Yahi N, Fantini J, Chermann JC; International Conference on AIDS.
Int Conf AIDS. 1991 Jun 16-21; 7: 157 (abstract no. W.A.1261).
INSERM Unite 322, Marseille, France
OBJECTIVE: To study the structure of HIV1-NDK envelop glycoprotein and to compare them with the prototype ones. METHODS: Radio immunoprecipitation and enzymatic deglycosylation. RESULTS: The precursor of HIV1-NDK synthetized in CEM cells has a shorter size (gp140). This precursor is cleaved to produce a smaller extracellular envelop glycoprotein (gp100) and a transmembrane component with a usual size (gp41). Immuno-precipitates from tunicamycin-treated cells demonstrated the presence of a non-glycosylated precursor of 100 kDa for HIV1-BRU and 90 kDa for HIV1-NDK. Digestion of labeled precipitates with a mixture of endoglycosidase F and glycopeptidase F reduced the size of HIV1-BRU gp160 and gp120 to respectively 100 kDa and 60 kDa, while HIV1-NDK gp140 and gp100, after treatment with the same enzymes, displayed an apparent molecular mass of 90 kDa and 55 kDa respectively. DISCUSSION AND CONCLUSIONS: From these data we can conclude that HIV1-BRU gp120 and HIV1-NDK gp100 differ both in their proteic moiety (60 kDa and 45 kDa respectively) and in their carbohydrate moiety (60 kDa and 45 kDa respectively). These differences cannot be deduced from the nucleotide sequence of the env gene. They could constitute a structural basis, at the level of glycoprotein glycosylation and processing, accounting for the acute cytopathy of the HIV1-NDK strain.
Publication Types:
Keywords:
- GP 140
- Gene Products, env
- Genes, env
- Glycoproteins
- Glycosylation
- HIV Envelope Protein gp120
- HIV-1
- Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
- Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
- Protein Precursors
- genetics
- immunology
- reverse transcriptase, Human immunodeficiency virus 1
Other ID:
UI: 102192469
From Meeting Abstracts