Properties of HIV membrane reconstituted from its recombinant gp160 envelope glycoprotein.
Human immunodeficiency virus (HIV) membrane has been reconstituted from the recombinant envelope glycoprotein precursor (gp160) by a detergent dialysis technique. Electron microscopy shows that gp160-virosomes are spherical vesicles with a mean diameter identical to that of viral particles. Enzyme-linked immunosorbent assay and immunogold labeling demonstrate efficient association of gp160 with lipid vesicles and proteolysis treatment reveals an asymmetric insertion with about 90% of glycoproteins having their gp120-moiety pointing outside. Glycoproteins are organized as dimers and tetramers and gp160 retains its ability to specifically bind CD4 receptor after reconstitution into virosome.
Cornet
B
B
Laboratoire de Chimie-Physique des Macromolécules aux Interfaces, Université Libre de Bruxelles, Belgium.
Decroly
E
E
Thines-Sempoux
D
D
Ruysschaert
J M
JM
Vandenbranden
M
M
D015704:CD4 Antigens / Q000378:metabolism; D015686:Gene Products, env / Q000737:chemistry / Q000378:metabolism*; D019302:HIV Envelope Protein gp160; D015497:HIV-1 / Q000378:metabolism* / Q000648:ultrastructure*; D006801:Humans; D066298:In Vitro Techniques; D008081:Liposomes; D016253:Microscopy, Immunoelectron; D011487:Protein Conformation; D011498:Protein Precursors / Q000737:chemistry / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
D015704:CD4 Antigens; D015686:Gene Products, env; D019302:HIV Envelope Protein gp160; D008081:Liposomes; D011498:Protein Precursors; D011994:Recombinant Proteins