dc.contributor.author | Fenouillet, E. | fr_FR |
dc.date.accessioned | 2013-02-18T16:18:55Z | |
dc.date.available | 2013-02-18T16:18:55Z | |
dc.date.issued | 1993 | fr_FR |
dc.identifier.citation | Fenouillet, E., La N-glycosylation du VIH : du modèle expérimental à l'application thérapeutique., Med Sci (Paris), 1993, Vol. 9, N° 8-9; p.901-906 | fr_FR |
dc.identifier.issn | 1958-5381 | fr_FR |
dc.identifier.uri | http://hdl.handle.net/10608/3010 | |
dc.description.abstract | Human. immunodeficiency virus type-1 (HIV) envelope precursor glycoprotein (gp160) is cleaved into gp120 and gp41 ; gp120 and gp41 are responsible for HIV tropism for CD4+ cells and for viral and cell membrane fusion leading to virus entry into cells, respectively. The functional role of gp160 N-linked glycans (CHO), which represent 50 % of its MW, was studied. During the biosynthesis, it was shown that CHO clusters of gp160 induce the bioactive folding of both gp41 and gp120 : the interaction between abnormally glycosylated gp120 and its CD4 receptor was altered and the accessibility of the V3 loop, a region that plays a key role in membrane fusion was diminished. Such modified properties could account for the impairment of HIV-1 infectivity by glycosylation inhibitors, the prototypes of potential anti-HIV drugs. Similarly, mutation of the gp41 cluster of glycosylation sites inhibited gP160 cleavage and abolished gp41-mediated membrane fusion. In contrast, after biosynthesis, CHO present on mature viral gp120 and gp41 are involved neither in their bioactivity nor in their conformation : the ability of deglycosylated virus to bind and to infect CD4+ cells was reduced by only 10 fold. CHO are then necessary to create but not to maintain the functional conformation Of HIV env products. | fr |
dc.language.iso | fr | fr_FR |
dc.publisher | John Libbery Eurotext, Montrouge | fr_FR |
dc.rights | Article en libre accès | fr |
dc.rights | Médecine/Sciences - Inserm - SRMS | fr |
dc.source | M/S. Médecine sciences [revue papier, ISSN : 0767-0974], 1993, Vol. 9, N° 8-9; p.901-906 | fr_FR |
dc.title | La N-glycosylation du VIH : du modèle expérimental à l'application thérapeutique. | fr |
dc.type | Article | fr_FR |
dc.identifier.doi | 10.4267/10608/3010 | |