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.
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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)