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The Journal of Immunology, Vol 155, Issue 8 4100-4110, Copyright © 1995 by American Association of Immunologists

ARTICLES

Lack of induction of antibodies specific for conserved, discontinuous epitopes of HIV-1 envelope glycoprotein by candidate AIDS vaccines

TC VanCott, FR Bethke, DS Burke, RR Redfield and DL Birx
Division of Retrovirology, Walter Reed Army Institute of Research, Rockville, MD, USA.

We examined the humoral immune response in both HIV-1 infected and uninfected volunteers immunized with candidate HIV-1 recombinant envelope subunit vaccines (Genentech gp120IIIB, MicroGeneSys gp160IIIB, or ImmunoAG gp160IIIB). Immunization of both HIV-1 infected and uninfected volunteers with these immunogens resulted in the induction of Abs preferentially reactive with epitopes accessible on a denatured form of gp120. While sera from HIV-1 uninfected gp120/gp160IIIB vaccinees bound gp120/gp41, which was expressed on the surface of H9 cells infected with HIV-1IIIB, minimal binding to HIV-1MN or HIV-1RF infected cells was obtained. Induction of qualitatively similar immune responses by these immunogens would not have been predicted based on their different tertiary structures. These data indicate a restriction of the immune response to linear, conserved epitopes poorly accessible on both monomeric gp120 and cell-surface expressed oligomeric gp120/gp41 and a lack of Abs specific for conformational epitopes conserved across divergent HIV-1 strains. Poor recognition of HIV-1 envelope tertiary and quaternary structure may explain the restricted neutralization profiles of vaccinee sera against laboratory-adapted strains of HIV-1 and their inability to neutralize primary HIV-1 isolates. Alternate immunogens or reformulations with the capacity to elicit Abs that preferentially bind to natively folded gp120 should be investigated and correlated with their ability to neutralize more diverse laboratory-adapted and primary HIV-1 isolates.


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