ArticleThe Journal of biological chemistry2012
Functional analysis of the relationship between Vpx and the restriction factor SAMHD1.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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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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Who cites it
19 citing papers in PubMed, 32 citations in OpenAlex.
- Role of Intracellular Distribution of Feline and Bovine SAMHD1 Proteins in Lentiviral Restriction.Virologica Sinica · 2021Article
- The C-terminal domain of feline and bovine SAMHD1 proteins has a crucial role in lentiviral restriction.The Journal of biological chemistry · 2020Article
- TRIM21-mediated proteasomal degradation of SAMHD1 regulates its antiviral activity.EMBO reports · 2020Article
- Human cytomegalovirus overcomes SAMHD1 restriction in macrophages via pUL97.Nature microbiology · 2019Article
- SAMHD1: Recurring roles in cell cycle, viral restriction, cancer, and innate immunity.Autoimmunity · 2018Review
- Incomplete Suppression of HIV-1 by SAMHD1 Permits Efficient Macrophage Infection.Pathogens & immunity · 2018Article
- SAMHD1 controls cell cycle status, apoptosis and HIV-1 infection in monocytic THP-1 cells.Virology · 2016Article
- Interferon regulatory factor 3 is a key regulation factor for inducing the expression of SAMHD1 in antiviral innate immunity.Scientific reports · 2016Article
- The susceptibility of primate lentiviruses to nucleosides and Vpx during infection of dendritic cells is regulated by CA.Journal of virology · 2015Article
- Discovery and characterization of auxiliary proteins encoded by type 3 simian T-cell lymphotropic viruses.Journal of virology · 2015Article
- Tissue myeloid cells in SIV-infected primates acquire viral DNA through phagocytosis of infected T cells.Immunity · 2014Article
- dNTP pool modulation dynamics by SAMHD1 protein in monocyte-derived macrophages.Retrovirology · 2014Article
- Dendritic cell-lymphocyte cross talk downregulates host restriction factor SAMHD1 and stimulates HIV-1 replication in dendritic cells.Journal of virology · 2014Article
- Specific and nonhepatotoxic degradation of nuclear hepatitis B virus cccDNA.Science (New York, N.Y.) · 2014Article
- Design and Potential of Non-Integrating Lentiviral Vectors.Biomedicines · 2014Review
- New insights into an X-traordinary viral protein.Frontiers in microbiology · 2014Review
- Variation of two primate lineage-specific residues in human SAMHD1 confers resistance to N terminus-targeted SIV Vpx proteins.Journal of virology · 2014Article
- Interferon block to HIV-1 transduction in macrophages despite SAMHD1 degradation and high deoxynucleoside triphosphates supply.Retrovirology · 2013Article
- Identification of critical regions in human SAMHD1 required for nuclear localization and Vpx-mediated degradation.PloS one · 2013Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SAMHD1 is a newly identified restriction factor that targets lentiviruses in myeloid cells and is countered by the SIV(SM)/HIV-2 Vpx protein. By analyzing a large panel of Vpx mutants, we identify several residues throughout the 3-helix bundle predicted for Vpx that impair both its functionality and its ability to degrade SAMHD1. We determine that SAMHD1 is a strictly non-shuttling nuclear protein and that as expected WT Vpx localizes with it in the nucleus. However, we also identify a functional Vpx mutant with predominant cytoplasmic distribution that colocalizes with SAMHD1 in this location, suggesting that Vpx may also retain SAMHD1 in the cell cytoplasm, prior to its entry into the nucleus. Several mutations in Vpx were shown to affect the stability of Vpx, as well as Vpx:Vpx interactions. However, no strict correlation was observed between these parameters and the functionality of Vpx, implying that neither properties is absolutely required for this function and indicating that even unstable Vpx mutants may be very efficient in inducing SAMHD1 degradation. Overall, our analysis identifies several Vpx residues required for SAMHD1 degradation and points to a very efficient and plastic mechanism through which Vpx depletes this restriction factor.
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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.