunoprecipitation assay (RIPA) procedures. However, gnotobiotically derived antiserum to an atypical American-origin PRRSV was reactive with BP03-P by both IPMA and western immunoblot. Despite a predicted potential for N-linked glycosylation, studies with tunicamycin and peptide-N-glycosidase F (PNGase F) indicated that BP03-P was not N-glycosylated in either insect cell cultures or Trichoplusia ni larvae infected with the recombinant baculovirus. Sera from rabbits inoculated with BP03-P failed to neutralize both the European (Lelystad) and American (ATCC VR-2332) reference isolates of PRRSV and did not react by IPMA with PRRSV-infected cell cultures. Taken together, the data suggest that the carboxyterminal portion of PRRSV ORF 3 encodes a non-neutralizing viral peptide that is partially responsible for the serologic differences noted between European and most American isolates of PRRSV.
Url:
DOI: 10.1016/0378-1135(94)00113-B
Links to Exploration step
ISTEX:C64535751CAE4C7BB1CA76683EEEF9034EF49389Le document en format XML
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Katz</name><affiliation><mods:affiliation>U.S. Department of Agriculture, Animal and Plant Health Inspection Service, Veterinary Services, National Veterinary Services Laboratories Ames, IA, USA</mods:affiliation></affiliation></author><author><name sortKey="Shafer, Amy L" sort="Shafer, Amy L" uniqKey="Shafer A" first="Amy L." last="Shafer">Amy L. Shafer</name><affiliation><mods:affiliation>U.S. Department of Agriculture, Animal and Plant Health Inspection Service, Veterinary Services, National Veterinary Services Laboratories Ames, IA, USA</mods:affiliation></affiliation></author><author><name sortKey="Eernisse, Kenneth A" sort="Eernisse, Kenneth A" uniqKey="Eernisse K" first="Kenneth A." last="Eernisse">Kenneth A. Eernisse</name><affiliation><mods:affiliation>U.S. Department of Agriculture, Animal and Plant Health Inspection Service, Veterinary Services, National Veterinary Services Laboratories Ames, IA, USA</mods:affiliation></affiliation></author><author><name sortKey="Landgraf, John G" sort="Landgraf, John G" uniqKey="Landgraf J" first="John G." last="Landgraf">John G. Landgraf</name><affiliation><mods:affiliation>U.S. Department of Agriculture, Animal and Plant Health Inspection Service, Veterinary Services, National Veterinary Services Laboratories Ames, IA, USA</mods:affiliation></affiliation></author><author><name sortKey="Nelson, Eric A" sort="Nelson, Eric A" uniqKey="Nelson E" first="Eric A." last="Nelson">Eric A. Nelson</name><affiliation><mods:affiliation>Department of Veterinary Science, South Dakota State University Brookings, SD, USA</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Veterinary Microbiology</title><title level="j" type="abbrev">VETMIC</title><idno type="ISSN">0378-1135</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1995">1995</date><biblScope unit="volume">44</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="65">65</biblScope><biblScope unit="page" to="76">76</biblScope></imprint><idno type="ISSN">0378-1135</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0378-1135</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>American prrs viruses</term><term>American swine</term><term>Amino</term><term>Amino acids</term><term>Antigenic</term><term>Antigenic differences</term><term>Antiserum</term><term>Baculovirus</term><term>Boehringer mannheim</term><term>Carboxyterminal portion</term><term>Cell cultures</term><term>Differentially reactive</term><term>Equine arteritis virus</term><term>Experimental reproduction</term><term>German sera</term><term>Glycosylation</term><term>Gnotobiotic</term><term>Gnotobiotic lelystad</term><term>Gnotobiotic swine</term><term>Hyperimmune rabbit serum</term><term>Immunoblot</term><term>Ipma</term><term>Katz</term><term>Lactate dehydrogenase</term><term>Lelystad</term><term>Lelystad virus</term><term>Microbiology</term><term>Molecular mass markers</term><term>Monoclonal antibodies</term><term>More reactive</term><term>Native protein</term><term>Nucleocapsid protein</term><term>Orfs</term><term>Porcine</term><term>Porcine epidemic abortion</term><term>Protein products</term><term>Prrs</term><term>Prrsv</term><term>Rabbits inoculated</term><term>Radioimmunoprecipitation assay</term><term>Reactive</term><term>Reading frame</term><term>Recombinant</term><term>Recombinant baculovirus</term><term>Recombinant fusion protein</term><term>Recombinant protein</term><term>Respiratory syndrome</term><term>Respiratory syndrome virus</term><term>Ripa</term><term>Serologic</term><term>Serologic analysis</term><term>Serologic differences</term><term>Simian hemorrhagic fever virus</term><term>Structural proteins</term><term>Swine</term><term>Swine infertility</term><term>Swine pratt</term><term>Syndrome</term><term>Veterinary microbiology</term><term>Viral</term><term>Viral antigen</term><term>Viral antigens</term><term>Virus</term><term>Wensvoort</term><term>Western immunoblot</term><term>Western immunoblotting</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Antigenic differences between European and American isolates of porcine reproductive and respiratory syndrome virus (PRRSV) were revealed by serologic analysis of a recombinant protein derived from PRRSV open reading frame 3 (ORF 3). The hydrophilic carboxyterminal 199 amino acids encoded by the ORF 3 of a European (Lelystad) isolate of PRRSV were expressed as a recombinant fusion protein (BP03-P) in a baculovirus gene expression system. Sera from gnotobiotic swine exposed to prototypic reference European and American isolates of PRRSV and sera from conventionally reared European and American swine convalescing from naturally acquired PRRSV infections were used to characterize the BP03-P protein. Sera from gnotobiotic and conventionally reared swine exposed to European isolates of PRRSV were significantly more reactive (P < 0.01) with BP03-P than were the corresponding American PRRSV antisera using the indirect immunoperoxidase monolayer assay (IPMA). Prototypic European, but not American, PRRSV antisera also recognized BP03-P using western immunoblotting and radioimmunoprecipitation assay (RIPA) procedures. However, gnotobiotically derived antiserum to an atypical American-origin PRRSV was reactive with BP03-P by both IPMA and western immunoblot. Despite a predicted potential for N-linked glycosylation, studies with tunicamycin and peptide-N-glycosidase F (PNGase F) indicated that BP03-P was not N-glycosylated in either insect cell cultures or Trichoplusia ni larvae infected with the recombinant baculovirus. Sera from rabbits inoculated with BP03-P failed to neutralize both the European (Lelystad) and American (ATCC VR-2332) reference isolates of PRRSV and did not react by IPMA with PRRSV-infected cell cultures. Taken together, the data suggest that the carboxyterminal portion of PRRSV ORF 3 encodes a non-neutralizing viral peptide that is partially responsible for the serologic differences noted between European and most American isolates of PRRSV.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>prrsv</json:string><json:string>lelystad</json:string><json:string>prrs</json:string><json:string>recombinant</json:string><json:string>viral</json:string><json:string>reactive</json:string><json:string>microbiology</json:string><json:string>ipma</json:string><json:string>porcine</json:string><json:string>serologic</json:string><json:string>immunoblot</json:string><json:string>katz</json:string><json:string>gnotobiotic</json:string><json:string>veterinary microbiology</json:string><json:string>respiratory syndrome</json:string><json:string>wensvoort</json:string><json:string>baculovirus</json:string><json:string>antigenic</json:string><json:string>cell cultures</json:string><json:string>orfs</json:string><json:string>glycosylation</json:string><json:string>ripa</json:string><json:string>viral antigens</json:string><json:string>more reactive</json:string><json:string>amino acids</json:string><json:string>swine</json:string><json:string>lelystad virus</json:string><json:string>respiratory syndrome virus</json:string><json:string>american swine</json:string><json:string>western immunoblotting</json:string><json:string>syndrome</json:string><json:string>amino</json:string><json:string>antigenic differences</json:string><json:string>carboxyterminal portion</json:string><json:string>serologic analysis</json:string><json:string>serologic differences</json:string><json:string>recombinant fusion protein</json:string><json:string>monoclonal antibodies</json:string><json:string>equine arteritis virus</json:string><json:string>lactate dehydrogenase</json:string><json:string>recombinant protein</json:string><json:string>swine infertility</json:string><json:string>antiserum</json:string><json:string>virus</json:string><json:string>reading frame</json:string><json:string>gnotobiotic swine</json:string><json:string>simian hemorrhagic fever virus</json:string><json:string>western immunoblot</json:string><json:string>nucleocapsid protein</json:string><json:string>protein products</json:string><json:string>american prrs viruses</json:string><json:string>boehringer mannheim</json:string><json:string>gnotobiotic lelystad</json:string><json:string>molecular mass markers</json:string><json:string>differentially reactive</json:string><json:string>hyperimmune rabbit serum</json:string><json:string>radioimmunoprecipitation assay</json:string><json:string>german sera</json:string><json:string>recombinant baculovirus</json:string><json:string>viral antigen</json:string><json:string>native protein</json:string><json:string>structural proteins</json:string><json:string>rabbits inoculated</json:string><json:string>swine pratt</json:string><json:string>experimental reproduction</json:string><json:string>porcine epidemic abortion</json:string></teeft></keywords><author><json:item><name>Jonathan B. Katz</name><affiliations><json:string>U.S. Department of Agriculture, Animal and Plant Health Inspection Service, Veterinary Services, National Veterinary Services Laboratories Ames, IA, USA</json:string></affiliations></json:item><json:item><name>Amy L. Shafer</name><affiliations><json:string>U.S. Department of Agriculture, Animal and Plant Health Inspection Service, Veterinary Services, National Veterinary Services Laboratories Ames, IA, USA</json:string></affiliations></json:item><json:item><name>Kenneth A. Eernisse</name><affiliations><json:string>U.S. Department of Agriculture, Animal and Plant Health Inspection Service, Veterinary Services, National Veterinary Services Laboratories Ames, IA, USA</json:string></affiliations></json:item><json:item><name>John G. Landgraf</name><affiliations><json:string>U.S. Department of Agriculture, Animal and Plant Health Inspection Service, Veterinary Services, National Veterinary Services Laboratories Ames, IA, USA</json:string></affiliations></json:item><json:item><name>Eric A. Nelson</name><affiliations><json:string>Department of Veterinary Science, South Dakota State University Brookings, SD, USA</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Antigen, virus</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Arterivirus</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Serodiagnosis</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Porcine Reproductive and Respiratory Syndrome Virus</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Recombinant protein</value></json:item></subject><arkIstex>ark:/67375/6H6-H3C4S1XJ-K</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: Antigenic differences between European and American isolates of porcine reproductive and respiratory syndrome virus (PRRSV) were revealed by serologic analysis of a recombinant protein derived from PRRSV open reading frame 3 (ORF 3). The hydrophilic carboxyterminal 199 amino acids encoded by the ORF 3 of a European (Lelystad) isolate of PRRSV were expressed as a recombinant fusion protein (BP03-P) in a baculovirus gene expression system. Sera from gnotobiotic swine exposed to prototypic reference European and American isolates of PRRSV and sera from conventionally reared European and American swine convalescing from naturally acquired PRRSV infections were used to characterize the BP03-P protein. Sera from gnotobiotic and conventionally reared swine exposed to European isolates of PRRSV were significantly more reactive (P > 0.01) with BP03-P than were the corresponding American PRRSV antisera using the indirect immunoperoxidase monolayer assay (IPMA). Prototypic European, but not American, PRRSV antisera also recognized BP03-P using western immunoblotting and radioimmunoprecipitation assay (RIPA) procedures. However, gnotobiotically derived antiserum to an atypical American-origin PRRSV was reactive with BP03-P by both IPMA and western immunoblot. Despite a predicted potential for N-linked glycosylation, studies with tunicamycin and peptide-N-glycosidase F (PNGase F) indicated that BP03-P was not N-glycosylated in either insect cell cultures or Trichoplusia ni larvae infected with the recombinant baculovirus. Sera from rabbits inoculated with BP03-P failed to neutralize both the European (Lelystad) and American (ATCC VR-2332) reference isolates of PRRSV and did not react by IPMA with PRRSV-infected cell cultures. Taken together, the data suggest that the carboxyterminal portion of PRRSV ORF 3 encodes a non-neutralizing viral peptide that is partially responsible for the serologic differences noted between European and most American isolates of PRRSV.</abstract><qualityIndicators><score>9.439</score><pdfWordCount>4439</pdfWordCount><pdfCharCount>28533</pdfCharCount><pdfVersion>1.2</pdfVersion><pdfPageCount>12</pdfPageCount><pdfPageSize>461 x 684 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>276</abstractWordCount><abstractCharCount>1994</abstractCharCount><keywordCount>5</keywordCount></qualityIndicators><title>Antigenic differences between European and American isolates of porcine reproductive and respiratory syndrome virus (PRRSV) are encoded by the carboxyterminal portion of viral open reading frame 3</title><pmid><json:string>7667907</json:string></pmid><pii><json:string>0378-1135(94)00113-B</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Proc. Natl. Acad. Sci.</title><language><json:string>unknown</json:string></language><volume>88</volume><pages><first>8972</first><last>8976</last></pages></serie><host><title>Veterinary Microbiology</title><language><json:string>unknown</json:string></language><publicationDate>1995</publicationDate><issn><json:string>0378-1135</json:string></issn><pii><json:string>S0378-1135(00)X0015-6</json:string></pii><volume>44</volume><issue>1</issue><pages><first>65</first><last>76</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1995</json:string></date><geogName></geogName><orgName><json:string>Kirkegaard and Perry Inc.</json:string><json:string>Boehringer Mannheim, Inc.</json:string><json:string>Department of Veterinary Science, South Dakota State Universip Brook</json:string><json:string>Central Veterinary Laboratory, United Kingdom</json:string><json:string>Boehringer Ingelheim Inc.</json:string><json:string>Pharmingen, Inc., San Diego</json:string><json:string>Diagnostic Virology Laboratory, National Veterinary</json:string><json:string>European and American PRRS</json:string><json:string>North American PRRS</json:string><json:string>American PRRSV</json:string><json:string>European and American PRSSV</json:string><json:string>American and European</json:string><json:string>Pfizer, Inc.</json:string><json:string>Services Laboratories</json:string><json:string>American, PRRSV</json:string><json:string>European and American PRRSV</json:string><json:string>Invitrogen, Inc., San Diego</json:string><json:string>Iowa State University</json:string><json:string>Pharmingen, Inc.</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName><json:string>S. Edwards</json:string><json:string>P.O. Box</json:string><json:string>Wayne Romp</json:string><json:string>D. Kinker</json:string><json:string>P. Aliquots</json:string><json:string>D. Chladek</json:string><json:string>Nancy Platter</json:string><json:string>Melanie Harris</json:string><json:string>Tom Glasson</json:string><json:string>P. Lane</json:string><json:string>O.Ol</json:string><json:string>T. Blaha</json:string><json:string>C. Terpstra</json:string></persName><placeName><json:string>Ames</json:string><json:string>Hydropathicity</json:string><json:string>Germany</json:string><json:string>United States</json:string><json:string>IA</json:string><json:string>Hanover</json:string><json:string>IN</json:string><json:string>American</json:string><json:string>Europe</json:string><json:string>USA</json:string><json:string>America</json:string><json:string>Gaithersburg</json:string><json:string>CT</json:string><json:string>San Francisco</json:string><json:string>MD</json:string><json:string>Lelystad</json:string><json:string>CA</json:string><json:string>Groton</json:string><json:string>Indianapolis</json:string><json:string>Netherlands</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Collins et al., 1992</json:string><json:string>Meulenberg et al., 1993</json:string><json:string>J. B. Katz et al.</json:string><json:string>Rademacher et al., 1988</json:string><json:string>Choi et al., 1992</json:string><json:string>J.B. Katz et al.</json:string><json:string>Yoon et al., 1994</json:string><json:string>Godeny et al., 1993</json:string><json:string>Li et al., 1993</json:string><json:string>Janknecht et al.</json:string><json:string>Nelson et al., 1993</json:string><json:string>Saiki et al., 1988</json:string><json:string>Reilly et al., 1992</json:string><json:string>Paton et al., 1991</json:string><json:string>Kyte and Doolittle, 1982</json:string><json:string>Grigera et al., 1991</json:string><json:string>Burnett, 1981</json:string><json:string>Boon et al., 1991</json:string><json:string>Goyal, 1993</json:string><json:string>Bautista et al., 1993</json:string><json:string>Fatunmbi et al., 1992</json:string><json:string>Maniatis et al., 1982</json:string><json:string>Benfield et al., 1992</json:string><json:string>Laemmli, 1970</json:string><json:string>Plagemann and Moennig, 1992</json:string><json:string>Wensvoort et al., 1992</json:string><json:string>Shimokawa and Smith, 1992</json:string><json:string>Kim et al., 1993</json:string><json:string>Boon et al.</json:string><json:string>Conzelmann et al., 1993</json:string><json:string>Terpstra et al., 1991</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-H3C4S1XJ-K</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - veterinary sciences</json:string><json:string>2 - microbiology</json:string></wos><scienceMetrix><json:string>1 - applied sciences</json:string><json:string>2 - agriculture, fisheries & forestry</json:string><json:string>3 - veterinary sciences</json:string></scienceMetrix><scopus><json:string>1 - Health Sciences</json:string><json:string>2 - Veterinary</json:string><json:string>3 - General Veterinary</json:string><json:string>1 - Health Sciences</json:string><json:string>2 - Medicine</json:string><json:string>3 - General Medicine</json:string><json:string>1 - Life Sciences</json:string><json:string>2 - Immunology and Microbiology</json:string><json:string>3 - Microbiology</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></inist></categories><publicationDate>1995</publicationDate><copyrightDate>1995</copyrightDate><doi><json:string>10.1016/0378-1135(94)00113-B</json:string></doi><id>C64535751CAE4C7BB1CA76683EEEF9034EF49389</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-H3C4S1XJ-K/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-H3C4S1XJ-K/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-H3C4S1XJ-K/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a">Antigenic differences between European and American isolates of porcine reproductive and respiratory syndrome virus (PRRSV) are encoded by the carboxyterminal portion of viral open reading frame 3</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>elsevier</p></licence></availability><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M"></p><date>1995</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></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Antigenic differences between European and American isolates of porcine reproductive and respiratory syndrome virus (PRRSV) are encoded by the carboxyterminal portion of viral open reading frame 3</title><author xml:id="author-0000"><persName><forename type="first">Jonathan B.</forename><surname>Katz</surname></persName><note type="correspondence"><p>Corresponding author. Diagnostic Virology Laboratory, National Veterinary Services Laboratories, P.O. Box 844, Ames, IA 50010, USA. Tel: (515) 239-8551; fax: (515) 239-8348</p></note><affiliation>U.S. Department of Agriculture, Animal and Plant Health Inspection Service, Veterinary Services, National Veterinary Services Laboratories Ames, IA, USA</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Amy L.</forename><surname>Shafer</surname></persName><affiliation>U.S. Department of Agriculture, Animal and Plant Health Inspection Service, Veterinary Services, National Veterinary Services Laboratories Ames, IA, USA</affiliation></author><author xml:id="author-0002"><persName><forename type="first">Kenneth A.</forename><surname>Eernisse</surname></persName><affiliation>U.S. Department of Agriculture, Animal and Plant Health Inspection Service, Veterinary Services, National Veterinary Services Laboratories Ames, IA, USA</affiliation></author><author xml:id="author-0003"><persName><forename type="first">John G.</forename><surname>Landgraf</surname></persName><affiliation>U.S. Department of Agriculture, Animal and Plant Health Inspection Service, Veterinary Services, National Veterinary Services Laboratories Ames, IA, USA</affiliation></author><author xml:id="author-0004"><persName><forename type="first">Eric A.</forename><surname>Nelson</surname></persName><affiliation>Department of Veterinary Science, South Dakota State University Brookings, SD, USA</affiliation></author><idno type="istex">C64535751CAE4C7BB1CA76683EEEF9034EF49389</idno><idno type="ark">ark:/67375/6H6-H3C4S1XJ-K</idno><idno type="DOI">10.1016/0378-1135(94)00113-B</idno><idno type="PII">0378-1135(94)00113-B</idno></analytic><monogr><title level="j">Veterinary Microbiology</title><title level="j" type="abbrev">VETMIC</title><idno type="pISSN">0378-1135</idno><idno type="PII">S0378-1135(00)X0015-6</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1995"></date><biblScope unit="volume">44</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="65">65</biblScope><biblScope unit="page" to="76">76</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1995</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: Antigenic differences between European and American isolates of porcine reproductive and respiratory syndrome virus (PRRSV) were revealed by serologic analysis of a recombinant protein derived from PRRSV open reading frame 3 (ORF 3). The hydrophilic carboxyterminal 199 amino acids encoded by the ORF 3 of a European (Lelystad) isolate of PRRSV were expressed as a recombinant fusion protein (BP03-P) in a baculovirus gene expression system. Sera from gnotobiotic swine exposed to prototypic reference European and American isolates of PRRSV and sera from conventionally reared European and American swine convalescing from naturally acquired PRRSV infections were used to characterize the BP03-P protein. Sera from gnotobiotic and conventionally reared swine exposed to European isolates of PRRSV were significantly more reactive (P < 0.01) with BP03-P than were the corresponding American PRRSV antisera using the indirect immunoperoxidase monolayer assay (IPMA). Prototypic European, but not American, PRRSV antisera also recognized BP03-P using western immunoblotting and radioimmunoprecipitation assay (RIPA) procedures. However, gnotobiotically derived antiserum to an atypical American-origin PRRSV was reactive with BP03-P by both IPMA and western immunoblot. Despite a predicted potential for N-linked glycosylation, studies with tunicamycin and peptide-N-glycosidase F (PNGase F) indicated that BP03-P was not N-glycosylated in either insect cell cultures or Trichoplusia ni larvae infected with the recombinant baculovirus. Sera from rabbits inoculated with BP03-P failed to neutralize both the European (Lelystad) and American (ATCC VR-2332) reference isolates of PRRSV and did not react by IPMA with PRRSV-infected cell cultures. Taken together, the data suggest that the carboxyterminal portion of PRRSV ORF 3 encodes a non-neutralizing viral peptide that is partially responsible for the serologic differences noted between European and most American isolates of PRRSV.</p></abstract><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>Antigen, virus</term></item><item><term>Arterivirus</term></item><item><term>Serodiagnosis</term></item><item><term>Porcine Reproductive and Respiratory Syndrome Virus</term></item><item><term>Recombinant protein</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1995">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-H3C4S1XJ-K/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: 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:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>VETMIC</jid><aid>9400113B</aid><ce:pii>0378-1135(94)00113-B</ce:pii><ce:doi>10.1016/0378-1135(94)00113-B</ce:doi><ce:copyright type="unknown" year="1995"></ce:copyright></item-info><head><ce:title>Antigenic differences between European and American isolates of porcine reproductive and respiratory syndrome virus (PRRSV) are encoded by the carboxyterminal portion of viral open reading frame 3</ce:title><ce:author-group><ce:author><ce:given-name>Jonathan B.</ce:given-name><ce:surname>Katz</ce:surname><ce:cross-ref refid="COR1"><ce:sup>∗</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Amy L.</ce:given-name><ce:surname>Shafer</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Kenneth A.</ce:given-name><ce:surname>Eernisse</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>John G.</ce:given-name><ce:surname>Landgraf</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Eric A.</ce:given-name><ce:surname>Nelson</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>b</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>U.S. Department of Agriculture, Animal and Plant Health Inspection Service, Veterinary Services, National Veterinary Services Laboratories Ames, IA, USA</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>Department of Veterinary Science, South Dakota State University Brookings, SD, USA</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>∗</ce:label><ce:text>Corresponding author. Diagnostic Virology Laboratory, National Veterinary Services Laboratories, P.O. Box 844, Ames, IA 50010, USA. Tel: (515) 239-8551; fax: (515) 239-8348</ce:text></ce:correspondence></ce:author-group><ce:date-received day="28" month="4" year="1994"></ce:date-received><ce:date-accepted day="7" month="9" year="1994"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Antigenic differences between European and American isolates of porcine reproductive and respiratory syndrome virus (PRRSV) were revealed by serologic analysis of a recombinant protein derived from PRRSV open reading frame 3 (ORF 3). The hydrophilic carboxyterminal 199 amino acids encoded by the ORF 3 of a European (Lelystad) isolate of PRRSV were expressed as a recombinant fusion protein (BP03-P) in a baculovirus gene expression system. Sera from gnotobiotic swine exposed to prototypic reference European and American isolates of PRRSV and sera from conventionally reared European and American swine convalescing from naturally acquired PRRSV infections were used to characterize the BP03-P protein. Sera from gnotobiotic and conventionally reared swine exposed to European isolates of PRRSV were significantly more reactive (<ce:italic>P</ce:italic> < 0.01) with BP03-P than were the corresponding American PRRSV antisera using the indirect immunoperoxidase monolayer assay (IPMA). Prototypic European, but not American, PRRSV antisera also recognized BP03-P using western immunoblotting and radioimmunoprecipitation assay (RIPA) procedures. However, gnotobiotically derived antiserum to an atypical American-origin PRRSV was reactive with BP03-P by both IPMA and western immunoblot. Despite a predicted potential for N-linked glycosylation, studies with tunicamycin and peptide-N-glycosidase F (PNGase F) indicated that BP03-P was not N-glycosylated in either insect cell cultures or <ce:italic>Trichoplusia ni</ce:italic> larvae infected with the recombinant baculovirus. Sera from rabbits inoculated with BP03-P failed to neutralize both the European (Lelystad) and American (ATCC VR-2332) reference isolates of PRRSV and did not react by IPMA with PRRSV-infected cell cultures. Taken together, the data suggest that the carboxyterminal portion of PRRSV ORF 3 encodes a non-neutralizing viral peptide that is partially responsible for the serologic differences noted between European and most American isolates of PRRSV.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>Antigen, virus</ce:text></ce:keyword><ce:keyword><ce:text>Arterivirus</ce:text></ce:keyword><ce:keyword><ce:text>Serodiagnosis</ce:text></ce:keyword><ce:keyword><ce:text>Porcine Reproductive and Respiratory Syndrome Virus</ce:text></ce:keyword><ce:keyword><ce:text>Recombinant protein</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Antigenic differences between European and American isolates of porcine reproductive and respiratory syndrome virus (PRRSV) are encoded by the carboxyterminal portion of viral open reading frame 3</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Antigenic differences between European and American isolates of porcine reproductive and respiratory syndrome virus (PRRSV) are encoded by the carboxyterminal portion of viral open reading frame 3</title></titleInfo><name type="personal"><namePart type="given">Jonathan B.</namePart><namePart type="family">Katz</namePart><affiliation>U.S. Department of Agriculture, Animal and Plant Health Inspection Service, Veterinary Services, National Veterinary Services Laboratories Ames, IA, USA</affiliation><description>Corresponding author. Diagnostic Virology Laboratory, National Veterinary Services Laboratories, P.O. Box 844, Ames, IA 50010, USA. Tel: (515) 239-8551; fax: (515) 239-8348</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Amy L.</namePart><namePart type="family">Shafer</namePart><affiliation>U.S. Department of Agriculture, Animal and Plant Health Inspection Service, Veterinary Services, National Veterinary Services Laboratories Ames, IA, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Kenneth A.</namePart><namePart type="family">Eernisse</namePart><affiliation>U.S. Department of Agriculture, Animal and Plant Health Inspection Service, Veterinary Services, National Veterinary Services Laboratories Ames, IA, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">John G.</namePart><namePart type="family">Landgraf</namePart><affiliation>U.S. Department of Agriculture, Animal and Plant Health Inspection Service, Veterinary Services, National Veterinary Services Laboratories Ames, IA, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Eric A.</namePart><namePart type="family">Nelson</namePart><affiliation>Department of Veterinary Science, South Dakota State University Brookings, SD, USA</affiliation><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">1995</dateIssued><copyrightDate encoding="w3cdtf">1995</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: Antigenic differences between European and American isolates of porcine reproductive and respiratory syndrome virus (PRRSV) were revealed by serologic analysis of a recombinant protein derived from PRRSV open reading frame 3 (ORF 3). The hydrophilic carboxyterminal 199 amino acids encoded by the ORF 3 of a European (Lelystad) isolate of PRRSV were expressed as a recombinant fusion protein (BP03-P) in a baculovirus gene expression system. Sera from gnotobiotic swine exposed to prototypic reference European and American isolates of PRRSV and sera from conventionally reared European and American swine convalescing from naturally acquired PRRSV infections were used to characterize the BP03-P protein. Sera from gnotobiotic and conventionally reared swine exposed to European isolates of PRRSV were significantly more reactive (P < 0.01) with BP03-P than were the corresponding American PRRSV antisera using the indirect immunoperoxidase monolayer assay (IPMA). Prototypic European, but not American, PRRSV antisera also recognized BP03-P using western immunoblotting and radioimmunoprecipitation assay (RIPA) procedures. However, gnotobiotically derived antiserum to an atypical American-origin PRRSV was reactive with BP03-P by both IPMA and western immunoblot. Despite a predicted potential for N-linked glycosylation, studies with tunicamycin and peptide-N-glycosidase F (PNGase F) indicated that BP03-P was not N-glycosylated in either insect cell cultures or Trichoplusia ni larvae infected with the recombinant baculovirus. Sera from rabbits inoculated with BP03-P failed to neutralize both the European (Lelystad) and American (ATCC VR-2332) reference isolates of PRRSV and did not react by IPMA with PRRSV-infected cell cultures. Taken together, the data suggest that the carboxyterminal portion of PRRSV ORF 3 encodes a non-neutralizing viral peptide that is partially responsible for the serologic differences noted between European and most American isolates of PRRSV.</abstract><subject><genre>Keywords</genre><topic>Antigen, virus</topic><topic>Arterivirus</topic><topic>Serodiagnosis</topic><topic>Porcine Reproductive and Respiratory Syndrome Virus</topic><topic>Recombinant protein</topic></subject><relatedItem type="host"><titleInfo><title>Veterinary Microbiology</title></titleInfo><titleInfo type="abbreviated"><title>VETMIC</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">1995</dateIssued></originInfo><identifier type="ISSN">0378-1135</identifier><identifier type="PII">S0378-1135(00)X0015-6</identifier><part><date>1995</date><detail type="volume"><number>44</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="issue-pages"><start>1</start><end>112</end></extent><extent unit="pages"><start>65</start><end>76</end></extent></part></relatedItem><identifier type="istex">C64535751CAE4C7BB1CA76683EEEF9034EF49389</identifier><identifier type="ark">ark:/67375/6H6-H3C4S1XJ-K</identifier><identifier type="DOI">10.1016/0378-1135(94)00113-B</identifier><identifier type="PII">0378-1135(94)00113-B</identifier><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></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-H3C4S1XJ-K/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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