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Envelope glycoprotein incorporation, not shedding of surface envelope glycoprotein (gp120/SU), Is the primary determinant of SU content of purified human immunodeficiency virus type 1 and simian immunodeficiency virus.
- Source :
-
Journal of virology [J Virol] 2002 Jun; Vol. 76 (11), pp. 5315-25. - Publication Year :
- 2002
-
Abstract
- Human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus (SIV) particles typically contain small amounts of the surface envelope protein (SU), and this is widely believed to be due to shedding of SU from mature virions. We purified proteins from HIV-1 and SIV isolates using procedures which allow quantitative measurements of viral protein content and determination of the ratios of gag- and env-encoded proteins in virions. All of the HIV-1 and most of the SIV isolates examined contained low levels of envelope proteins, with Gag:Env ratios of approximately 60:1. Based on an estimate of 1,200 to 2,500 Gag molecules per virion, this corresponds to an average of between 21 and 42 SU molecules, or between 7 and 14 trimers, per particle. In contrast, some SIV isolates contained levels of SU at least 10-fold greater than SU from HIV-1 isolates. Quantification of relative amounts of SU and transmembrane envelope protein (TM) provides a means to assess the impact of SU shedding on virion SU content, since such shedding would be expected to result in a molar excess of TM over SU on virions that had shed SU. With one exception, viruses with sufficient SU and TM to allow quantification were found to have approximately equivalent molar amounts of SU and TM. The quantity of SU associated with virions and the SU:TM ratios were not significantly changed during multiple freeze-thaw cycles or purification through sucrose gradients. Exposure of purified HIV-1 and SIV to temperatures of 55 degrees C or greater for 1 h resulted in loss of most of the SU from the virus but retention of TM. Incubation of purified virus with soluble CD4 at 37 degrees C resulted in no appreciable loss of SU from either SIV or HIV-1. These results indicate that the association of SU and TM on the purified virions studied is quite stable. These findings suggest that incorporation of SU-TM complexes into the viral membrane may be the primary factor determining the quantity of SU associated with SIV and HIV-1 virions, rather than shedding of SU from mature virions.
- Subjects :
- Animals
CD4 Antigens metabolism
CHO Cells
Cricetinae
Freezing
Gene Products, env isolation & purification
Gene Products, env metabolism
Gene Products, gag isolation & purification
Gene Products, gag metabolism
HIV Envelope Protein gp120 isolation & purification
HIV-1 isolation & purification
Heating
Humans
Simian Immunodeficiency Virus isolation & purification
HIV Envelope Protein gp120 metabolism
HIV Envelope Protein gp41 metabolism
HIV-1 metabolism
Membrane Glycoproteins metabolism
Retroviridae Proteins metabolism
Simian Immunodeficiency Virus metabolism
Viral Envelope Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0022-538X
- Volume :
- 76
- Issue :
- 11
- Database :
- MEDLINE
- Journal :
- Journal of virology
- Publication Type :
- Academic Journal
- Accession number :
- 11991960
- Full Text :
- https://doi.org/10.1128/jvi.76.11.5315-5325.2002