Mutation of conserved N-glycosylation sites around the CD4-binding site of human immunodeficiency virus type 1 GP120 affects viral infectivity.
Virus Res
; 18(1): 9-20, 1990 Dec.
Article
em En
| MEDLINE
| ID: mdl-2082620
ABSTRACT
Infection by the human immunodeficiency virus type 1 (HIV-1) is initiated through interaction of its exterior envelope glycoprotein gp120 with the CD4 receptor on target cells. To address the possible role of N-glycosylation of HIV-1 gp120 in binding CD4, we mutated different conserved N-glycosylation site Asn-residues in the vicinity of the putative CD4 binding site, as single mutations or in combinations. Authentic and mutant gp120 proteins were produced using the baculovirus expression system. All mutant proteins were produced and secreted at similar levels and could be immunoprecipitated with an HIV(+)-serum. Furthermore, all glycosylation mutants retained the full capacity to bind CD4 except for a triple mutant which showed reduced binding. Different gp120 mutant genes were then introduced in an infectious proviral DNA clone. Upon transfection of MT-2 cells, the authentic HIV-1 clone induced maximal virus production after 6 days. In the case of the triple glycosylation mutant, comparable virus production was first reached after a delay of about 12 days. Moreover, in contrast to native HIV, the mutant virus induced no typical multinucleated giant cells. These results suggest that the attached carbohydrates around the CD4-binding site of gp120, may contribute to the generation of this protein domain required for high affinity receptor interaction.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Antígenos CD4
/
Proteína gp120 do Envelope de HIV
/
Síndrome da Imunodeficiência Adquirida
/
HIV-1
Idioma:
En
Revista:
Virus Res
Assunto da revista:
VIROLOGIA
Ano de publicação:
1990
Tipo de documento:
Article
País de afiliação:
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