ArticlePloS one2011
Molecular design, functional characterization and structural basis of a protein inhibitor against the HIV-1 pathogenicity factor Nef.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 32 citations in OpenAlex.
- HIV-1 Nef Uses a Conserved Pocket to Recruit the N-Terminal Cytoplasmic Tail of Serinc3.Viruses · 2025Article
- Synergy and allostery in ligand binding by HIV-1 Nef.The Biochemical journal · 2021Article
- Structure, function, and inhibitor targeting of HIV-1 Nef-effector kinase complexes.The Journal of biological chemistry · 2020Review
- Structure of HIV-2 Nef Reveals Features Distinct from HIV-1 Involved in Immune Regulation.iScience · 2020Article
- How HIV Nef Proteins Hijack Membrane Traffic To Promote Infection.Journal of virology · 2019Review
- Lovastatin Inhibits HIV-1-Induced MHC-I Downregulation by Targeting Nef-AP-1 Complex Formation: A New Strategy to Boost Immune Eradication of HIV-1 Infected Cells.Frontiers in immunology · 2019Article
- A single β-octyl glucoside molecule induces HIV-1 Nef dimer formation in the absence of partner protein binding.PloS one · 2018Article
- Tat-induced histopathological alterations mediate hippocampus-associated behavioural impairments in rats.Behavioral and brain functions : BBF · 2015Article
- HIV-1 Infection of T Lymphocytes and Macrophages Affects Their Migration via Nef.Frontiers in immunology · 2015Review
- HIV-1 Nef and Vpu are functionally redundant broad-spectrum modulators of cell surface receptors, including tetraspanins.Journal of virology · 2014Article
- Structural basis for the inhibition of HIV-1 Nef by a high-affinity binding single-domain antibody.Retrovirology · 2014Article
- Expression, purification and preliminary crystallographic studies of the C-terminal SH3 domain of human Tks4.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Article
- Viral proteins and Src family kinases: Mechanisms of pathogenicity from a "liaison dangereuse".World journal of virology · 2013Review
- A Biochemical/Biophysical Assay Dyad for HTS-Compatible Triaging of Inhibitors of the HIV-1 Nef/Hck SH3 Interaction.Current chemical genomics and translational medicine · 2013Article
- Single-domain antibody-SH3 fusions for efficient neutralization of HIV-1 Nef functions.Journal of virology · 2012Article
- Identification of a highly conserved valine-glycine-phenylalanine amino acid triplet required for HIV-1 Nef function.Retrovirology · 2012Article
- The Continuing Evolution of HIV-1 Therapy: Identification and Development of Novel Antiretroviral Agents Targeting Viral and Cellular Targets.Molecular biology international · 2012Article
- Intracellular overexpression of HIV-1 Nef impairs differentiation and maturation of monocytic precursors towards dendritic cells.PloS one · 2012Article
- High-affinity target binding engineered via fusion of a single-domain antibody fragment with a ligand-tailored SH3 domain.PloS one · 2012Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Increased spread of HIV-1 and rapid emergence of drug resistance warrants development of novel antiviral strategies. Nef, a critical viral pathogenicity factor that interacts with host cell factors but lacks enzymatic activity, is not targeted by current antiviral measures. Here we inhibit Nef function by simultaneously blocking several highly conserved protein interaction surfaces. This strategy, referred to as "wrapping Nef", is based on structure-function analyses that led to the identification of four target sites: (i) SH3 domain interaction, (ii) interference with protein transport processes, (iii) CD4 binding and (iv) targeting to lipid membranes. Screening combinations of Nef-interacting domains, we developed a series of small Nef interacting proteins (NIs) composed of an SH3 domain optimized for binding to Nef, fused to a sequence motif of the CD4 cytoplasmic tail and combined with a prenylation signal for membrane association. NIs bind to Nef in the low nM affinity range, associate with Nef in human cells and specifically interfere with key biological activities of Nef. Structure determination of the Nef-inhibitor complex reveals the molecular basis for binding specificity. These results establish Nef-NI interfaces as promising leads for the development of potent Nef inhibitors.
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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.