Cited by 163HIV Research and TreatmentT-cell and Retrovirus StudiesHIV/AIDS drug development and treatment

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Overexpression of the gag-pol precursor from human immunodeficiency virus type 1 proviral genomes results in efficient proteolytic processing in the absence of virion production

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Park, J, Morrow, C D·1991·Journal of Virology

DOI 10.1128/jvi.65.9.5111-5117.1991PMC PMC248980

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Abstract

The expression of the gag-pol polyprotein of human immunodeficiency virus type 1 (HIV-1) occurs via ribosomal frameshifting between the gag and pol genes. Because low levels of the gag-pol precursor are naturally produced in HIV-1-infected cells, a limited amount of information is available on the biology of this molecule. To further study this polyprotein, two mutant HIV-1 proviral genomes were created to position the gag and pol genes in the same translational reading frame. The mutations inserted a single thymidine nucleotide at the site of ribosomal frameshifting (nucleotide 1635), which results in the addition of a phenylalanine residue (frameshift 1 [FS1]), or a single adenine nucleotide, which results in the addition of a leucine residue (frameshift 2 [FS2]). Transfection of the mutant proviral genomes into COS-1 cells resulted in the expression of the p160gag-pol polyprotein precursor as well as the proteolytically processed gag and pol gene products. Metabolic labeling of the transfected cells with [3H]myristic acid revealed that the p160gag-pol and p17gag proteins expressed from the mutant genomes were myristylated. While the supernatants from COS-1 cells transfected with wild-type or mutant proviral genomes contained similar amounts of p24 antigen, the levels of reverse transcriptase were, on the average, 10 times greater in the supernatants from cells transfected with the FS1 and FS2 proviral genomes. The cells transfected with the wild-type proviral genome released infectious viral particles, while the mutant proviral genomes released p24 and reverse transcriptase in the absence of detectable particle formation. The mutant proviral genomes were completely noninfectious as determined by coculture of the transfected COS-1 cells with SupT1 cells. These results demonstrate that the gag-pol polyprotein of HIV-1 contains the appropriate signals for proteolytic processing and association with intracytoplasmic membranes in the absence of virion formation.

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Authors: Park, J., & Morrow, C. D.
Affiliations: University of Alabama at Birmingham (US)
ORCID: Morrow, C D
Venue: Journal of Virology
Publisher: American Society for Microbiology
Published: 1991-09
Volume: 65
Issue: 9
Pages: 5111-5117
ISSN: 0022-538X (ISSN-L)
1098-5514
DOI: 10.1128/jvi.65.9.5111-5117.1991
PMC: PMC248980
OpenAlex: W2099481042
Cited by: 163
References: 35
Citations by year: 2026: 3 · 2025: 2 · 2024: 6 · 2023: 3 · 2022: 1 · 2021: 1 · 2020: 4 · 2019: 3 · 2017: 3 · 2016: 3 · 2015: 10 · 2014: 2 · 2013: 2 · 2012: 11
FWCI: 1.48
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Journal of Virology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5p01ai027290-05)
National Cancer Institute (CA-13 148, P30CA013148)
National Institute of Allergy and Infectious Diseases (AI 27290, AI-27767, P30AI027767)
Topics: Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
Keywords: ribosomal frameshifting, proteolytic processing, myristoylation, reverse transcriptase, p24 antigen, viral assembly
MeSH terms: Amino Acid Sequence, Base Sequence, DNA Mutational Analysis, Molecular Sequence Data, Morphogenesis, Oligonucleotides, Protein Processing, Post-Translational, Proteins, Recombinant Proteins, Structure-Activity Relationship, HIV-1, Gene Products, gag, Gene Products, pol, Polymerase Chain Reaction

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Overexpression of the gag-pol precursor from human immunodeficiency virus type 1 proviral genomes results in efficient proteolytic processing in the absence of virion production

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