par Cornet, Bernard 
;Vandenbranden, Michel ;Cogniaux, Jacqueline;Giurgea, L;Dekegel, Daniel ;Ruysschaert, Jean Marie
Référence Biochemical and biophysical research communications, 167, 1, page (222-231)
Publication Publié, 1990-02
;Vandenbranden, Michel ;Cogniaux, Jacqueline;Giurgea, L;Dekegel, Daniel ;Ruysschaert, Jean Marie Référence Biochemical and biophysical research communications, 167, 1, page (222-231)
Publication Publié, 1990-02
Article révisé par les pairs
| Résumé : | Purified Human Immunodeficiency Virus (HIV) was solubilized in octylglucopyranoside. After centrifugation, the supernatant was added to lipid-detergent mixed micelles. Formation of virosomes occurred during overnight dialysis. Centrifugation on a continuous glycerol gradient showed that envelope glycoproteins (gp120 and gp41) and matrix protein p17 but not core protein p25 were associated to virosomes. Proteolytic treatment of virosomes indicates that gp120 is oriented toward the outside as in the virus particles, whereas p17 protein is anchored on both sides of the liposomal membrane. Virosomes are spherical vesicles with approximately the size of the virus as shown by electron microscopy. |
