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NLM AIDSLINE
Apolipoprotein A-I and its amphipathic helix peptide analogues inhibit human immunodeficiency virus-induced syncytium formation.
Owens BJ; Anantharamaiah GM; Kahlon JB; Srinivas RV; Compans RW; Segrest
January 30, 1991
J Clin Invest. 1990 Oct;86(4):1142-50. Unique Identifier : AIDSLINE

The envelope (membrane) glycoprotein of HIV is essential for virus attachment and entry into host cells. Additionally, when expressed on the plasma membrane of infected cells, the envelope protein is responsible for mediating cell-cell fusion which leads to the formation of multinucleated giant cells, one of the major cytopathic effects of HIV infections. The envelope glycoproteins of HIV contain regions that can fold into amphipathic alpha-helixes, and these regions have been suggested to play a role in subunit associations and in virus-induced cell fusion and cytopathic effects of HIV. We therefore tested the possibility that amphipathic helix-containing peptides and proteins may interfere with the HIV amphipathic peptides and inhibit those steps of HIV infection involving membrane fusion. Apolipoprotein A-I, the major protein component of high density lipoprotein, and its amphipathic peptide analogue were found to inhibit cell fusion, both in HIV-1-infected T cells and in recombinant vaccinia-virus-infected CD4+ HeLa cells expressing HIV envelope protein on their surfaces. The amphipathic peptides inhibited the infectivity of HIV-1. The inhibitory effects were manifest when the virus, but not cells, was pretreated with the peptides. Also, a reduction in HIV-induced cell killing was observed when virus-infected cell cultures were maintained in presence of amphipathic peptides. These results have potential implications for HIV biology and therapy.

Amino Acid Sequence Apolipoproteins A/*PHARMACOLOGY Cell Survival/DRUG EFFECTS Cells, Cultured Giant Cells/*DRUG EFFECTS Human HIV/*DRUG EFFECTS/PATHOGENICITY HIV Seropositivity/BLOOD Lipoproteins, HDL/BLOOD Molecular Sequence Data Peptides/PHARMACOLOGY Polioviruses/DRUG EFFECTS Protein Conformation Support, Non-U.S. Gov't Support, U.S. Gov't, P.H.S. JOURNAL ARTICLE

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