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Vaccine-induced antibodies to the native, oligomeric envelope glycoproteins of primary HIV-1 isolates.

Authors
  • Sa, Lee
  • R, Orque
  • Pa, Escarpe
  • Ml, Peterson
  • Jw, Good
  • Em, Zaharias
  • Phil Berman
  • Hw, Sheppard
  • R, Shibata
Type
Published Article
Journal
Vaccine
Publisher
Elsevier
Volume
20
Issue
3-4
Pages
563–576
Source
UCSC Bioinformatics biomedical-ucsc
License
Unknown

Abstract

A simple and sensitive method for measuring antibodies to primary human immunodeficiency virus type 1 (HIV-1) isolates has been developed. The flow cytometric immuno-fluorescence assay detects antibodies that bind to the native, oligomeric form of the envelope glycoprotein (gp120) expressed on the surface of PM-1 cells infected with primary isolates of HIV-1. Sera from people infected with HIV-1 or those immunized with recombinant gp120 vaccines were tested. Significant correlation was observed between neutralizing activity and oligomeric gp120 binding activity. Thirteen to 100% of individuals immunized with the subtype B bivalent vaccine AIDSVAX B/B developed oligomeric gp120 binding antibodies against a variety of subtype B primary isolates. For several isolates, AIDSVAX B/B sera reacted better than monovalent AIDSVAX B sera, suggesting that addition of the second immunogen improved the breadth of the antibody response. Cross-subtype binding activities, induced by AIDSVAX B/B, were lower than activities to subtype B isolates, suggesting that additional immunogen(s) may be desirable in vaccine(s) formulated for geographic regions where non-B subtypes are dominant.

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