ArticleProceedings of the National Academy of Sciences of the United States of America2000
The long cytoplasmic tail of gp41 is required in a cell type-dependent manner for HIV-1 envelope glycoprotein incorporation into virions.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 177 papers, 1 of them a synthesis that pooled it.
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Who cites it
177 citing papers in PubMed, 1 synthesis or guideline pooled it, 249 citations in OpenAlex.
- HIV Genome-Wide Protein Associations: a Review of 30 Years of Research.Microbiology and molecular biology reviews : MMBR · 2016Pooled it
- Mechanisms of HIV-1 assembly, release and maturation.Nature reviews. Microbiology · 2026Review
- Engineering Viral Surface Antigens to Improve Display on Virus-like Particle (VLP) Vaccine Prototypes.Biotech (Basel (Switzerland)) · 2026Article
- Reconstructing a Missing Link of HIV-1 Assembly: HIV-1 Envelope-Matrix Interactions in a Native Viral Context.bioRxiv : the preprint server for biology · 2026Article
- Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication.FEMS microbiology reviews · 2026Review
- Natural variations at the E433 site in Env-gp120 β20-β21 cooperate with V2 and gp41 mutations to modulate HIV-1 infectivity.Frontiers in microbiology · 2026Article
- Characterization of full-length and cytoplasmic tail-truncated envelope glycoproteins incorporated into human immunodeficiency virus (HIV-1) virions and virus-like particles.Journal of virology · 2025Article
- Direct visualization of HIV-1 core nuclear import and its interplay with the nuclear pore.EMBO reports · 2025Article
- Structural maturation of the matrix lattice is not required for HIV-1 particle infectivity.Science advances · 2025Article
- Guanylate-binding protein 5 antagonizes viral glycoproteins independently of furin processing.mBio · 2024Article
- The Assembly of HTLV-1-How Does It Differ from HIV-1?Viruses · 2024Review
- Probing Gag-Env dynamics at HIV-1 assembly sites using live-cell microscopy.Journal of virology · 2024Article
- The evolution of envelope function during coinfection with phylogenetically distinct human immunodeficiency virus.BMC infectious diseases · 2024Article
- Second site reversion of HIV-1 envelope protein baseplate mutations maps to the matrix protein.Journal of virology · 2024Article
- KIF16B Mediates Anterograde Transport and Modulates Lysosomal Degradation of the HIV-1 Envelope Glycoprotein.Journal of virology · 2023Article
- Tryptophan-based motifs in the LLP3 Region of the HIV-1 envelope glycoprotein cytoplasmic tail direct trafficking to the endosomal recycling compartment and mediate particle incorporation.bioRxiv : the preprint server for biology · 2023Article
- Article
- Rab11-FIP1C Is Dispensable for HIV-1 Replication in Primary CD4Journal of virology · 2022Article
- Viral and Host Factors Regulating HIV-1 Envelope Protein Trafficking and Particle Incorporation.Viruses · 2022Review
- Endocytosed HIV-1 Envelope Glycoprotein Traffics to Rab14Journal of virology · 2022Article
117 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Lentiviruses, including HIV-1, have transmembrane envelope (Env) glycoproteins with cytoplasmic tails that are quite long compared with those of other retroviruses. However, mainly because of the lack of biochemical studies performed in cell types that are targets for HIV-1 infection, no clear consensus exists regarding the function of the long lentiviral Env cytoplasmic tail in virus replication. In this report, we characterize the biological and biochemical properties of an HIV-1 mutant lacking the gp41 cytoplasmic tail. We find that the gp41 cytoplasmic tail is necessary for the efficient establishment of a productive, spreading infection in the majority of T cell lines tested, peripheral blood mononuclear cells, and monocyte-derived macrophages. Biochemical studies using a high-level, transient HIV-1 expression system based on pseudotyping with the vesicular stomatitis virus glycoprotein demonstrate that in HeLa and MT-4 cells, mutant Env incorporation into virions is reduced only 3-fold relative to wild type. In contrast, gp120 levels in virions produced from a number of other T cell lines and primary macrophages are reduced more than 10-fold by the gp41 truncation. The Env incorporation defect imposed by the cytoplasmic tail truncation is not the result of increased shedding of gp120 from virions or reduced cell-surface Env expression. These results demonstrate that in the majority of T cell lines, and in primary cell types that serve as natural targets for HIV-1 infection in vivo, the gp41 cytoplasmic tail is essential for efficient Env incorporation into virions.
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