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| Neutralization of the human immunodeficiency virus type 1 primary isolate JR-FL by human monoclonal antibodies correlates with antibody binding to the oligomeric form of the envelope glycoprotein complex |
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| Author(s): Fouts TR, Binley JM, Trkola A, Robinson JE, Moore JP |
| Source: JOURNAL OF VIROLOGY Volume: 71 Issue: 4 Pages: 2779-2785 Published: APR 1997 |
| Times Cited: 162 References: 77 |
| Abstract: To test whether antibodies that are neutralizing or nonneutralizing for human immunodeficiency virus type 1 (HIV-1) primary isolates can be distinguished by their affinities for the oligomeric envelope glycoproteins, we selected HIV-1(JR-FL) as a model primary virus and a panel of 13 human monoclonal antibodies (MAbs) and evaluated three parameters: (i) half-maximal binding to recombinant monomeric envelope, gp120(JR-FL); (ii) half-maximal binding to oligomeric envelope of HIV-1(JR-FL) expressed on the surface of transfected 293 cells; and (iii) neutralization of HIV-1(HR-FL) in a peripheral blood mononuclear cell-based neutralization assay. Two conclusions can be drawn from these experiments, First, we confirm that antibody interactions with monomeric gp120 do not predict primary virus neutralization. Second, we show that neutralization correlates qualitatively with the relative affinity of an antibody for the oligomeric envelope glycoproteins, at least for HIV-1(JR-FL). |
| Document Type: Article |
| Language: English |
Addresses:
1. ROCKEFELLER UNIV, AARON DIAMOND AIDS RES CTR, NEW YORK, NY 10016 USA
2. TULANE UNIV, MED CTR, DEPT PEDIAT, NEW ORLEANS, LA 70112 USA |
| Publisher: AMER SOC MICROBIOLOGY, 1325 MASSACHUSETTS AVENUE, NW, WASHINGTON, DC 20005-4171 |
| Subject Category: Virology |
| IDS Number: WM911 |
| ISSN: 0022-538X |
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