▪ Abstract Viral envelope glycoproteins promote viral infection by mediating the fusion of the
viral membrane with the host-cell membrane. Structural and biochemical studies of two viral …

The current general model of HIV viral entry involves the binding of the trimeric viral
envelope glycoprotein gp120/gp41 to cell surface receptor CD4 and chemokine co-receptor …

The envelope glycoprotein of human immunodeficiency virus type 1 (HIV-1) consists of a
complex of gp120 and gp41. gp120 determines viral tropism by binding to target-cell …

Fusion of viral and cellular membranes by the envelope glyco-protein gp120/gp41 effects
entry of HIV-1 into the cell. The precursor, gp160, is cleaved post-translationally into gp120 …

Background Studies on the fusion-inhibitory peptides derived from the heptad repeat 1 and
2 (HR1 and HR2) regions of the HIV-1 envelope glycoprotein gp41 provided crucial …

T-20, a synthetic peptide corresponding to a region of the transmembrane subunit of the HIV-
1 envelope protein, blocks cell fusion and viral entry at concentrations of less than 2 ng/ml in …

To define the role of the human immunodeficiency virus type 1 (HIV-1) envelope proteins in
virus infection, a series of peptides were synthesized based on various regions of the HIV-1 …

This book grew out of a scientific review, originally published in Microbiological Reviews. It
has been updated and expanded-now citing more than 2100 references (100 pages of the …

Infection with HIV-1 is initiated by fusion of cellular and viral membranes. The gp41 subunit
of the HIV-1 envelope plays a major role in this process, but the structure of gp41 is …

Editor: A number of reports have appeared in the literature attributing biological activity to
synthetic peptides sharing pri-mary sequence homology with the envelope glycoproteins of …