Characterization of a monoclonal anti-capsid antibody that cross-reacts with three major primate lentivirus lineages
Abstract Mouse monoclonal antibodies with varying specificities against the Gag capsid of simian and human immunodeficiency virus (SIV/HIV) were generated by immunizing mice with whole inactivated SIVagmTYO-1. Monoclonal antibody AG3.0 showed the broadest reactivity recognizing the Gag capsid protei...
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| Veröffentlicht in: | Virology (New York, N.Y.) N.Y.), 2012-01, Vol.422 (2), p.402-412 |
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| container_title | Virology (New York, N.Y.) |
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| creator | Sanders-Beer, Brigitte E Eschricht, Magdalena Seifried, Janna Hirsch, Vanessa M Allan, Jonathan S Norley, Stephen |
| description | Abstract Mouse monoclonal antibodies with varying specificities against the Gag capsid of simian and human immunodeficiency virus (SIV/HIV) were generated by immunizing mice with whole inactivated SIVagmTYO-1. Monoclonal antibody AG3.0 showed the broadest reactivity recognizing the Gag capsid protein (p24–27) and Gag precursors p38, p55, and p150 of HIV-1, HIV-2, SIVmac, and SIVagm. Using overlapping peptides, the AG3.0 epitope was mapped in capsid to a sequence (SPRTLNA) conserved among HIV-1, HIV-2, SIVrcm, SIVsm/mac, and SIVagm related viruses. Because of its broad cross-reactivity, AG3.0 was used to develop an antigen capture assay with a lower detection limit of 100 pg/ml HIV-1 Gag p24. Interestingly, AG3.0 was found to have a faster binding on/off rate for SIVagmVer and SIVmac Gag than for SIVagmSab Gag, possibly due to differences outside the SPRTLNA motif. In addition, the ribonucleic acid (RNA) coding for AG3.0 was sequenced to facilitate the development of humanized monoclonal antibodies. |
| doi_str_mv | 10.1016/j.virol.2011.11.003 |
| format | Article |
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Monoclonal antibody AG3.0 showed the broadest reactivity recognizing the Gag capsid protein (p24–27) and Gag precursors p38, p55, and p150 of HIV-1, HIV-2, SIVmac, and SIVagm. Using overlapping peptides, the AG3.0 epitope was mapped in capsid to a sequence (SPRTLNA) conserved among HIV-1, HIV-2, SIVrcm, SIVsm/mac, and SIVagm related viruses. Because of its broad cross-reactivity, AG3.0 was used to develop an antigen capture assay with a lower detection limit of 100 pg/ml HIV-1 Gag p24. Interestingly, AG3.0 was found to have a faster binding on/off rate for SIVagmVer and SIVmac Gag than for SIVagmSab Gag, possibly due to differences outside the SPRTLNA motif. In addition, the ribonucleic acid (RNA) coding for AG3.0 was sequenced to facilitate the development of humanized monoclonal antibodies.</description><identifier>ISSN: 0042-6822</identifier><identifier>EISSN: 1096-0341</identifier><identifier>DOI: 10.1016/j.virol.2011.11.003</identifier><identifier>PMID: 22153299</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>AG3.0 ; Amino Acid Sequence ; Animals ; Antibodies, Monoclonal - immunology ; Antibodies, Monoclonal - metabolism ; Capsid ; Capsid Proteins - immunology ; CD4-Positive T-Lymphocytes ; Cell Line ; Cross Reactions ; Enzyme-Linked Immunosorbent Assay ; Epitope ; Epitope Mapping ; Gag ; HIV-1 - immunology ; HIV-2 - immunology ; Human immunodeficiency virus ; Human immunodeficiency virus 1 ; Human immunodeficiency virus 2 ; Humans ; Infectious Disease ; Lentivirus ; Mice ; Molecular Sequence Data ; p24 ; p27 ; Primates ; Simian immunodeficiency virus ; Simian Immunodeficiency Virus - immunology ; Simian/human immunodeficiency virus</subject><ispartof>Virology (New York, N.Y.), 2012-01, Vol.422 (2), p.402-412</ispartof><rights>Elsevier Inc.</rights><rights>2011 Elsevier Inc.</rights><rights>Copyright © 2011 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c545t-a5d3201898918fee2afc8ee64b1112559ccae816aaa1e9c0df724d2ea8eb10c23</citedby><cites>FETCH-LOGICAL-c545t-a5d3201898918fee2afc8ee64b1112559ccae816aaa1e9c0df724d2ea8eb10c23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.virol.2011.11.003$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,780,784,885,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22153299$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sanders-Beer, Brigitte E</creatorcontrib><creatorcontrib>Eschricht, Magdalena</creatorcontrib><creatorcontrib>Seifried, Janna</creatorcontrib><creatorcontrib>Hirsch, Vanessa M</creatorcontrib><creatorcontrib>Allan, Jonathan S</creatorcontrib><creatorcontrib>Norley, Stephen</creatorcontrib><title>Characterization of a monoclonal anti-capsid antibody that cross-reacts with three major primate lentivirus lineages</title><title>Virology (New York, N.Y.)</title><addtitle>Virology</addtitle><description>Abstract Mouse monoclonal antibodies with varying specificities against the Gag capsid of simian and human immunodeficiency virus (SIV/HIV) were generated by immunizing mice with whole inactivated SIVagmTYO-1. Monoclonal antibody AG3.0 showed the broadest reactivity recognizing the Gag capsid protein (p24–27) and Gag precursors p38, p55, and p150 of HIV-1, HIV-2, SIVmac, and SIVagm. Using overlapping peptides, the AG3.0 epitope was mapped in capsid to a sequence (SPRTLNA) conserved among HIV-1, HIV-2, SIVrcm, SIVsm/mac, and SIVagm related viruses. Because of its broad cross-reactivity, AG3.0 was used to develop an antigen capture assay with a lower detection limit of 100 pg/ml HIV-1 Gag p24. Interestingly, AG3.0 was found to have a faster binding on/off rate for SIVagmVer and SIVmac Gag than for SIVagmSab Gag, possibly due to differences outside the SPRTLNA motif. In addition, the ribonucleic acid (RNA) coding for AG3.0 was sequenced to facilitate the development of humanized monoclonal antibodies.</description><subject>AG3.0</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Antibodies, Monoclonal - metabolism</subject><subject>Capsid</subject><subject>Capsid Proteins - immunology</subject><subject>CD4-Positive T-Lymphocytes</subject><subject>Cell Line</subject><subject>Cross Reactions</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Epitope</subject><subject>Epitope Mapping</subject><subject>Gag</subject><subject>HIV-1 - immunology</subject><subject>HIV-2 - immunology</subject><subject>Human immunodeficiency virus</subject><subject>Human immunodeficiency virus 1</subject><subject>Human immunodeficiency virus 2</subject><subject>Humans</subject><subject>Infectious Disease</subject><subject>Lentivirus</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>p24</subject><subject>p27</subject><subject>Primates</subject><subject>Simian immunodeficiency virus</subject><subject>Simian Immunodeficiency Virus - immunology</subject><subject>Simian/human immunodeficiency virus</subject><issn>0042-6822</issn><issn>1096-0341</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNUk2P0zAQtRCILQu_AAn5xinF4zhpcmAlVPElrcQBOFtTZ7J1cOJiO12VX4_bLivgAtJI_npv_GbeMPYcxBIE1K-G5d4G75ZSACxzCFE-YAsQbV2IUsFDthBCyaJupLxgT2IcRD6vVuIxu5ASqlK27YKl9RYDmkTB_sBk_cR9z5GPfvLG-QkdxynZwuAu2u603_juwNMWEzfBx1gEyvTIb23a5utAxEccfOC7YEdMxB1lUlY6R-7sRHhD8Sl71KOL9OxuvWRf3739sv5QXH96_3H95rowlapSgVVX5uKatmmh6Ykk9qYhqtUGAGRVtcYgNVAjIlBrRNevpOokYUMbEEaWl-zqnHc3b0bqTFYS0OmTsnDQHq3-82WyW33j97oupYJG5QQv7xIE_32mmPRooyHncCI_R511iUqt4H-QpVKyBcjI8ow8tS9Qf68HhD4aqwd9MlYfjdU5srGZ9eL3Uu45v5zMgNdnAOWG7i0FHY2lyVBnA5mkO2__8cHVX3yT7bIG3Tc6UBz8HPI0RA06Si305-NsHUcLQIhKyqb8CSyQzlw</recordid><startdate>20120120</startdate><enddate>20120120</enddate><creator>Sanders-Beer, Brigitte E</creator><creator>Eschricht, Magdalena</creator><creator>Seifried, Janna</creator><creator>Hirsch, Vanessa M</creator><creator>Allan, Jonathan S</creator><creator>Norley, Stephen</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</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>7X8</scope><scope>7U9</scope><scope>H94</scope><scope>5PM</scope></search><sort><creationdate>20120120</creationdate><title>Characterization of a monoclonal anti-capsid antibody that cross-reacts with three major primate lentivirus lineages</title><author>Sanders-Beer, Brigitte E ; Eschricht, Magdalena ; Seifried, Janna ; Hirsch, Vanessa M ; Allan, Jonathan S ; Norley, Stephen</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c545t-a5d3201898918fee2afc8ee64b1112559ccae816aaa1e9c0df724d2ea8eb10c23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>AG3.0</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibodies, Monoclonal - immunology</topic><topic>Antibodies, Monoclonal - metabolism</topic><topic>Capsid</topic><topic>Capsid Proteins - immunology</topic><topic>CD4-Positive T-Lymphocytes</topic><topic>Cell Line</topic><topic>Cross Reactions</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Epitope</topic><topic>Epitope Mapping</topic><topic>Gag</topic><topic>HIV-1 - immunology</topic><topic>HIV-2 - immunology</topic><topic>Human immunodeficiency virus</topic><topic>Human immunodeficiency virus 1</topic><topic>Human immunodeficiency virus 2</topic><topic>Humans</topic><topic>Infectious Disease</topic><topic>Lentivirus</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>p24</topic><topic>p27</topic><topic>Primates</topic><topic>Simian immunodeficiency virus</topic><topic>Simian Immunodeficiency Virus - immunology</topic><topic>Simian/human immunodeficiency virus</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sanders-Beer, Brigitte E</creatorcontrib><creatorcontrib>Eschricht, Magdalena</creatorcontrib><creatorcontrib>Seifried, Janna</creatorcontrib><creatorcontrib>Hirsch, Vanessa M</creatorcontrib><creatorcontrib>Allan, Jonathan S</creatorcontrib><creatorcontrib>Norley, Stephen</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Virology (New York, N.Y.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sanders-Beer, Brigitte E</au><au>Eschricht, Magdalena</au><au>Seifried, Janna</au><au>Hirsch, Vanessa M</au><au>Allan, Jonathan S</au><au>Norley, Stephen</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of a monoclonal anti-capsid antibody that cross-reacts with three major primate lentivirus lineages</atitle><jtitle>Virology (New York, N.Y.)</jtitle><addtitle>Virology</addtitle><date>2012-01-20</date><risdate>2012</risdate><volume>422</volume><issue>2</issue><spage>402</spage><epage>412</epage><pages>402-412</pages><issn>0042-6822</issn><eissn>1096-0341</eissn><abstract>Abstract Mouse monoclonal antibodies with varying specificities against the Gag capsid of simian and human immunodeficiency virus (SIV/HIV) were generated by immunizing mice with whole inactivated SIVagmTYO-1. Monoclonal antibody AG3.0 showed the broadest reactivity recognizing the Gag capsid protein (p24–27) and Gag precursors p38, p55, and p150 of HIV-1, HIV-2, SIVmac, and SIVagm. Using overlapping peptides, the AG3.0 epitope was mapped in capsid to a sequence (SPRTLNA) conserved among HIV-1, HIV-2, SIVrcm, SIVsm/mac, and SIVagm related viruses. Because of its broad cross-reactivity, AG3.0 was used to develop an antigen capture assay with a lower detection limit of 100 pg/ml HIV-1 Gag p24. Interestingly, AG3.0 was found to have a faster binding on/off rate for SIVagmVer and SIVmac Gag than for SIVagmSab Gag, possibly due to differences outside the SPRTLNA motif. In addition, the ribonucleic acid (RNA) coding for AG3.0 was sequenced to facilitate the development of humanized monoclonal antibodies.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>22153299</pmid><doi>10.1016/j.virol.2011.11.003</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Access via ScienceDirect (Elsevier) |
| subjects | AG3.0 Amino Acid Sequence Animals Antibodies, Monoclonal - immunology Antibodies, Monoclonal - metabolism Capsid Capsid Proteins - immunology CD4-Positive T-Lymphocytes Cell Line Cross Reactions Enzyme-Linked Immunosorbent Assay Epitope Epitope Mapping Gag HIV-1 - immunology HIV-2 - immunology Human immunodeficiency virus Human immunodeficiency virus 1 Human immunodeficiency virus 2 Humans Infectious Disease Lentivirus Mice Molecular Sequence Data p24 p27 Primates Simian immunodeficiency virus Simian Immunodeficiency Virus - immunology Simian/human immunodeficiency virus |
| title | Characterization of a monoclonal anti-capsid antibody that cross-reacts with three major primate lentivirus lineages |
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