Structural definition of a conserved neutralization epitope on HIV-1 gp120
Identifieur interne : 004168 ( Main/Exploration ); précédent : 004167; suivant : 004169Structural definition of a conserved neutralization epitope on HIV-1 gp120
Auteurs : Tongqing Zhou ; Ling Xu ; Barna Dey ; Ann J. Hessell [États-Unis] ; Donald Van Ryk [États-Unis] ; Shi-Hua Xiang [États-Unis] ; Xinzhen Yang [États-Unis] ; Mei-Yun Zhang [États-Unis] ; Michael B. Zwick [États-Unis] ; James Arthos [États-Unis] ; Dennis R. Burton [États-Unis] ; Dimiter S. Dimitrov [États-Unis] ; Joseph Sodroski [États-Unis] ; Richard Wyatt ; Gary J. Nabel ; Peter D. KwongSource :
- Nature [ 0028-0836 ] ; 2007-02-15.
Abstract
The remarkable diversity, glycosylation and conformational flexibility of the human immunodeficiency virus type 1 (HIV-1) envelope (Env), including substantial rearrangement of the gp120 glycoprotein upon binding the CD4 receptor, allow it to evade antibody-mediated neutralization. Despite this complexity, the HIV-1 Env must retain conserved determinants that mediate CD4 binding. To evaluate how these determinants might provide opportunities for antibody recognition, we created variants of gp120 stabilized in the CD4-bound state, assessed binding of CD4 and of receptor-binding-site antibodies, and determined the structure at 2.3 Å resolution of the broadly neutralizing antibody b12 in complex with gp120. b12 binds to a conformationally invariant surface that overlaps a distinct subset of the CD4-binding site. This surface is involved in the metastable attachment of CD4, before the gp120 rearrangement required for stable engagement. A site of vulnerability, related to a functional requirement for efficient association with CD4, can therefore be targeted by antibody to neutralize HIV-1.
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DOI: 10.1038/nature05580
Affiliations:
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Kwong</name><affiliation></affiliation><affiliation><wicri:noCountry code="no comma">E-mail: pdkwong@nih.gov</wicri:noCountry></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Nature</title><idno type="ISSN">0028-0836</idno><idno type="eISSN">1476-4687</idno><imprint><publisher>Nature Publishing Group</publisher><date when="2007-02-15">2007-02-15</date><biblScope unit="vol">445</biblScope><biblScope unit="issue">7129</biblScope><biblScope unit="page" from="732">732</biblScope><biblScope unit="page" to="737">737</biblScope><date type="Copyright" when="2006">2006</date></imprint><idno type="ISSN">0028-0836</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0028-0836</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="eng">The remarkable diversity, glycosylation and conformational flexibility of the human immunodeficiency virus type 1 (HIV-1) envelope (Env), including substantial rearrangement of the gp120 glycoprotein upon binding the CD4 receptor, allow it to evade antibody-mediated neutralization. Despite this complexity, the HIV-1 Env must retain conserved determinants that mediate CD4 binding. To evaluate how these determinants might provide opportunities for antibody recognition, we created variants of gp120 stabilized in the CD4-bound state, assessed binding of CD4 and of receptor-binding-site antibodies, and determined the structure at 2.3 Å resolution of the broadly neutralizing antibody b12 in complex with gp120. b12 binds to a conformationally invariant surface that overlaps a distinct subset of the CD4-binding site. This surface is involved in the metastable attachment of CD4, before the gp120 rearrangement required for stable engagement. A site of vulnerability, related to a functional requirement for efficient association with CD4, can therefore be targeted by antibody to neutralize HIV-1.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Dey, Barna" sort="Dey, Barna" uniqKey="Dey B" first="Barna" last="Dey">Barna Dey</name><name sortKey="Kwong, Peter D" sort="Kwong, Peter D" uniqKey="Kwong P" first="Peter D." last="Kwong">Peter D. Kwong</name><name sortKey="Nabel, Gary J" sort="Nabel, Gary J" uniqKey="Nabel G" first="Gary J." last="Nabel">Gary J. Nabel</name><name sortKey="Wyatt, Richard" sort="Wyatt, Richard" uniqKey="Wyatt R" first="Richard" last="Wyatt">Richard Wyatt</name><name sortKey="Xu, Ling" sort="Xu, Ling" uniqKey="Xu L" first="Ling" last="Xu">Ling Xu</name><name sortKey="Zhou, Tongqing" sort="Zhou, Tongqing" uniqKey="Zhou T" first="Tongqing" last="Zhou">Tongqing Zhou</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Hessell, Ann J" sort="Hessell, Ann J" uniqKey="Hessell A" first="Ann J." last="Hessell">Ann J. Hessell</name></noRegion><name sortKey="Arthos, James" sort="Arthos, James" uniqKey="Arthos J" first="James" last="Arthos">James Arthos</name><name sortKey="Burton, Dennis R" sort="Burton, Dennis R" uniqKey="Burton D" first="Dennis R." last="Burton">Dennis R. Burton</name><name sortKey="Dimitrov, Dimiter S" sort="Dimitrov, Dimiter S" uniqKey="Dimitrov D" first="Dimiter S." last="Dimitrov">Dimiter S. Dimitrov</name><name sortKey="Sodroski, Joseph" sort="Sodroski, Joseph" uniqKey="Sodroski J" first="Joseph" last="Sodroski">Joseph Sodroski</name><name sortKey="Van Ryk, Donald" sort="Van Ryk, Donald" uniqKey="Van Ryk D" first="Donald" last="Van Ryk">Donald Van Ryk</name><name sortKey="Xiang, Shi Hua" sort="Xiang, Shi Hua" uniqKey="Xiang S" first="Shi-Hua" last="Xiang">Shi-Hua Xiang</name><name sortKey="Yang, Xinzhen" sort="Yang, Xinzhen" uniqKey="Yang X" first="Xinzhen" last="Yang">Xinzhen Yang</name><name sortKey="Zhang, Mei Yun" sort="Zhang, Mei Yun" uniqKey="Zhang M" first="Mei-Yun" last="Zhang">Mei-Yun Zhang</name><name sortKey="Zwick, Michael B" sort="Zwick, Michael B" uniqKey="Zwick M" first="Michael B." last="Zwick">Michael B. Zwick</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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