Cited by 428HIV Research and TreatmentCellular transport and secretionT-cell and Retrovirus Studies

Biosynthesis, cleavage, and degradation of the human immunodeficiency virus 1 envelope glycoprotein gp160

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Willey, R L, Bonifacino, J S, Potts, B J, Martin, M A, Klausner, R D·1988·Proceedings of the National Academy of Sciences

Abstract

The synthesis and processing of the human immunodeficiency virus 1 (HIV-1) envelope precursor glycoprotein gp 160 was studied in an infected CD4+ lymphocytic cell line. Surprisingly, only a small percentage (5-15%) of gp160 is cleaved to produce the mature gp120 component. Intracellular sorting results in the transfer of most uncleaved gp160 to lysosomes, where it is degraded, while gp120 is transported to the cell surface and subsequently secreted. Cleavage of gp160 to generate gp120 occurs intracellularly and can be inhibited by NH4Cl. Taken together, these results indicate that intracellular cleavage of gp160 determines the intracellular transport and survival of the envelope glycoproteins necessary to produce infectious virus.

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Crossref · 10.1073/pnas.85.24.9580

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1 of 1 references verified0 citation errors · 0 not checkable

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  • The Env protein of retroviruses is synthesized from a singly spliced mRNA as a precursor protein, which is cleaved by cellular proteases into gp120 (SU) and gp41 (TM), forming the gp120-gp41 heterotrimer.

    “Without exception, the Env protein of retroviruses is synthesized from a singly spliced mRNA as a precursor protein, which is then cleaved by cellular proteases into the external glycoprotein gp120 (SU), which noncovalently associates with the gp41 (TM) domain to form the gp120–gp41 heterotrimer (McCune et al. 1988, Willey et al. 1988, Freed and Martin 1995).”
  • 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
Willey, R. L., Bonifacino, J. S., Potts, B. J., Martin, M. A., & Klausner, R. D.
Affiliations
National Institute of Allergy and Infectious Diseases (US)
Venue
Proceedings of the National Academy of Sciences
Published
1988-12
Volume
85
Issue
24
Pages
9580-9584
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2026318059
Cited by
428
References
1
Citations by year
2026: 1 · 2025: 8 · 2024: 9 · 2023: 11 · 2022: 9 · 2021: 3 · 2020: 3 · 2019: 5 · 2018: 3 · 2017: 2 · 2016: 5 · 2015: 3 · 2014: 11 · 2013: 9 · 2012: 10
FWCI
4.46
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
Keywords
HIV-1, gp160, gp120, envelope glycoprotein, proteolytic cleavage, intracellular sorting, lysosomal degradation, cell surface transport, protein secretion, CD4+ T cells
MeSH terms
Ammonium Chloride, Antigens, Differentiation, T-Lymphocyte, Cell Line, Humans, Kinetics, Models, Biological, Retroviridae Proteins, Viral Envelope Proteins, Leukemia, Lymphocytic, Chronic, B-Cell, HIV Envelope Protein gp120, HIV Envelope Protein gp160

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