Accessibility of the highly conserved amino- and carboxy-terminal regions from HIV-1 external envelope glycoproteins.
AIDS Res Hum Retroviruses
; 5(4): 451-63, 1989 Aug.
Article
em En
| MEDLINE
| ID: mdl-2548546
ABSTRACT
Amino- and carboxy-terminal extremities of the envelope external glycoproteins are regions that have remained highly conserved between human immunodeficiency viruses HIV-1 and HIV-2. The corresponding peptides have been synthesized and their structure and function analyzed. Circular dichroism spectra showed evidence of alpha helical conformation when the peptides were dissolved in the nonpolar solvent trifuoroethanol. These two regions are indeed exposed on the molecule because they were accessible to their respective specific antibodies on the native gp160 precursor or processed gp120 glycoproteins of HIV-1. Neither the peptides nor rabbit or human antibodies directed against the N- and C-terminal peptides interfered with the interaction between HIV-1 external glycoprotein gp120 and its CD4 cellular receptor. Taken together, these results indicate that N- and C-terminal regions of gp120 are accessible on the quaternary structure of the virion as well as on the soluble form of gp120 and that these regions are not directly or indirectly involved in the binding of gp120 to CD4.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fragmentos de Peptídeos
/
Proteínas dos Retroviridae
Limite:
Animals
Idioma:
En
Revista:
AIDS Res Hum Retroviruses
Assunto da revista:
SINDROME DA IMUNODEFICIENCIA ADQUIRIDA (AIDS)
Ano de publicação:
1989
Tipo de documento:
Article
País de afiliação:
França