ArticleJournal of virology2005
Heterologous late-domain sequences have various abilities to promote budding of human immunodeficiency virus type 1.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
18 citing papers in PubMed.
- Review
- Viruses go modular.The Journal of biological chemistry · 2020Review
- A PLPPV sequence in the p8 region of Gag provides late domain function for mouse mammary tumor virus.Virology · 2019Article
- Review
- Equine Infectious Anemia Virus Gag Assembly and Export Are Directed by Matrix Protein through trans-Golgi Networks and Cellular Vesicles.Journal of virology · 2016Article
- Selective acquisition of host-derived ICAM-1 by HIV-1 is a matrix-dependent process.Journal of virology · 2015Article
- HIV Assembly and Budding: Ca(2+) Signaling and Non-ESCRT Proteins Set the Stage.Molecular biology international · 2012Article
- Basic residues in the nucleocapsid domain of Gag are critical for late events of HIV-1 budding.Journal of virology · 2011Article
- Efficient production of HIV-1 virus-like particles from a mammalian expression vector requires the N-terminal capsid domain.PloS one · 2011Article
- An LYPSL late domain in the gag protein contributes to the efficient release and replication of Rous sarcoma virus.Journal of virology · 2010Article
- The nucleocapsid region of human immunodeficiency virus type 1 Gag assists in the coordination of assembly and Gag processing: role for RNA-Gag binding in the early stages of assembly.Journal of virology · 2009Article
- The nucleocapsid region of HIV-1 Gag cooperates with the PTAP and LYPXnL late domains to recruit the cellular machinery necessary for viral budding.PLoS pathogens · 2009Article
- The Mechanism of Budding of Retroviruses From Cell Membranes.Advances in virology · 2009Article
- Mutations in human immunodeficiency virus type 1 nucleocapsid protein zinc fingers cause premature reverse transcription.Journal of virology · 2008Article
- CD45 immunoaffinity depletion of vesicles from Jurkat T cells demonstrates that exosomes contain CD45: no evidence for a distinct exosome/HIV-1 budding pathway.Retrovirology · 2008Article
- Proteomic and biochemical analysis of purified human immunodeficiency virus type 1 produced from infected monocyte-derived macrophages.Journal of virology · 2006Article
- YRKL sequence of influenza virus M1 functions as the L domain motif and interacts with VPS28 and Cdc42.Journal of virology · 2006Article
- Redundant roles for nucleocapsid and matrix RNA-binding sequences in human immunodeficiency virus type 1 assembly.Journal of virology · 2005Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Retroviral late (L) domains present within Gag act in conjunction with cellular proteins to efficiently release virions from the surface of the cell. Three different critical core sequences have been identified as required elements for L-domain function: PPPY, PTAP (also PSAP), and YPDL, with different retroviruses utilizing one or two of these core sequences. The human immunodeficiency virus type 1 (HIV-1) L domain is centered around a PTAP sequence in the p6 region of Gag. To assess the ability of heterologous L-domain sequences to be functionally interchanged for those in full-length HIV-1, we produced a series of constructs that replaced PTAP-containing p6(Gag) sequences with those of PPPY- or YPDL-based L domains. While previous studies had found that L domains are interchangeable in other retroviruses, most of the sequences introduced into p6(Gag) failed to substitute for PTAP-mediated L-domain function. One exception was the 11-amino-acid p2b sequence of Rous sarcoma virus (RSV) Gag, which could fully restore HIV-1 budding, while a PPPPY sequence exchange alone did not. This suggests that the RSV L domain consists of more than simply its core L-domain sequence. The HIV-p2b chimera was as infectious as the wild type, produced normal virions, and was sensitive to proteasome inhibitors. These results show that L-domain sequences are not necessarily interchangeable. Thus, HIV-1 Gag might have a more stringent requirement for L-domain function than the other retroviruses previously studied.
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