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Production of polyclonal antibodies against the S and preS2 regions of woodchuck hepatitis virus: lack of detectable low glycosylated preS2 protein (GP33) in sera from infected animals
UPR 41 CNRS Recombinaisons Génétiques, Centre Hayem, Hôpital Saint-Louis, 75475 Paris Cedex 10, France Polyclonal antibodies directed against the preS2 and S domains of the woodchuck hepatitis virus (WHV) envelope proteins were prepared using synthetic peptides and fusion polypeptides as immunogens....
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Published in: | Journal of general virology 1991-02, Vol.72 (2), p.421-425 |
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container_title | Journal of general virology |
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creator | Shamoon, Blanche-Marie Kay, Alan Dupont de Dinechin, Stephane Galibert, Francis Mandart, Elisabeth |
description | UPR 41 CNRS Recombinaisons Génétiques, Centre Hayem, Hôpital Saint-Louis, 75475 Paris Cedex 10, France
Polyclonal antibodies directed against the preS2 and S domains of the woodchuck hepatitis virus (WHV) envelope proteins were prepared using synthetic peptides and fusion polypeptides as immunogens. They were tested by immunoblotting and immunoprecipitation of infected woodchuck sera and lysates of a eukaryotic cell line expressing WHV envelope proteins. Only one anti-peptide serum directed against the preS2 domain was reactive with WHV envelope proteins, recognizing the preS2 and preS1 proteins by their preS2 epitopes. With recombinant fusion proteins we generated several anti-S sera, which recognized all envelope proteins, and anti-preS2 antisera, which recognized the preS proteins. Results obtained with our antisera showed that sera of infected woodchucks lack the low glycosylated form (GP33) of the preS2 protein, unlike human hepatitis B virus.
Present address: UPR 2420 CNRS, Centre de Génétique Moléculaire, avenue de la Terrasse, 91198 Gif-sur-Yvette, France
Received 4 July 1990;
accepted 22 October 1990. |
doi_str_mv | 10.1099/0022-1317-72-2-421 |
format | article |
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Polyclonal antibodies directed against the preS2 and S domains of the woodchuck hepatitis virus (WHV) envelope proteins were prepared using synthetic peptides and fusion polypeptides as immunogens. They were tested by immunoblotting and immunoprecipitation of infected woodchuck sera and lysates of a eukaryotic cell line expressing WHV envelope proteins. Only one anti-peptide serum directed against the preS2 domain was reactive with WHV envelope proteins, recognizing the preS2 and preS1 proteins by their preS2 epitopes. With recombinant fusion proteins we generated several anti-S sera, which recognized all envelope proteins, and anti-preS2 antisera, which recognized the preS proteins. Results obtained with our antisera showed that sera of infected woodchucks lack the low glycosylated form (GP33) of the preS2 protein, unlike human hepatitis B virus.
Present address: UPR 2420 CNRS, Centre de Génétique Moléculaire, avenue de la Terrasse, 91198 Gif-sur-Yvette, France
Received 4 July 1990;
accepted 22 October 1990.</description><identifier>ISSN: 0022-1317</identifier><identifier>EISSN: 1465-2099</identifier><identifier>DOI: 10.1099/0022-1317-72-2-421</identifier><identifier>PMID: 1993879</identifier><identifier>CODEN: JGVIAY</identifier><language>eng</language><publisher>Reading: Soc General Microbiol</publisher><subject>Animals ; Antibodies, Viral - immunology ; Biological and medical sciences ; Fundamental and applied biological sciences. Psychology ; Glycosylation ; Hepadnaviridae - immunology ; Hepatitis, Viral, Animal - immunology ; Hepatitis, Viral, Animal - microbiology ; Immunoblotting ; Marmota ; Microbiology ; Precipitin Tests ; Protein Precursors - blood ; Protein Precursors - immunology ; Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains ; Viral Envelope Proteins - blood ; Viral Envelope Proteins - immunology ; Virology</subject><ispartof>Journal of general virology, 1991-02, Vol.72 (2), p.421-425</ispartof><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c435t-b8c8c48c7a11a23ed7e5ecceb6c4a4bad91d3ce358a23585e2075164541c65663</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,778,782,27911,27912</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19665076$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1993879$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shamoon, Blanche-Marie</creatorcontrib><creatorcontrib>Kay, Alan</creatorcontrib><creatorcontrib>Dupont de Dinechin, Stephane</creatorcontrib><creatorcontrib>Galibert, Francis</creatorcontrib><creatorcontrib>Mandart, Elisabeth</creatorcontrib><title>Production of polyclonal antibodies against the S and preS2 regions of woodchuck hepatitis virus: lack of detectable low glycosylated preS2 protein (GP33) in sera from infected animals</title><title>Journal of general virology</title><addtitle>J Gen Virol</addtitle><description>UPR 41 CNRS Recombinaisons Génétiques, Centre Hayem, Hôpital Saint-Louis, 75475 Paris Cedex 10, France
Polyclonal antibodies directed against the preS2 and S domains of the woodchuck hepatitis virus (WHV) envelope proteins were prepared using synthetic peptides and fusion polypeptides as immunogens. They were tested by immunoblotting and immunoprecipitation of infected woodchuck sera and lysates of a eukaryotic cell line expressing WHV envelope proteins. Only one anti-peptide serum directed against the preS2 domain was reactive with WHV envelope proteins, recognizing the preS2 and preS1 proteins by their preS2 epitopes. With recombinant fusion proteins we generated several anti-S sera, which recognized all envelope proteins, and anti-preS2 antisera, which recognized the preS proteins. Results obtained with our antisera showed that sera of infected woodchucks lack the low glycosylated form (GP33) of the preS2 protein, unlike human hepatitis B virus.
Present address: UPR 2420 CNRS, Centre de Génétique Moléculaire, avenue de la Terrasse, 91198 Gif-sur-Yvette, France
Received 4 July 1990;
accepted 22 October 1990.</description><subject>Animals</subject><subject>Antibodies, Viral - immunology</subject><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycosylation</subject><subject>Hepadnaviridae - immunology</subject><subject>Hepatitis, Viral, Animal - immunology</subject><subject>Hepatitis, Viral, Animal - microbiology</subject><subject>Immunoblotting</subject><subject>Marmota</subject><subject>Microbiology</subject><subject>Precipitin Tests</subject><subject>Protein Precursors - blood</subject><subject>Protein Precursors - immunology</subject><subject>Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains</subject><subject>Viral Envelope Proteins - blood</subject><subject>Viral Envelope Proteins - immunology</subject><subject>Virology</subject><issn>0022-1317</issn><issn>1465-2099</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><recordid>eNqFUctu1DAUjRCoDIUfQELyhtci4GecsEMVFKRKVCqsLce5SQxOnNoOo_kzPg9HMxR2rK7t87rWKYqnBL8huGneYkxpSRiRpaQlLTkl94od4ZUoaYbvF7s7wsPiUYzfMSacC3lWnJGmYbVsdsWv6-C71STrZ-R7tHh3MM7P2iE9J9v6zkJEetB2jgmlEdBNBjq0BLihKMCQdXET7r3vzLiaH2iERSebbEQ_bVjjO-R0fs2UDhKYpFsHyPk9GnKSjwenE_zxW4JPYGf06vKasdconyIEjfrgp3zpszpT9Wwn7eLj4kGfBzw5zfPi28cPXy8-lVdfLj9fvL8qDWcilW1tasNrIzUhmjLoJAgwBtrKcM1b3TWkYwaYqDMqagEUS0EqLjgxlagqdl68OPrm5W5XiElNNhpwTs_g16hqzLmsKf8vkYiGEMo2R3okmuBjDNCrJeQvhYMiWG29qq02tdWmJFVU5V6z6NnJfW0n6P5KjkVm_PkJ19Fo1wc9Gxv_oVWVwHILf3nkjXYY9zaAGmCebF6ltV7lxu4SfwOIYrtF</recordid><startdate>19910201</startdate><enddate>19910201</enddate><creator>Shamoon, Blanche-Marie</creator><creator>Kay, Alan</creator><creator>Dupont de Dinechin, Stephane</creator><creator>Galibert, Francis</creator><creator>Mandart, Elisabeth</creator><general>Soc General Microbiol</general><general>Society for General Microbiology</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7T5</scope><scope>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19910201</creationdate><title>Production of polyclonal antibodies against the S and preS2 regions of woodchuck hepatitis virus: lack of detectable low glycosylated preS2 protein (GP33) in sera from infected animals</title><author>Shamoon, Blanche-Marie ; Kay, Alan ; Dupont de Dinechin, Stephane ; Galibert, Francis ; Mandart, Elisabeth</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c435t-b8c8c48c7a11a23ed7e5ecceb6c4a4bad91d3ce358a23585e2075164541c65663</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Animals</topic><topic>Antibodies, Viral - immunology</topic><topic>Biological and medical sciences</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycosylation</topic><topic>Hepadnaviridae - immunology</topic><topic>Hepatitis, Viral, Animal - immunology</topic><topic>Hepatitis, Viral, Animal - microbiology</topic><topic>Immunoblotting</topic><topic>Marmota</topic><topic>Microbiology</topic><topic>Precipitin Tests</topic><topic>Protein Precursors - blood</topic><topic>Protein Precursors - immunology</topic><topic>Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains</topic><topic>Viral Envelope Proteins - blood</topic><topic>Viral Envelope Proteins - immunology</topic><topic>Virology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shamoon, Blanche-Marie</creatorcontrib><creatorcontrib>Kay, Alan</creatorcontrib><creatorcontrib>Dupont de Dinechin, Stephane</creatorcontrib><creatorcontrib>Galibert, Francis</creatorcontrib><creatorcontrib>Mandart, Elisabeth</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of general virology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shamoon, Blanche-Marie</au><au>Kay, Alan</au><au>Dupont de Dinechin, Stephane</au><au>Galibert, Francis</au><au>Mandart, Elisabeth</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Production of polyclonal antibodies against the S and preS2 regions of woodchuck hepatitis virus: lack of detectable low glycosylated preS2 protein (GP33) in sera from infected animals</atitle><jtitle>Journal of general virology</jtitle><addtitle>J Gen Virol</addtitle><date>1991-02-01</date><risdate>1991</risdate><volume>72</volume><issue>2</issue><spage>421</spage><epage>425</epage><pages>421-425</pages><issn>0022-1317</issn><eissn>1465-2099</eissn><coden>JGVIAY</coden><abstract>UPR 41 CNRS Recombinaisons Génétiques, Centre Hayem, Hôpital Saint-Louis, 75475 Paris Cedex 10, France
Polyclonal antibodies directed against the preS2 and S domains of the woodchuck hepatitis virus (WHV) envelope proteins were prepared using synthetic peptides and fusion polypeptides as immunogens. They were tested by immunoblotting and immunoprecipitation of infected woodchuck sera and lysates of a eukaryotic cell line expressing WHV envelope proteins. Only one anti-peptide serum directed against the preS2 domain was reactive with WHV envelope proteins, recognizing the preS2 and preS1 proteins by their preS2 epitopes. With recombinant fusion proteins we generated several anti-S sera, which recognized all envelope proteins, and anti-preS2 antisera, which recognized the preS proteins. Results obtained with our antisera showed that sera of infected woodchucks lack the low glycosylated form (GP33) of the preS2 protein, unlike human hepatitis B virus.
Present address: UPR 2420 CNRS, Centre de Génétique Moléculaire, avenue de la Terrasse, 91198 Gif-sur-Yvette, France
Received 4 July 1990;
accepted 22 October 1990.</abstract><cop>Reading</cop><pub>Soc General Microbiol</pub><pmid>1993879</pmid><doi>10.1099/0022-1317-72-2-421</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Animals Antibodies, Viral - immunology Biological and medical sciences Fundamental and applied biological sciences. Psychology Glycosylation Hepadnaviridae - immunology Hepatitis, Viral, Animal - immunology Hepatitis, Viral, Animal - microbiology Immunoblotting Marmota Microbiology Precipitin Tests Protein Precursors - blood Protein Precursors - immunology Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains Viral Envelope Proteins - blood Viral Envelope Proteins - immunology Virology |
title | Production of polyclonal antibodies against the S and preS2 regions of woodchuck hepatitis virus: lack of detectable low glycosylated preS2 protein (GP33) in sera from infected animals |
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