Back to Search
Start Over
Transfer of endoplasmic reticulum and Golgi retention signals to human immunodeficiency virus type 1 gp160 inhibits intracellular transport and proteolytic processing of viral glycoprotein but does not influence the cellular site of virus particle budding.
- Source :
-
The Journal of general virology [J Gen Virol] 1997 Jul; Vol. 78 ( Pt 7), pp. 1745-53. - Publication Year :
- 1997
-
Abstract
- In this study, specific signals known to mediate endoplasmic reticulum or Golgi localization of transmembrane proteins have been transferred to the human immunodeficiency virus type 1 (HIV-1) env gene product. The intracellularly retained recombinant glycoproteins were not proteolytically processed to gp120 and gp41, which is further evidence that this process occurs at a later stage in the transport pathway, presumably within or near the trans-Golgi network. Since the subcellular localization of the viral glycoproteins of enveloped viruses can be one of the factors determining the cellular site of particle assembly and release, experiments were performed to determine if this property was altered by coexpression of the recombinant HIV-1 glycoproteins. When wild-type virus was compared to mutant virus encoding the intracellularly retained glycoproteins, the extent of HIV-1 particle release into the extracellular medium remained unaffected, and electron-microscopic analysis did not reveal any significant alteration in the cellular sites of particle assembly and budding. Thus, in COS-7 cells, altered subcellular localization of the viral glycoprotein does not exert a dominant influence on the assembly site of the HIV-1 particle.
- Subjects :
- Amino Acid Sequence
Animals
Biological Transport
COS Cells
Cell Line, Transformed
Endopeptidases
Endoplasmic Reticulum metabolism
Gene Expression
Golgi Apparatus metabolism
HIV Core Protein p24 biosynthesis
HIV Envelope Protein gp160 genetics
HIV-1 genetics
HIV-1 physiology
HIV-1 ultrastructure
Humans
Membrane Fusion
Molecular Sequence Data
Protein Sorting Signals genetics
Recombinant Fusion Proteins genetics
Recombinant Fusion Proteins metabolism
Virion
HIV Envelope Protein gp160 metabolism
HIV-1 metabolism
Protein Processing, Post-Translational
Protein Sorting Signals metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0022-1317
- Volume :
- 78 ( Pt 7)
- Database :
- MEDLINE
- Journal :
- The Journal of general virology
- Publication Type :
- Academic Journal
- Accession number :
- 9225051
- Full Text :
- https://doi.org/10.1099/0022-1317-78-7-1745