Cited by 44HIV Research and TreatmentT-cell and Retrovirus StudiesHIV/AIDS drug development and treatment

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Proline Residues in Human Immunodeficiency Virus Type 1 p6 Gag Exert a Cell Type-Dependent Effect on Viral Replication and Virion Incorporation of Pol Proteins

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Dettenhofer, Markus, Yu, Xiao-Fang·1999·Journal of Virology

DOI 10.1128/jvi.73.6.4696-4704.1999PMC PMC112511

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Abstract

The C terminus of the HIV-1 Gag protein contains a proline-rich domain termed p6(Gag). This domain has been shown to play a role in efficient virus release and incorporation of Vpr into virions. In a previous study (X. F. Yu, L. Dawson, C. J. Tian, C. Flexner, and M. Dettenhofer, J. Virol. 72:3412-3417, 1998), we observed that the removal of the p6 domain of Gag as well as drastic mutations in the PTAP motif resulted in reduced virion-associated Pol proteins from transfected COS cells. In the present study, amino acid substitutions at residues 5 and 7 of p6(Gag) resulted in a cell type-dependent replication of the mutant virus in CD4(+) T cells; the virus was replication competent in Jurkat cells but restricted in H9 cells and primary blood-derived monocytes. Established Jurkat and H9 cell lines expressing p6(Gag) mutant and parental virus were used to further understand this defect. Mutant virions produced from H9 cells, which displayed no defect in extracellular virion production, showed an approximately 16-fold reduction in Pol protein levels, whereas the levels of Pol proteins were only marginally reduced in mutant virions produced from Jurkat cells. The reduction in the virion-associated Pol proteins could not be accounted for by differences in the levels of intracellular p160(Gag-Pol) or in the interaction between p55(Gag) and p160(Gag-Pol) precursors. Electron microscopic analysis of the p6(Gag) mutant virions showed a predominately immature morphology in the absence of significant defects in Gag proteolytic cleavage. Taken together, these data suggest that the proline-rich motif of p6(Gag) is involved in the late stages of virus maturation, which include the packaging of cleaved Pol proteins in viral particles, a process which may involve cell-type-specific factors.

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Authors: Dettenhofer, M., & Yu, X.-F.
Affiliations: Johns Hopkins University (US)
ORCID: Dettenhofer, Markus
Yu, Xiao-Fang
Venue: Journal of Virology
Publisher: American Society for Microbiology
Published: 1999-06
Volume: 73
Issue: 6
Pages: 4696-4704
ISSN: 0022-538X (ISSN-L)
1098-5514
DOI: 10.1128/jvi.73.6.4696-4704.1999
PMC: PMC112511
OpenAlex: W2147833851
Cited by: 44
References: 0
Citations by year: 2026: 1 · 2022: 1 · 2021: 1 · 2020: 2 · 2018: 1 · 2014: 3 · 2013: 1 · 2012: 1
FWCI: 1.56
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 (5r29ai035525-04)
National Institute of Allergy and Infectious Diseases (AI-35525)
National Institute of Environmental Health Sciences (ES 07141, T32ES007141)
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: proline-rich region, PTAP motif, viral replication, cell type dependence, viral assembly, virus maturation, CD4+ T cells, Jurkat cells, H9 cells, monocytes, virion morphology
MeSH terms: Amino Acid Sequence, Animals, Base Sequence, Microscopy, Electron, Molecular Sequence Data, Proline, Protein Precursors, Structure-Activity Relationship, Virion, Virus Replication, HIV-1, Gene Products, gag, Gene Products, pol, Fusion Proteins, gag-pol, Virus Assembly, COS Cells

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Proline Residues in Human Immunodeficiency Virus Type 1 p6 Gag Exert a Cell Type-Dependent Effect on Viral Replication and Virion Incorporation of Pol Proteins

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