Folding, interaction with GRP78-BiP, assembly, and transport of the human immunodeficiency virus type 1 envelope protein
- PMID: 1900540
- PMCID: PMC240054
- DOI: 10.1128/JVI.65.4.2047-2055.1991
Folding, interaction with GRP78-BiP, assembly, and transport of the human immunodeficiency virus type 1 envelope protein
Abstract
A detailed kinetic and quantitative analysis of the early and late biosynthetic events undergone by the human immunodeficiency virus type 1 envelope protein expressed by a recombinant vaccinia virus was performed. Early folding events that occurred in the endoplasmic reticulum included disulfide bond formation (t1/2 approximately 10 min), folding of envelope protein into a form competent to bind CD4 (t1/2 approximately 15 min), and specific and transient association and dissociation with GRP78-BiP (t1/2 approximately 25 min). After initial folding, envelope protein monomers formed noncovalently associated dimers with high efficiency (t1/2 approximately 30 min). Studies with brefeldin A, a compound that inhibits endoplasmic reticulum-to-Golgi transport, suggested that assembly occurred in the endoplasmic reticulum while cleavage of gp160 into gp120/gp41 subunits occurred in a post-endoplasmic reticulum compartment. Transport to the Golgi was monitored by modification of N-linked sugars to forms partially resistant to endoglycosidase H. The kinetics of endoglycosidase H resistance were nearly identical to the kinetics of gp160 cleavage (t1/2 approximately 80 min). Cleavage efficiency was strongly cell type dependent, ranging from 13 to 70%. By contrast, approximately 50% of the gp120 generated by the cleavage event was shed (t1/2 approximately 120 min) regardless of the cell type used. The results are discussed in terms of the overall biosynthetic pathway of the envelope protein and provide a framework with which to assess the effects of mutations on structure and function.
Similar articles
-
Folding, assembly, and intracellular trafficking of the human immunodeficiency virus type 1 envelope glycoprotein analyzed with monoclonal antibodies recognizing maturational intermediates.J Virol. 1996 Jun;70(6):3407-15. doi: 10.1128/JVI.70.6.3407-3415.1996. J Virol. 1996. PMID: 8648672 Free PMC article.
-
Functional role of the glycan cluster of the human immunodeficiency virus type 1 transmembrane glycoprotein (gp41) ectodomain.J Virol. 1993 Jan;67(1):150-60. doi: 10.1128/JVI.67.1.150-160.1993. J Virol. 1993. PMID: 8093218 Free PMC article.
-
Intracellular membrane traffic of human immunodeficiency virus type 1 envelope glycoproteins: vpu liberates Golgi-targeted gp160 from CD4-dependent retention in the endoplasmic reticulum.J Biochem. 1994 May;115(5):1010-20. doi: 10.1093/oxfordjournals.jbchem.a124414. J Biochem. 1994. PMID: 7961587
-
Human studies in the development of human immunodeficiency virus vaccines.J Infect Dis. 1995 Nov;172(5):1175-83. doi: 10.1093/infdis/172.5.1175. J Infect Dis. 1995. PMID: 7594651 Review.
-
AIDS pathogenesis: HIV envelope and its interaction with cell proteins.Immunol Today. 1990 Nov;11(11):418-25. doi: 10.1016/0167-5699(90)90162-3. Immunol Today. 1990. PMID: 2078296 Review.
Cited by
-
Inhibition of human immunodeficiency virus (HIV-1) infectivity by expression of poorly or broadly neutralizing antibodies against Env in virus-producing cells.J Virol. 2024 Feb 20;98(2):e0159423. doi: 10.1128/jvi.01594-23. Epub 2024 Jan 30. J Virol. 2024. PMID: 38289101
-
Direct interaction of the molecular chaperone GRP78/BiP with the Newcastle disease virus hemagglutinin-neuraminidase protein plays a vital role in viral attachment to and infection of culture cells.Front Immunol. 2023 Oct 16;14:1259237. doi: 10.3389/fimmu.2023.1259237. eCollection 2023. Front Immunol. 2023. PMID: 37920471 Free PMC article.
-
Alterations in gp120 glycans or the gp41 fusion peptide-proximal region modulate the stability of the human immunodeficiency virus (HIV-1) envelope glycoprotein pretriggered conformation.J Virol. 2023 Sep 28;97(9):e0059223. doi: 10.1128/jvi.00592-23. Epub 2023 Sep 11. J Virol. 2023. PMID: 37696048 Free PMC article.
-
Impact of stabilizing mutations on the antigenic profile and glycosylation of membrane-expressed HIV-1 envelope glycoprotein.PLoS Pathog. 2023 Aug 7;19(8):e1011452. doi: 10.1371/journal.ppat.1011452. eCollection 2023 Aug. PLoS Pathog. 2023. PMID: 37549185 Free PMC article.
-
Conformations of Human Immunodeficiency Virus Envelope Glycoproteins in Detergents and Styrene-Maleic Acid Lipid Particles.J Virol. 2023 Jun 29;97(6):e0032723. doi: 10.1128/jvi.00327-23. Epub 2023 May 31. J Virol. 2023. PMID: 37255444 Free PMC article.
References
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials
Miscellaneous