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Positionally independent and exchangeable late budding functions of the Rous sarcoma virus and human immunodeficiency virus Gag proteins
Open accessAbstract
The Gag proteins of Rous sarcoma virus and human immunodeficiency virus (HIV) each contain a function involved in a late step in budding, defects in which result in the accumulation of these molecules at the plasma membrane. In the Rous sarcoma virus Gag protein (Pr76gag), this assembly domain is associated with a PPPY motif, which is located at an internal position between the MA and CA sequences. This motif is not contained anywhere within the HIV Gag protein (Pr55gag), and the MA sequence is linked directly to CA. Instead, a late assembly function of HIV has been associated with the p6 sequence situated at the C terminus of Gag. Here we demonstrate the remarkable finding that the late assembly domains from these two unrelated Gag proteins are exchangeable between retroviruses and can function in a positionally independent manner.
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“RSV Gag chimeras demonstrated that the L domain function of p2b could be substituted by the C-terminal sequence of HIV-1 p6, regardless of its position in the precursor”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Parent et al. 1995
In the citing paper
“The “L” domains have been reported in many retroviruses, such as HIV, MLV, RSV, EIAV, HIV-2, FIV, HTLV-1, MPMV, and FV”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Parent et al. 1995
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Items 201–239 of 239
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“The PPXY L-domain can bind to the Nedd4 family ubiquitin ligases, a subgroup of HETC-E3 ligases, which can target and initiate ESCRT machinery via their enzymatic activity (28).”
BackgroundThe Road Less Traveled: HIV's Use of Alternative Routes through Cellular Pathways
Marx, A., & Alian, A. (2015) · Journal of Virology · doi:10.1128/jvi.03684-14 · Cited by 11
“Given their functional essentiality, these short motifs are highly conserved (11, 52, 53), function independently of their location within the targeting protein, and can be functionally exchanged with comparable motifs from other proteins (39, 55).”
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“Although p6gag has been well characterized with regard to its late domain function, less is known about individual residues downstream of the late domain sequence: PTAP (Demirov et al., 2002; Freed, 2002; Huang et al., 1995; Parent et al., 1995).”
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A PLPPV sequence in the p8 region of Gag provides late domain function for mouse mammary tumor virus
Coren, L. V., Nagashima, K., & Ott, D. E. (2019) · Virology · doi:10.1016/j.virol.2019.07.015 · Cited by 6
“, 1996) and can also be exchanged between viruses (Li et al., 2002; Medina et al., 2005; Parent et al., 1995; Shehu-Xhilaga et al., 2004).”
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Jehad, M. A., Ali, L. M., Pillai, V. N., Prabhu, S. G., Mustafa, F., & Rizvi, T. A. (2026) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuaf066 · Cited by 5
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An Inducible ESCRT-III Inhibition Tool to Control HIV-1 Budding
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Self-citationInsertion of Capsid Proteins from Nonenveloped Viruses into the Retroviral Budding Pathway
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“Although the p6 peptide is naturally located at the C terminus of the HIV Gag protein, it remains functional when positioned internally (22).”
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Self-citationConserved serines in simian immunodeficiency virus capsid are required for virus budding
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Carter, C. A. (2026) · Annual Review of Virology · doi:10.1146/annurev-virology-100424-011327
Kaur, H., Guevara, R. B., Rivera-Cuevas, Y., Olafsson, E. B., Mayoral, J., Augusto, L. D. S., Guerra, A. J., Patel, R. K., Bohannon, K. P., Sexton, J. Z., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.07.20.739547
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“En effet, il a été démontré que la mutation de l’un de ces L-domaines, inhibe le bourgeonnement viral (Carlton, 2010; Parent et al., 1995; Puffer et al., 1997; von Schwedler et al., 2003; Usami et al., 2012).”
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Studies on Cellular Host Factors Involved in the HIV-1 Life Cycle: A Dissertation
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“Other retroviruses have equivalent motifs that are required for virus release, and these different motifs are functionally interchangeable (Parent et al. 1995).”
Background
Metadata
- Authors
- Parent, L. J., Bennett, R. P., Craven, R. C., Nelle, T. D., Krishna, N. K., Bowzard, J. B., Wilson, C. B., Puffer, B. A., Montelaro, R. C., & Wills, J. W.
- Affiliations
- Pennsylvania State University (US)
- Venue
- Journal of Virology
- Publisher
- American Society for Microbiology
- Published
- 1995-09
- Volume
- 69
- Issue
- 9
- Pages
- 5455-5460
- ISSN
- 0022-538X (ISSN-L)
- 1098-5514
- PMC
- PMC189393
- OpenAlex
- W2157103983
- Cited by
- 258
- References
- 27
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 1 · 2023: 4 · 2022: 5 · 2021: 4 · 2020: 6 · 2019: 4 · 2018: 4 · 2017: 2 · 2016: 2 · 2015: 6 · 2014: 2 · 2013: 11 · 2012: 8
- FWCI
- 3.85
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Virology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5k11ai001148-05)
- National Cancer Institute (CA60395, T32CA060395)
- National Institute of Allergy and Infectious Diseases (R01AI025850, AI 25850, K11 AI01148)
- 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
- Rous sarcoma virus, HIV-1, Gag protein, viral assembly, matrix protein, capsid protein
- MeSH terms
- Alleles, Amino Acid Sequence, Animals, Avian Sarcoma Viruses, Base Sequence, Cell Line, Chlorocebus aethiops, Cloning, Molecular, HIV, Kidney, Molecular Sequence Data, Recombinant Proteins, Species Specificity, Transfection, Gene Products, gag, Genes, gag, Polymerase Chain Reaction, Sequence Deletion, Sequence Homology, Amino Acid, DNA Primers
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