ArticleJournal of virology2010
Ancient adaptive evolution of tetherin shaped the functions of Vpu and Nef in human immunodeficiency virus and primate lentiviruses.
Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers, 1 of them a synthesis that pooled it.
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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
94 citing papers in PubMed, 1 synthesis or guideline pooled it, 136 citations in OpenAlex.
- HIV Genome-Wide Protein Associations: a Review of 30 Years of Research.Microbiology and molecular biology reviews : MMBR · 2016Pooled it
- Beyond Genetic Conservation: The Baton Pass Model of Essential Biological Functions.Biomolecules · 2026Review
- Viral interferon antagonism shapes host tropism.PLoS pathogens · 2025Review
- Indels allow antiviral proteins to evolve functional novelty inaccessible by missense mutations.Cell genomics · 2025Article
- Indels allow antiviral proteins to evolve functional novelty inaccessible by missense mutations.bioRxiv : the preprint server for biology · 2024Article
- Phylogenetic Reconstruction and Functional Characterization of the Ancestral Nef Protein of Primate Lentiviruses.Molecular biology and evolution · 2023Article
- Article
- The Feline Immunodeficiency Virus Envelope Signal Peptide Is a Tetherin Antagonizing Protein.mBio · 2023Article
- Unique Evolution of Antiviral Tetherin in Bats.Journal of virology · 2022Article
- Simplexviruses Successfully Adapt to Their Host by Fine-Tuning Immune Responses.Molecular biology and evolution · 2022Article
- Evolutionary Profile for (Host and Viral) MLKL Indicates Its Activities as a Battlefront for Extensive Counteradaptation.Molecular biology and evolution · 2021Article
- SERINC proteins potentiate antiviral type I IFN production and proinflammatory signaling pathways.Science signaling · 2021Article
- Positive natural selection in primate genes of the type I interferon response.BMC ecology and evolution · 2021Article
- Article
- Retroviral Restriction Factors and Their Viral Targets: Restriction Strategies and Evolutionary Adaptations.Microorganisms · 2020Review
- Signatures of host-pathogen evolutionary conflict reveal MISTR-A conserved MItochondrial STress Response network.PLoS biology · 2020Article
- Site-Specific Evolutionary Rate Shifts in HIV-1 and SIV.Viruses · 2020Article
- Antiviral Activity and Adaptive Evolution of Avian Tetherins.Journal of virology · 2020Article
- Multifaceted Roles of TIM-Family Proteins in Virus-Host Interactions.Trends in microbiology · 2020Review
- Vpu of a Simian Immunodeficiency Virus Isolated from Greater Spot-Nosed Monkey Antagonizes Human BST-2 via Two AxxxxxxxW Motifs.Journal of virology · 2020Article
34 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
3 authors at 2 institutions in 1 country.
Funding
Abstract
Tetherin/BST-2 is a host-encoded protein that restricts a wide diversity of viruses at the stage of virion release. However, viruses have evolved antagonists of Tetherin, including the Vpu and Nef proteins of primate lentiviruses. Like other host genes subject to viral antagonism, primate Tetherin genes have evolved under positive selection. We show here that viral antagonists acting at three independent sites of selection have driven the evolution of Tetherin, with the strongest selective pressure on the cytoplasmic tail domain. Human Tetherin is unique among the Tetherins of simian primates in that it has a 5-amino-acid deletion that results in the loss of the residue under the strongest positive selection. We show that this residue at amino acid 17 is the site of the functional interaction of Tetherin with Nef, since single amino acid substitutions at this single position can determine the susceptibility of Tetherin to Nef antagonism. While the simian immunodeficiency viruses SIVcpz and SIVgor are able to antagonize their hosts' Tetherin with Nef, human immunodeficiency virus type 1 (HIV-1) Vpu has evolved to counteract Tetherin in humans. We mapped the adaptations in the N-terminal transmembrane domain of Vpu that allow it to counteract human Tetherin. Our combined evolutionary and functional studies have allowed us to reconstruct the host-pathogen interactions that have shaped Tetherin and its lentivirus-encoded antagonists.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.