Cited by 189Cellular transport and secretionHIV Research and TreatmentGlycosylation and Glycoproteins Research

Intracellular processing of the gp160 HIV-1 envelope precursor. Endoproteolytic cleavage occurs in a cis or medial compartment of the Golgi complex

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Stein, B S, Engleman, E G·1990·Journal of Biological Chemistry

Abstract

The intracellular processing of the gp160 HIV-1 envelope precursor was characterized in acutely infected CD4+ T cells. Our data show that gp160 undergoes endoproteolytic cleavage by a nonacid dependent protease(s) in the rough endoplasmic reticulum-Golgi complex, within cis or medial cisternae, and is not transported to the cell surface. Two-dimensional electrophoretic pulse-chase analysis indicates that it takes greater than 2 h for gp160 to be transported from the rough endoplasmic reticulum to the site of action of sialyltransferases in the trans Golgi. Evidence is presented that gp160 is subject to mannose trimming in the Golgi complex, which is inhibited by 1-deoxymannojirimycin (a specific Golgi alpha-mannosidase I inhibitor). Preliminary data also suggest that gp120 is post-translationally modified by sialylated O-linked oligosaccharides.

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Crossref · 10.1016/s0021-9258(19)39849-7

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  • In HIV-1, the Env glycoproteins precursor, gp160, is cleaved in the Golgi by cellular furin or furin-like PRs into a mature surface glycoprotein gp120 and the transmembrane glycoprotein gp41.

    “In case of HIV-1, the Env glycoproteins precursor, gp160, is cleaved in the Golgi by cellular furin or furin-like PRs into: (i) a mature surface glycoprotein gp120 and (ii) the transmembrane glycoprotein gp41”

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Authors
Stein, B. S., & Engleman, E. G.
Affiliations
Stanford Blood Center (US)
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1990-02
Volume
265
Issue
5
Pages
2640-2649
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1529498974
Cited by
189
References
0
Citations by year
2025: 2 · 2024: 2 · 2023: 3 · 2022: 1 · 2021: 4 · 2020: 4 · 2019: 2 · 2018: 2 · 2017: 1 · 2016: 1 · 2015: 3 · 2014: 3 · 2013: 4 · 2012: 6
FWCI
7.90
Type
journal article
Language
en
Open access
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (5u01ai025922-05, 5p50hl033811-10)
  • National Heart, Lung, and Blood Institute (HL33811)
  • National Institute of Allergy and Infectious Diseases (AI25922)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
Keywords
HIV-1 envelope glycoprotein, gp160, endoproteolytic cleavage, Golgi apparatus, sialyltransferase, mannose trimming, 1-deoxymannojirimycin, gp120, CD4+ T cells, HIV-1 infection, glycosylation
MeSH terms
Cell Line, Glycoside Hydrolases, Golgi Apparatus, Humans, Kinetics, Molecular Weight, Neuraminidase, Protein Precursors, Protein Processing, Post-Translational, T-Lymphocytes, Electrophoresis, Gel, Two-Dimensional, HIV-1, Gene Products, env, HIV Envelope Protein gp160

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