NDLI: Neutralizing antibodies to human immunodeficiency virus type-1 gp120 induce envelope glycoprotein subunit dissociation.

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Neutralizing antibodies to human immunodeficiency virus type-1 gp120 induce envelope glycoprotein subunit dissociation.

Content Provider	Scilit
Author	Poignard, P. Fouts, Timothy Naniche, D. Moore, J. P. Sattentau, Q. J.
Copyright Year	1996
Description	The spectrum of the anti-human immunodeficiency virus (HIV) neutralizing immune response has been analyzed by the production and characterization of monoclonal antibodies (mAbs) to the viral envelope glycoproteins, gp41 and gp120. Little is known, however, about the neutralization mechanism of these antibodies. Here we show that the binding of a group of neutralizing mAbs that react with regions of the gp120 molecule associated with and including the V2 and V3 loops, the C4 domain and supporting structures, induce the dissociation of gp120 from gp41 on cells infected with the T cell line-adapted HIV-1 molecular clone Hx10. Similar to soluble receptor-induced dissociation of gp120 from gp41, the antibody-induced dissociation is dose- and time-dependent. By contrast, mAbs binding to discontinuous epitopes overlapping the CD4 binding site do not induce gp120 dissociation, implying that mAb induced conformational changes in gp120 are epitope specific, and that HIV neutralization probably involves several mechanisms.
Related Links	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2192467/pdf http://jem.rupress.org/content/183/2/473.full.pdf
Ending Page	484
Page Count	12
Starting Page	473
DOI	10.1084/jem.183.2.473
Journal	The Journal of experimental medicine
Issue Number	2
Volume Number	183
Language	English
Publisher	Rockefeller University Press
Publisher Date	1996-02-01
Access Restriction	Open
Subject Keyword	Virology Antibodies Hiv Glycoprotein Conformational Changes Virus Gp120 Mabs Induced Dissociation Neutralization Journal: The Journal of experimental medicine (Vol- 183, Issue- 2)
Content Type	Text

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