Binding of the 2F5 monoclonal antibody to native and fusion-intermediate forms of human immunodeficiency virus type 1 gp41: Implications for fusion-inducing conformational changes

被引：76

作者：

de Rosny, E

Vassell, R

Jiang, S

Kunert, R

Weiss, CD

机构：

[1] US FDA, Ctr Biol Evaluat & Res, Bethesda, MD 20892 USA

[2] New York Blood Ctr, Lindsley F Kimball Res Inst, New York, NY 10021 USA

[3] Univ Nat Resources & Appl Life Sci Vienna, Inst Appl Microbiol, A-1180 Vienna, Austria

来源：

JOURNAL OF VIROLOGY | 2004年 / 78卷 / 05期

关键词：

D O I：

10.1128/JVI.78.5.2627-2631.2004

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

We investigated how the broadly neutralizing monoclonal antibody 2F5 affects the human immunodeficiency virus type 1 envelope glycoprotein as it undergoes receptor-induced conformational changes and show that 2F5 binds both native and fusion-intermediate conformations, suggesting inhibition of a late step in virus entry. We also demonstrate conformational changes in the C heptad of gp41.

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页码：2627 / 2631

页数：5

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共 42 条

[1] Structural analysis of the epitope of the Anti-HIV antibody 2F5 sheds light into its mechanism of neutralization and HIV fusion [J].

Barbato, G ;

Bianchi, E ;

Ingallinella, P ;

Hurni, WH ;

Miller, MD ;

Cilibertol, G ;

Cortese, R ;

Bazzo, R ;

Shiver, JW ;

Pessi, A .

JOURNAL OF MOLECULAR BIOLOGY, 2003, 330 (05) :1101-1115

[2] A monomeric 310-helix is formed in water by a 13-residue peptide representing the neutralizing determinant of HIV-1 on gp41 [J].

Biron, Z ;

Khare, S ;

Samson, AO ;

Hayek, Y ;

Naider, F ;

Anglister, J .

BIOCHEMISTRY, 2002, 41 (42) :12687-12696

[3] A SPRING-LOADED MECHANISM FOR THE CONFORMATIONAL CHANGE OF INFLUENZA HEMAGGLUTININ [J].

CARR, CM ;

KIM, PS .

CELL, 1993, 73 (04) :823-832

[4] Core structure of gp41 from the HIV envelope glycoprotein [J].

Chan, DC ;

Fass, D ;

Berger, JM ;

Kim, PS .

CELL, 1997, 89 (02) :263-273

[5] HIV entry and its inhibition [J].

Chan, DC ;

Kim, PS .

CELL, 1998, 93 (05) :681-684

[6] Peptides corresponding to the heptad repeat motifs in the transmembrane protein (gp41) of human immunodeficiency virus type 1 elicit antibodies to receptor-activated conformations of the envelope glycoprotein [J].

De Rosny, E ;

Vassell, R ;

Wingfield, PT ;

Wild, CT ;

Weiss, CD .

JOURNAL OF VIROLOGY, 2001, 75 (18) :8859-8863

[7] NATIVE OLIGOMERIC HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 ENVELOPE GLYCOPROTEIN ELICITS DIVERSE MONOCLONAL-ANTIBODY REACTIVITIES [J].

EARL, PL ;

BRODER, CC ;

LONG, D ;

LEE, SA ;

PETERSON, J ;

CHAKRABARTI, S ;

DOMS, RW ;

MOSS, B .

JOURNAL OF VIROLOGY, 1994, 68 (05) :3015-3026

[8] Epitope map of human immunodeficiency virus type 1 gp41 derived from 47 monoclonal antibodies produced by immunization with oligomeric envelope protein [J].

Earl, PL ;

Broder, CC ;

Doms, RW ;

Moss, B .

JOURNAL OF VIROLOGY, 1997, 71 (04) :2674-2684

[9] Antigenic properties of the human immunodeficiency virus transmembrane glycoprotein during cell-cell fusion [J].

Finnegan, CM ;

Berg, W ;

Lewis, GK ;

DeVico, AL .

JOURNAL OF VIROLOGY, 2002, 76 (23) :12123-12134

[10] Genetic evidence that interhelical packing interactions in the gp41 core are critical for transition of the human immunodeficiency virus type 1 envelope glycoprotein to the fusion-active state [J].

Follis, KE ;

Larson, SJ ;

Lu, M ;

Nunberg, JH .

JOURNAL OF VIROLOGY, 2002, 76 (14) :7356-7362

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