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J. Virol., 06 1997, 4847-4851, Vol 71, No. 6
CD Rizzuto and JG Sodroski
Incorporation of the intercellular adhesion molecule ICAM-1 into human
immunodeficiency virus type 1 (HIV-1) particles increased virus infectivity
on peripheral blood mononuclear cells (PBMCs) by two- to sevenfold. The
degree of ICAM-1-mediated enhancement was greater for viruses bearing
envelope glycoproteins derived from primary HIV-1 isolates than for those
bearing envelope glycoproteins from laboratory- adapted strains. Treatment
of target PBMCs with an antibody against LFA- 1, a principal ICAM-1
receptor, was able to nullify the ICAM-1-mediated enhancement. The
incorporation of ICAM-1 rendered HIV-1 virions less susceptible to
neutralization by a monoclonal antibody directed against the viral envelope
glycoproteins. Surprisingly, an antibody against ICAM-1 completely
neutralized infection by ICAM-1-containing viruses, reducing the efficiency
of virus entry by almost 100-fold. Thus, HIV-1 neutralization by an
ICAM-1-directed antibody involves more than an inhibition of the
contribution of ICAM-1 to virus entry.
Copyright © 1997, American Society for Microbiology
Contribution of virion ICAM-1 to human immunodeficiency virus infectivity and sensitivity to neutralization
Division of Human Retrovirology, Dana-Farber Cancer Institute, Boston, Massachusetts 01225, USA.
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