title: Antibody to native human immunodeficiency virus type 1 envelope glycoproteins induced by IIIB and MN recombinant gp120 vaccines. The NIAID AIDS Vaccine Evaluation Group.
abstract: The ability of antibody induced by MN and IIIB recombinant gp120 (rgp120) human immunodeficiency virus type 1 (HIV-1) vaccines the bind to oligomeric native and monomeric recombinant HIV-1 envelope glycoproteins (rgp 120) was measured in 25 uninfected, healthy adult volunteers. A major focus was to evaluate the effect of simultaneous and sequential immunization with vaccines representing different strains of HIV-1 on the ability to broaden cross-reactivity of antibodies against these and other HIV-1 strains. A flow cytometric indirect immunofluorescence assay (FIFA) to detect vaccine-induced antibody to envelope glycoprotein expressed by infected and rgp120-coated target cells was used, MN rgp120 HIV-1 vaccine given alone and coadministered with IIIB rgp120 HIV-1 vaccine elicited antibody which bound to cells infected with HIV-1MN, HIV-IIIB, HIV-1RF, and HIV-1-SF2. The presence of envelope glycoprotein-binding antibody detected by FIFA correlated to a moderate degree with functional antibody against HIV-1MN and HIV-IIIB. Priming immunization with IIIB rgp120 HIV-1 vaccine followed by booster injections of MN rgp120 HIV-1 vaccine resulted in increased cross-reactive antibody binding to these and heterologous clade B HIV-1 strains infecting cells. MN rgp120 HIV-1 vaccine given alone was better able to induce cross-reactive antibody to cells infected with heterologous HIV-1 laboratory strains than was IIIB rgp120 HIV-1 vaccine given alone. The vaccines induced binding antibody to rgp120 possessing the amino acid sequence of a clade E HIV-1 strain as measured by enzyme-linked immunosorbent assay. Levels of antibody binding to cells infected with clade B HIV-1 and cells coated with monomeric rgp120 were greater than that induced by HIV-1IIIB-based gp160 vaccines in previous studies.
authors.affiliation: Division of Infectious Diseases and Immunology, Saint Louis University, Missouri, USA.
authors.forename: G J
authors.initials: GJ
authors.lastname: Gorse
authors.forename: G B
authors.initials: GB
authors.lastname: Patel
authors.forename: F K
authors.initials: FK
authors.lastname: Newman
authors.forename: R B
authors.initials: RB
authors.lastname: Belshe
authors.forename: P W
authors.initials: PW
authors.lastname: Berman
authors.forename: T J
authors.initials: TJ
authors.lastname: Gregory
authors.forename: T J
authors.initials: TJ
authors.lastname: Matthews
mesh_terms: D016915:AIDS Vaccines / Q000276:immunology*; D000328:Adult; D002460:Cell Line; D003429:Cross Reactions; D004311:Double-Blind Method; D015483:HIV Antibodies / Q000096:biosynthesis* / Q000276:immunology*; D015699:HIV Envelope Protein gp120 / Q000276:immunology* / Q000494:pharmacology; D015497:HIV-1 / Q000276:immunology*; D006801:Humans; D007115:Immunization Schedule; D007117:Immunization, Secondary; D011485:Protein Binding / Q000276:immunology; D014614:Vaccines, Synthetic / Q000276:immunology* / Q000494:pharmacology
chemical_list: D016915:AIDS Vaccines; D015483:HIV Antibodies; D015699:HIV Envelope Protein gp120; D014614:Vaccines, Synthetic