Properties of Hiv Membrane Reconstituted From its Recombinant Gp160 Envelope Glycoprotein
Cornet, B.;Decroly, E.;Thinessempoux, D.;Ruysschaert, JM.;Vandenbranden, M.
(1992) AIDS Research and Human Retroviruses — Vol. 8, n° 10, p. 1823-1831 (1992)
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Authors
Cornet, B.
Author
Decroly, E.
Author
Thinessempoux, D.
Author
Ruysschaert, JM.
Author
Vandenbranden, M.
Author
Abstract
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., Decroly, E., Thinessempoux, D., Ruysschaert, JM., & Vandenbranden, M. (1992). Properties of Hiv Membrane Reconstituted From its Recombinant Gp160 Envelope Glycoprotein. AIDS Research and Human Retroviruses, 8(10), 1823-1831. https://doi.org/10.1089/aid.1992.8.1823 (Original work published 1992)