Induction of antibodies in rhesus macaques that recognize a fusion-intermediate conformation of HIV-1 gp41
A component to the problem of inducing broad neutralizing HIV-1 gp41 membrane proximal external region (MPER) antibodies is the need to focus the antibody response to the transiently exposed MPER pre-hairpin intermediate neutralization epitope. Here we describe a HIV-1 envelope (Env) gp140 oligomer...
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| Veröffentlicht in: | PloS one 2011-11, Vol.6 (11), p.e27824-e27824 |
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| creator | Dennison, S Moses Sutherland, Laura L Jaeger, Frederick H Anasti, Kara M Parks, Robert Stewart, Shelley Bowman, Cindy Xia, Shi-Mao Zhang, Ruijun Shen, Xiaoying Scearce, Richard M Ofek, Gilad Yang, Yongping Kwong, Peter D Santra, Sampa Liao, Hua-Xin Tomaras, Georgia Letvin, Norman L Chen, Bing Alam, S Munir Haynes, Barton F |
| description | A component to the problem of inducing broad neutralizing HIV-1 gp41 membrane proximal external region (MPER) antibodies is the need to focus the antibody response to the transiently exposed MPER pre-hairpin intermediate neutralization epitope. Here we describe a HIV-1 envelope (Env) gp140 oligomer prime followed by MPER peptide-liposomes boost strategy for eliciting serum antibody responses in rhesus macaques that bind to a gp41 fusion intermediate protein. This Env-liposome immunization strategy induced antibodies to the 2F5 neutralizing epitope ⁶⁶⁴DKW residues, and these antibodies preferentially bound to a gp41 fusion intermediate construct as well as to MPER scaffolds stabilized in the 2F5-bound conformation. However, no serum lipid binding activity was observed nor was serum neutralizing activity for HIV-1 pseudoviruses present. Nonetheless, the Env-liposome prime-boost immunization strategy induced antibodies that recognized a gp41 fusion intermediate protein and was successful in focusing the antibody response to the desired epitope. |
| doi_str_mv | 10.1371/journal.pone.0027824 |
| format | Article |
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Here we describe a HIV-1 envelope (Env) gp140 oligomer prime followed by MPER peptide-liposomes boost strategy for eliciting serum antibody responses in rhesus macaques that bind to a gp41 fusion intermediate protein. This Env-liposome immunization strategy induced antibodies to the 2F5 neutralizing epitope ⁶⁶⁴DKW residues, and these antibodies preferentially bound to a gp41 fusion intermediate construct as well as to MPER scaffolds stabilized in the 2F5-bound conformation. However, no serum lipid binding activity was observed nor was serum neutralizing activity for HIV-1 pseudoviruses present. Nonetheless, the Env-liposome prime-boost immunization strategy induced antibodies that recognized a gp41 fusion intermediate protein and was successful in focusing the antibody response to the desired epitope.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0027824</identifier><identifier>PMID: 22140469</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Animals ; Antibodies ; Antibody Formation - immunology ; Antibody response ; Antibody Specificity - immunology ; Antigenic determinants ; Antigens ; B cells ; Binding sites ; Biology ; Children & youth ; Cross-Priming - immunology ; Deoxyribonucleic acid ; DNA ; Epitopes ; Epitopes - immunology ; Fusion protein ; Glycoprotein gp41 ; Glycoproteins ; Guinea Pigs ; HIV ; HIV Antibodies - blood ; HIV Antibodies - immunology ; HIV Envelope Protein gp41 - chemistry ; HIV Envelope Protein gp41 - immunology ; HIV-1 - immunology ; Hospitals ; Human immunodeficiency virus ; Immunization ; Immunoglobulins ; Infections ; Infectious diseases ; Lipids ; Liposomes ; Liposomes - chemistry ; Macaca mulatta - immunology ; Medicine ; Neutralization ; Neutralization Tests ; Neutralizing ; Peptides ; Peptides - chemistry ; Peptides - immunology ; Physicians ; Protein binding ; Protein Structure, Quaternary ; Proteins ; Recombinant Fusion Proteins - metabolism ; Scaffolds ; Strategy ; Well construction ; Yang, Cindy</subject><ispartof>PloS one, 2011-11, Vol.6 (11), p.e27824-e27824</ispartof><rights>COPYRIGHT 2011 Public Library of Science</rights><rights>2011 Dennison et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Dennison et al. 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c691t-a7d1bc5383c1c175df26fd751e9202e1d37fa59d5f38cb1d2a4d2b75f10fbf543</citedby><cites>FETCH-LOGICAL-c691t-a7d1bc5383c1c175df26fd751e9202e1d37fa59d5f38cb1d2a4d2b75f10fbf543</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3227606/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3227606/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2095,2914,23846,27903,27904,53769,53771,79346,79347</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22140469$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Goepfert, Paul A.</contributor><creatorcontrib>Dennison, S Moses</creatorcontrib><creatorcontrib>Sutherland, Laura L</creatorcontrib><creatorcontrib>Jaeger, Frederick H</creatorcontrib><creatorcontrib>Anasti, Kara M</creatorcontrib><creatorcontrib>Parks, Robert</creatorcontrib><creatorcontrib>Stewart, Shelley</creatorcontrib><creatorcontrib>Bowman, Cindy</creatorcontrib><creatorcontrib>Xia, Shi-Mao</creatorcontrib><creatorcontrib>Zhang, Ruijun</creatorcontrib><creatorcontrib>Shen, Xiaoying</creatorcontrib><creatorcontrib>Scearce, Richard M</creatorcontrib><creatorcontrib>Ofek, Gilad</creatorcontrib><creatorcontrib>Yang, Yongping</creatorcontrib><creatorcontrib>Kwong, Peter D</creatorcontrib><creatorcontrib>Santra, Sampa</creatorcontrib><creatorcontrib>Liao, Hua-Xin</creatorcontrib><creatorcontrib>Tomaras, Georgia</creatorcontrib><creatorcontrib>Letvin, Norman L</creatorcontrib><creatorcontrib>Chen, Bing</creatorcontrib><creatorcontrib>Alam, S Munir</creatorcontrib><creatorcontrib>Haynes, Barton F</creatorcontrib><title>Induction of antibodies in rhesus macaques that recognize a fusion-intermediate conformation of HIV-1 gp41</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>A component to the problem of inducing broad neutralizing HIV-1 gp41 membrane proximal external region (MPER) antibodies is the need to focus the antibody response to the transiently exposed MPER pre-hairpin intermediate neutralization epitope. Here we describe a HIV-1 envelope (Env) gp140 oligomer prime followed by MPER peptide-liposomes boost strategy for eliciting serum antibody responses in rhesus macaques that bind to a gp41 fusion intermediate protein. This Env-liposome immunization strategy induced antibodies to the 2F5 neutralizing epitope ⁶⁶⁴DKW residues, and these antibodies preferentially bound to a gp41 fusion intermediate construct as well as to MPER scaffolds stabilized in the 2F5-bound conformation. However, no serum lipid binding activity was observed nor was serum neutralizing activity for HIV-1 pseudoviruses present. Nonetheless, the Env-liposome prime-boost immunization strategy induced antibodies that recognized a gp41 fusion intermediate protein and was successful in focusing the antibody response to the desired epitope.</description><subject>Animals</subject><subject>Antibodies</subject><subject>Antibody Formation - immunology</subject><subject>Antibody response</subject><subject>Antibody Specificity - immunology</subject><subject>Antigenic determinants</subject><subject>Antigens</subject><subject>B cells</subject><subject>Binding sites</subject><subject>Biology</subject><subject>Children & youth</subject><subject>Cross-Priming - immunology</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>Epitopes</subject><subject>Epitopes - immunology</subject><subject>Fusion protein</subject><subject>Glycoprotein gp41</subject><subject>Glycoproteins</subject><subject>Guinea Pigs</subject><subject>HIV</subject><subject>HIV Antibodies - blood</subject><subject>HIV Antibodies - immunology</subject><subject>HIV Envelope Protein gp41 - chemistry</subject><subject>HIV Envelope Protein gp41 - immunology</subject><subject>HIV-1 - immunology</subject><subject>Hospitals</subject><subject>Human immunodeficiency virus</subject><subject>Immunization</subject><subject>Immunoglobulins</subject><subject>Infections</subject><subject>Infectious diseases</subject><subject>Lipids</subject><subject>Liposomes</subject><subject>Liposomes - chemistry</subject><subject>Macaca mulatta - immunology</subject><subject>Medicine</subject><subject>Neutralization</subject><subject>Neutralization Tests</subject><subject>Neutralizing</subject><subject>Peptides</subject><subject>Peptides - chemistry</subject><subject>Peptides - immunology</subject><subject>Physicians</subject><subject>Protein binding</subject><subject>Protein Structure, Quaternary</subject><subject>Proteins</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Scaffolds</subject><subject>Strategy</subject><subject>Well construction</subject><subject>Yang, 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of antibodies in rhesus macaques that recognize a fusion-intermediate conformation of HIV-1 gp41</title><author>Dennison, S Moses ; Sutherland, Laura L ; Jaeger, Frederick H ; Anasti, Kara M ; Parks, Robert ; Stewart, Shelley ; Bowman, Cindy ; Xia, Shi-Mao ; Zhang, Ruijun ; Shen, Xiaoying ; Scearce, Richard M ; Ofek, Gilad ; Yang, Yongping ; Kwong, Peter D ; Santra, Sampa ; Liao, Hua-Xin ; Tomaras, Georgia ; Letvin, Norman L ; Chen, Bing ; Alam, S Munir ; Haynes, Barton F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c691t-a7d1bc5383c1c175df26fd751e9202e1d37fa59d5f38cb1d2a4d2b75f10fbf543</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Animals</topic><topic>Antibodies</topic><topic>Antibody Formation - immunology</topic><topic>Antibody response</topic><topic>Antibody Specificity - immunology</topic><topic>Antigenic determinants</topic><topic>Antigens</topic><topic>B 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gp41</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2011-11-30</date><risdate>2011</risdate><volume>6</volume><issue>11</issue><spage>e27824</spage><epage>e27824</epage><pages>e27824-e27824</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>A component to the problem of inducing broad neutralizing HIV-1 gp41 membrane proximal external region (MPER) antibodies is the need to focus the antibody response to the transiently exposed MPER pre-hairpin intermediate neutralization epitope. Here we describe a HIV-1 envelope (Env) gp140 oligomer prime followed by MPER peptide-liposomes boost strategy for eliciting serum antibody responses in rhesus macaques that bind to a gp41 fusion intermediate protein. This Env-liposome immunization strategy induced antibodies to the 2F5 neutralizing epitope ⁶⁶⁴DKW residues, and these antibodies preferentially bound to a gp41 fusion intermediate construct as well as to MPER scaffolds stabilized in the 2F5-bound conformation. However, no serum lipid binding activity was observed nor was serum neutralizing activity for HIV-1 pseudoviruses present. Nonetheless, the Env-liposome prime-boost immunization strategy induced antibodies that recognized a gp41 fusion intermediate protein and was successful in focusing the antibody response to the desired epitope.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>22140469</pmid><doi>10.1371/journal.pone.0027824</doi><tpages>e27824</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2011-11, Vol.6 (11), p.e27824-e27824 |
| issn | 1932-6203 1932-6203 |
| language | eng |
| recordid | cdi_plos_journals_1317915214 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Public Library of Science (PLoS); PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Animals Antibodies Antibody Formation - immunology Antibody response Antibody Specificity - immunology Antigenic determinants Antigens B cells Binding sites Biology Children & youth Cross-Priming - immunology Deoxyribonucleic acid DNA Epitopes Epitopes - immunology Fusion protein Glycoprotein gp41 Glycoproteins Guinea Pigs HIV HIV Antibodies - blood HIV Antibodies - immunology HIV Envelope Protein gp41 - chemistry HIV Envelope Protein gp41 - immunology HIV-1 - immunology Hospitals Human immunodeficiency virus Immunization Immunoglobulins Infections Infectious diseases Lipids Liposomes Liposomes - chemistry Macaca mulatta - immunology Medicine Neutralization Neutralization Tests Neutralizing Peptides Peptides - chemistry Peptides - immunology Physicians Protein binding Protein Structure, Quaternary Proteins Recombinant Fusion Proteins - metabolism Scaffolds Strategy Well construction Yang, Cindy |
| title | Induction of antibodies in rhesus macaques that recognize a fusion-intermediate conformation of HIV-1 gp41 |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-23T23%3A28%3A34IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Induction%20of%20antibodies%20in%20rhesus%20macaques%20that%20recognize%20a%20fusion-intermediate%20conformation%20of%20HIV-1%20gp41&rft.jtitle=PloS%20one&rft.au=Dennison,%20S%20Moses&rft.date=2011-11-30&rft.volume=6&rft.issue=11&rft.spage=e27824&rft.epage=e27824&rft.pages=e27824-e27824&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0027824&rft_dat=%3Cgale_plos_%3EA476861389%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1317915214&rft_id=info:pmid/22140469&rft_galeid=A476861389&rft_doaj_id=oai_doaj_org_article_d801a98ba7d142af95ee9b07aa0ca372&rfr_iscdi=true |