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Vpx relieves inhibition of HIV-1 infection of macrophages mediated by the SAMHD1 protein
Open accessAbstract
Macrophages and dendritic cells have key roles in viral infections, providing virus reservoirs that frequently resist antiviral therapies and linking innate virus detection to antiviral adaptive immune responses. Human immunodeficiency virus 1 (HIV-1) fails to transduce dendritic cells and has a reduced ability to transduce macrophages, due to an as yet uncharacterized mechanism that inhibits infection by interfering with efficient synthesis of viral complementary DNA. In contrast, HIV-2 and related simian immunodeficiency viruses (SIVsm/mac) transduce myeloid cells efficiently owing to their virion-associated Vpx accessory proteins, which counteract the restrictive mechanism. Here we show that the inhibition of HIV-1 infection in macrophages involves the cellular SAM domain HD domain-containing protein 1 (SAMHD1). Vpx relieves the inhibition of lentivirus infection in macrophages by loading SAMHD1 onto the CRL4(DCAF1) E3 ubiquitin ligase, leading to highly efficient proteasome-dependent degradation of the protein. Mutations in SAMHD1 cause Aicardi-Goutières syndrome, a disease that produces a phenotype that mimics the effects of a congenital viral infection. Failure to dispose of endogenous nucleic acid debris in Aicardi-Goutières syndrome results in inappropriate triggering of innate immune responses via cytosolic nucleic acids sensors. Thus, our findings show that macrophages are defended from HIV-1 infection by a mechanism that prevents an unwanted interferon response triggered by self nucleic acids, and uncover an intricate relationship between innate immune mechanisms that control response to self and to retroviral pathogens.
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In the citing paper
“This approach was necessary because PU.1 is the master transcriptional regulator necessary for macrophage differentiation and silencing PU.1 prior to infection results in a change in the cellular phenotype that causes resistance to HIV infection72,73.”
From HIV-1 Vpr combats the PU.1-driven antiviral response in primary human macrophages (2024) · cites this paper as [73]
Experimental — accuracy not yet measuredIn the citing paper
“It was then determined that Vpx may facilitate the association of SAMHD1 with this complex to promote its proteasome-dependent degradation.”
From Proteomic approaches to uncovering virus–host protein interactions during the progression of viral infection (2016) · cites this paper as [81]
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“Upon MS analysis, the cellular innate immune protein SAMHD1 was the most spectrally abundant association with the Vpx-E3 ubiquitin ligase complex.”
From Proteomic approaches to uncovering virus–host protein interactions during the progression of viral infection (2016) · cites this paper as [81]
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“Recent studies have revealed that Vpx inactivates a myeloid celltype specific antiviral inhibitor sterile alpha motif (SAM) and HD domain-containing protein-1 (SAMHD1) (Berger et al., 2011; Hrecka et al., 2011; Laguette et al., 2011; Shah et al., 2013).”
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HIV-2-Infected Macrophages Produce and Accumulate Poorly Infectious Viral Particles
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Dimeric Hold States of Anti-HIV Protein SAMHD1 are Redox Tunable
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Tissue‐like environments shape functional interactions of HIV‐1 with immature dendritic cells
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“To this end, iDCs were treated 5 days post-initiation of monocyte differentiation with Vpx-containing virus-like particles (Vpx-VLPs) to overcome post-entry blocks to HIV-1 infection such as SAMHD1 (Hrecka et al, 2011; Descours et al, 2012; Baldauf et al, 2012; Baldauf et al, 2017).”
MethodAbemaciclib restricts HCMV replication by suppressing pUL97-mediated phosphorylation of SAMHD1
Syrigos, G. V., Feige, M., Dirlam, A., Businger, R., Gruska, I., Wiebusch, L., Hamprecht, K., & Schindler, M. (2023) · Antiviral Research · doi:10.1016/j.antiviral.2023.105689 · Cited by 5
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“Through its ability to degrade dNTPs, SAMHD1 restricts the replication of retroviruses and DNA viruses, thus blocking the virus life cycle [2,4].”
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Zotova, A., Atemasova, A., Filatov, A. V., & Mazurov, D. V. (2019) · Molecular Biology · doi:10.1134/s0026893319020171 · Cited by 5
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“SAMHD1 was reported to suppress HIV-1 infection of cells of myeloid lineage, including monocyte-derived macrophages [30,31].”
BackgroundInfluentialSIV replication in human cells
Sakuma, R., & Takeuchi, H. (2012) · Frontiers in Microbiology · doi:10.3389/fmicb.2012.00162 · Cited by 5
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An efficient lentiviral CRISPRi approach to silence genes in primary human monocytesPreprint
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“Transduction of cells with a lentivirus together with a VLP containing the HIV-2-derived virion-associated VPX protein leads to degradation of SAMHD1 and efficient lentivirus integration.(11,12) When we infected purified blood-derived CD14 monocytes with VPX-carrying VLPs together with a lentivirus expressing KRABdCas…”
ResultThe emerging roles of ubiquitin-like modifications in regulating HIV replication and host defense
Yuan, J., Wang, H., Sun, X., & Huan, C. (2025) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2025.1593445 · Cited by 5
Chimeric antigen receptor dendritic cells suppress melanoma growth in preclinical cancer models
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“Interestingly, degradation of the SAMHD1 protein in i 3 Neurons by the human immunodeficiency virus type 2 virion-associated protein Vpx 52,53 improved neuronal cisplatin resistance (Figure S6E).”
Acetylation of SAMHD1 at lysine 580 is crucial for blocking HIV-1 infection
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BackgroundEIAV encodes an accessory protein that antagonizes the host restriction factor equine tetherin
Bai, B., Zhang, X. X., Zhang, M., Ma, W.-W., Li, J., Zhang, H., Na, L., Guo, X. Y., Lin, Y., Wang, X., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2413703122 · Cited by 4
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“Sterile alpha-motif and histidine-aspartate domaincontaining (SAMHD1) protein is a triphosphohydrolase (dNTPase) that was originally identified as a Vpx-binding protein, which led to a more comprehensive view of the specific function of Vpx in non-cycling cells [3, 4].”
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Multiple lysines combined in HIV-1 Vif determines the responsiveness to CBF-β
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Retroviral Factors Promoting Infectivity
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The role of SAMHD1 expression and its relation to HIV-2 (Vpx) gene production
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“Recently, HIV2 has been shown to escape the host immune system by targeting a myeloid cell specific restriction factor, SAMHD1 (Hrecka et al., 2011) (Laguette and Benkirane, 2012) (Delucia et al.”
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Role of Intracellular Distribution of Feline and Bovine SAMHD1 Proteins in Lentiviral Restriction
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Thippeshappa, R., Polacino, P. S., Chandrasekar, S., Truong, K., Misra, A., Aulicino, P. C., Hu, S., Kaushal, D., & Kimata, J. T. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.779460 · Cited by 4
HIV-1 infection in sickle cell disease and sickle cell trait: role of iron and innate response
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Human cytomegalovirus UL24 and UL43 products participate in SAMHD1 subcellular localization
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“However, Vpx overcomes this restriction in macrophages by raising intracellular dNTP pools (26, 32).”
BackgroundHIV-1 Adapts To Replicate in Cells Expressing Common Marmoset APOBEC3G and BST2
Fernández-Oliva, A., Finzi, A., Haim, H., Menéndez‐Arias, L., Sodroski, J., & Pacheco, B. (2015) · Journal of Virology · doi:10.1128/jvi.02431-15 · Cited by 4
“The main restriction factors that block HIV-1 and other lentivirus infections at different stages of the viral life cycle are TRIM5 (1), APOBEC3G (A3G) (2), BST2 (3, 4), SAMHD1 (5, 6), and the recently discovered Mx2 (7–9).”
BackgroundDiallo, M. S., Samri, A., Charpentier, C., Bertine, M., Cheynier, R., Thiébaut, R., Matheron, S., Collin, F., Braibant, M., Candotti, D., et al. (2020) · AIDS Research and Human Retroviruses · doi:10.1089/aid.2020.0084 · Cited by 4
“8,9 The high levels of SAMHD1 limit HIV-1 infection in resting CD4 T cells, whereas the SAMHD1 expression decreases in activated cells as a function of cell divisions.”
SAMHD1 Promotes the Antiretroviral Adaptive Immune Response in Mice Exposed to Lipopolysaccharide
Barrett, B. S., Nguyen, D. H. A., Xu, J., Guo, K., Shetty, S., Jones, S. T., Mickens, K. L., Shepard, C., Roers, A., Behrendt, R., et al. (2021) · The Journal of Immunology · doi:10.4049/jimmunol.2001389 · Cited by 4
Nguyen, X.-N., Barateau, V., Wu, N., Berger, G., & Cimarelli, A. (2015) · PLoS ONE · doi:10.1371/journal.pone.0140561 · Cited by 4
“The infection of myeloid cells by primate lentiviruses is however hindered by a strong restriction that limits vDNA accumulation during the early phases of the viral life cycle [5,6,7,8,9,10,11,12,13,14,15].”
BackgroundProspects for Foamy Viral Vector Anti-HIV Gene Therapy
Nalla, A. K., & Trobridge, G. D. (2016) · Biomedicines · doi:10.3390/biomedicines4020008 · Cited by 5
“These include tripartite motif-containing protein 5 alpha (TRIM5α), APOBEC3G, tetherin and SAMHD1 (SAM domain and HD domain-containing protein 1) [112–118].”
BackgroundMaedi-visna virus as a model for HIV
Andrésdóttir, V. (2018) · Icelandic Agricultural Sciences · doi:10.16886/ias.2018.03 · Cited by 4
“SAMHD1 causes inefficient replication of HIV-1 and other lentiviruses in macrophages and dendritic cells, but is antagonized by the viral protein Vpx which targets the protein for proteasomal degradation (Hrecka et al. 2011, Laguette et al. 2011).”
BackgroundFujita, M. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.00254 · Cited by 4
“One of these restriction factors is SAMHD1 (Hrecka et al., 2011; Laguette et al., 2011).”
InfluentialEvasion of CARD8 activation during HIV-1 assembly
Hughes, I. K., Hood, J. B., Quiñones-Molina, A. A., Akiyama, H., & Gummuluru, S. (2025) · Science Advances · doi:10.1126/sciadv.adz1069 · Cited by 3
“…vesicular stomatitis virus glycoprotein (VSVG)–pseudotyped HIV-1 and simian immunodeficiency virus viral protein X (Vpx)- containing virus-like particles [SIV3 + VLPs; to overcome SAM domain and HD domain-containing protein 1 (SAMHD1)- mediated restriction of HIV-1 in myeloid cells] ( 24 ).”
Sun, J., Zheng, W., Zhang, Z.-G., Zhou, H., Wang, S., Huang, D., Hu, X., Yu, Q., Wu, Z., Shi, Y., et al. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02523-1 · Cited by 3
“1,7,52,53 Altered dNTP levels could result in DNA damage and aberrant replication, potentially leading to tumorigenesis.”
Nair, R., Salinas-Illarena, A., Sponheimer, M., Wullkopf, I., Schreiber, Y., Côrte‐Real, J. V., Ben, A. D. P., Marterer, H., Thomas, D., Geißlinger, G., et al. (2024) · Clinical and Experimental Medicine · doi:10.1007/s10238-024-01425-w · Cited by 3
“In particular, amino acid 75 is close to the known Q76 position, which is essential for Vpx binding to DCAF1 [12].”
BackgroundE3 ligase RAD18 targets phosphorylated IRF3 to terminate IFNB1 transcription
Cai, Y., Zheng, J., Zhao, L., Wang, X., Zhang, P., Wang, J., Zhang, Y., Shi, R., Han, J., Han, W., et al. (2025) · Nature Immunology · doi:10.1038/s41590-025-02256-x · Cited by 3
“These recovered individuals were categorized into mild and severe subgroups according to severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection 32 , and CD14 + monocytes were isolated from peripheral blood mononuclear cells (PBMCs) to generate monocyte-derived macrophages (MDMs) 33 .”
Keeping your armour intact: How HIV‐1 evades detection by the innate immune system
Maelfait, J., Seiradake, E., & Rehwinkel, J. (2014) · BioEssays · doi:10.1002/bies.201400019 · Cited by 3
“Vpx targets the host restriction factor SAMHD1 for proteasomal degradation [78, 79].”
BackgroundLentiviral Vpx induces alteration of mammalian cell nuclear envelope integrity
Singh, S. P., Raja, S., & Mahalingam, S. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.02.018 · Cited by 3
Shimagaki, K., Koga, R., Fujino, H., Ahagon, A., Tateishi, H., Otsuka, M., Yamaguchi, Y., & Fujita, M. (2020) · Journal of General Virology · doi:10.1099/jgv.0.001456 · Cited by 3
Vasudevan, A. A. J., Balakrishnan, K., Franken, A., Krikoni, A., Häussinger, D., Luedde, T., & Münk, C. (2021) · Virology · doi:10.1016/j.virol.2021.01.017 · Cited by 3
Minimal impact of ZAP on lentiviral vector production and transduction efficiency
Sertkaya, H., Hidalgo, L., Ficarelli, M., Kmieć, D., Signell, A. W., Ali, S., Parker, H., Wilson, H., Neil, S. J. D., Malim, M. H., et al. (2021) · Molecular Therapy — Methods & Clinical Development · doi:10.1016/j.omtm.2021.08.008 · Cited by 3
You, D., Zhang, S., Yan, S., Ding, Y., Li, C., Cheng, X., Wu, L., Wang, W., Zhang, T., Li, Z., et al. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.939982 · Cited by 3
HIV-1 Transcription Inhibitor 1E7-03 Decreases Nucleophosmin Phosphorylation
Lin, X., Ahmad, A., Ivanov, A. I., Simhadri, J. J., Wang, S., Kumari, N., Ammosova, T., & Nekhai, S. A. (2022) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2022.100488 · Cited by 3
Maehigashi, T., Lim, C. S., Wade, L. R., Bowen, N. E., Knecht, K. M., Alvarez, N. N., Kelly, W. G., Schinazi, R. F., Kim, D., Xiong, Y., et al. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105148 · Cited by 3
“However, unlike HIV-1, HIV-2 and many simian immunodeficiency viruses encode an accessary protein, viral protein X (Vpx), which proteosomally degrades SAMHD1 (7, 8), leading to the elevation of the cellular dNTP levels and ultimately to the infectivity enhancement of these lentiviruses in the myeloid cells (16).”
BackgroundDeubiquitinase USP37 enhances the anti-HIV-2/SIV ability of the host restriction factor SAMHD1
Cui, W., Wang, H., Gao, Y., Zhang, X., Xin, J., Li, Z., Li, G., Gao, W., & Zhang, W. (2024) · Journal of Virology · doi:10.1128/jvi.01858-24 · Cited by 3
HIV capsids: orchestrators of innate immune evasion, pathogenesis and pandemicity
Morling, K. L., ElGhazaly, M., Milne, R. S. B., & Towers, G. J. (2025) · Journal of General Virology · doi:10.1099/jgv.0.002057 · Cited by 7
“Furthermore, mutating HIV-1 p6 so that it can incorporate Vpx expressed in trans [167] and treating cells with virus-like particles (VLPs) bearing Vpx both enhance HIV-1 single-round infection in myeloid cells [131, 166, 168, 169].”
Hellenbrand, C. N., Stevenson, D. M., Gromek, K. A., Amador‐Noguez, D., & Hershey, D. M. (2025) · Journal of Bacteriology · doi:10.1128/jb.00145-25 · Cited by 3
Review of basic science advances in HIV.
Stevenson, M. (2012) · Europe PMC (PubMed Central) · Cited by 3
Properties of Human and Simian Immunodeficiency Viruses
Sauter, D., & Kirchhoff, F. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-404734-1.00004-8 · Cited by 3
Cellular Factors That Regulate Retrovirus Uncoating and Reverse Transcription
Goff, S. P. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-811185-7.00002-9 · Cited by 3
Факторы рестрикции вируса иммунодефицита человека и их неоднозначная роль в инфекции
Zotova, A., Atemasova, A., Filatov, A. V., & Mazurov, D. V. (2019) · Molecular Biology · doi:10.1134/s0026898419020174 · Cited by 4
Bao, Q., & Zhou, J. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115188 · Cited by 4
HIV-Infektion – Virus, Immunologie, Pathogenese
Metzner, K. J. (2014) · Therapeutische Umschau · doi:10.1024/0040-5930/a000536 · Cited by 4
Inhibition of HIV Replication by Host Cellular Factors
Azevedo‐Pereira, J. M., Canhão, P., Calado, M. S., Santos‐Costa, Q., & Barroca, P. (2015) · InTech eBooks · doi:10.5772/60795 · Cited by 4
“Sterile alpha motif (SAM) and histidine/aspartic acid (HD) domain-containing protein 1 (SAMHD1), an analogue of the murine IFN-y-induced gene Mg11 [136], was identified as a HIV-1 restriction factor that blocks early-stage virus replication in DCs and other myeloid cells [137, 138].”
BackgroundTwo Tales (Tails) of SAMHD1 Destruction by Vpx
Ji, X., & Xiong, Y. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2015.03.013 · Cited by 3
Mx Oligomer: A Novel Capsid Pattern Sensor?
Kong, J., Ma, M., He, S., & Qin, X. (2016) · Future Microbiology · doi:10.2217/fmb-2016-0004 · Cited by 3
Münch, J., & Kirchhoff, F. (2011) · Elsevier eBooks · doi:10.1016/b978-0-12-387715-4.00001-0 · Cited by 3
Post-entry Restriction Factors of SIVcpz
Twizerimana, A. P., Scheck, R., Häussinger, D., & Münk, C. (2018) · Future Virology · doi:10.2217/fvl-2018-0093 · Cited by 3
Kong, J., Wang, M., He, S., Peng, X., & Qin, X. (2019) · FEBS Journal · doi:10.1111/febs.14943 · Cited by 3
Xu, F., Zhao, F., Zhao, X., Zhang, D., Liu, X., Hu, S., Mei, S., Fan, Z., Huang, Y., Sun, H., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.012439 · Cited by 3
“the N terminal (1-25) deletion, lacking the NLS, was dispersed in the cytoplasm.”
BackgroundMethodInfluentialKazmierski, J., Postmus, D., Pietrobon, A. J., Wyler, E., Jansen, J., Møller, L. F., Fadejeva, J., Steijaert, T. H., Fischer, C., Koppe, U., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.04.075119 · Cited by 3
“…2002), IFITM1 -3 (Compton et al., 2014; Foster et al., 2016; Tartour et al., 2014), MX2 (Goujon et al., 2013; Kane et al., 2013; Liu et al., 2013) and SAMHD1 (Hrecka et al., 2011; Laguette et al., 2011) were downregulated in the context of Panobinostat treatment for the majority of cell subsets.”
BackgroundHIV-1 latency: From acquaintance to confidant
Yang, C., Tong, L., & Xue, J. (2025) · Journal of Virus Eradication · doi:10.1016/j.jve.2025.100597 · Cited by 3
“141,147,148 It has been reported that the HIV-2 and SIV Vpx proteins counteract this restriction by promoting the degradation of SAMHD1, which leads to an increase in cellular dNTP levels and facilitates the completion of viral reverse transcription.”
Li, Y., Qu, L., Tang, Y., Ni, F., Shen, S., Guo, H., Yu, X., & Wei, W. (2025) · Journal of Virology · doi:10.1128/jvi.00354-25 · Cited by 2
“In addition, HIV-2 Vpx hijacks host CRL4(DCAF1) E3 ligase to downregulate the expression of antiviral factor SAMHD1, thereby facilitating intrinsic immune evasion (11– 13).”
Aicardi-Goutières Syndrome caused by SAMHD1 mutation: Pathogenesis and Beyond
Li, Y., & Ying, S. (2026) · Clinical Immunology · doi:10.1016/j.clim.2026.110680 · Cited by 2
Chen, X., Zhou, F., Chen, Q., Dong, J., Zhang, Y., Liu, X., Zhang, Y., & Xu, J. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6c00025 · Cited by 2
Transcription start site heterogeneity controls MDA5 sensing of unspliced HIV-1 RNAs
Hughes, I. A., Kharytonchyk, S., Ramaswamy, S., Jalloh, S., Hood, J. B., He, X., Henderson, A. J., Akiyama, H., Telesnitsky, A., & Gummuluru, S. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2522948123 · Cited by 4
“To overcome SAMHD1 - mediated inhibition of reverse transcription in primary MDMs, we coinfected with SIVmac Vpx - containing VLPs (SIV3+ VLPs) as previously described (27).”
Sun, Y. W., Shang, H.-M., Wang, M.-D., Huang, M.-W., Qing, Y.-X., Cai, Y.-Y., Luo, Y., Lu, Z.-D., Bian-xia, L., Du, X., et al. (2026) · ACS Nano · doi:10.1021/acsnano.5c21015 · Cited by 2
Shared principles of human and bacterial antiviral immunity
Kranzusch, P. J. (2026) · Nature · doi:10.1038/s41586-026-10756-5 · Cited by 5
“Nucleotides are particularly conserved targets of antiviral immunity with the dNTPase SAMHD1 in animals 232,233 , the Detocs system and multiple additional dNTPases in bacteria 116,234,235 , and AvcID and RADAR nucleotide deaminase systems in bacteria 185,186,236 each reducing nucleotide…”
Stevenson, M., Chomont, N., & Lafeuillade, A. (2012) · AIDS Research and Therapy · doi:10.1186/1742-6405-9-7 · Cited by 2
“In the past year, research from 2 groups identified the restriction as a deoxynucleoside triphosphate triphosphohydreolase called SAMHD1 [11,12].”
BackgroundInfluentialHuman Immunodeficiency Virus Type-1
Spector, S. A. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.00088-x · Cited by 2
Toward the unveiling of HIV-1 dynamics: Involvement of monocytes/macrophages in HIV-1 infection
Sukegawa, S., & Takeuchi, H. (2022) · Frontiers in Virology · doi:10.3389/fviro.2022.934892 · Cited by 2
Tada, T., Norton, T. D., Leibowitz, R., & Landau, N. R. (2024) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2023-008761 · Cited by 2
Blockade of de novo dNTP biosynthesis pathway delays HIV-1 early life cycle kinetics and dynamics
Siddique, M. A., McRaven, M. D., Arif, M. S., Allen, E. J., McKee, C., Honne, S., Sultana, T., Kim, B., Carias, A. M., Mamede, J. I., et al. (2025) · mBio · doi:10.1128/mbio.01047-25 · Cited by 2
“The activation of cells can also overcome SAMHD1 activity through specific phosphorylation that inhibits the dNTP hydrolysis activity (9, 11, 13, 18, 19).”
Shigematsu, S., Hayashi, H., Yasui, K., & Matsuyama, T. (2014) · Institutional Repositories DataBase (IRDB) · doi:10.11343/amn.58.103 · Cited by 2
HIV-1/HIV-2 versus SAMHD1 Restriction: A Tale of Two Viruses
Wei, W., & Yu, X.-F. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2014.12.005 · Cited by 2
“Interestingly, cyclin L2-mediated SAMHD1 regulation is very similar to Vpx-induced SAMHD1 degradation (Figure 1), which also engages the cellular CRL4-DCAF1 E3 ligase (Hrecka et al., 2011; Laguette et al., 2011).”
BackgroundEvidence that HIV-1 restriction factor SAMHD1 facilitates differentiation of myeloid THP-1 cells
Dragin, L., Munir, S., Froehlich, J., Morel, M., Sourisce, A., Lahouassa, H., Bailly, K., Mangeney, M., Ramírez, B. C., & Margottin-Goguet, F. (2015) · Virology Journal · doi:10.1186/s12985-015-0425-y · Cited by 2
“Among them, sterile alpha motif and HDdomain containing protein 1 (SAMHD1) inhibits both HIV-1 and Vpx-deleted HIV-2/SIVsmm viruses at the level of reverse transcription [1, 2].”
Background
Metadata
- Authors
- Hrecka, K., Hao, C., Gierszewska, M., Swanson, S. K., Kesik-Brodacka, M., Srivastava, S., Florens, L., Washburn, M. P., & Skowronski, J.
- Affiliations
- Case Western Reserve University (US)
- Cold Spring Harbor Laboratory (US)
- Stowers Institute for Medical Research (US)
- Venue
- Nature
- Published
- 2011-06
- Volume
- 474
- Issue
- 7353
- Pages
- 658-661
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC3179858
- OpenAlex
- W1964567249
- Cited by
- 1,200
- References
- 30
- Citations by year
- 2026: 30 · 2025: 51 · 2024: 54 · 2023: 47 · 2022: 62 · 2021: 58 · 2020: 66 · 2019: 82 · 2018: 88 · 2017: 87 · 2016: 91 · 2015: 101 · 2014: 125 · 2013: 125 · 2012: 109
- FWCI
- 48.11
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Cold Spring Harbor Laboratory Institutional Repository (Cold Spring Harbor Laboratory) (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (R21AI084694, R01AI077459)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Virus-based gene therapy research
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Keywords
- HIV-1, Vpx, SAMHD1, macrophages, dendritic cells, host restriction factors, proteasomal degradation, Aicardi-Goutières syndrome, innate immunity, interferon response, retroviral infection, HIV-2, simian immunodeficiency virus
- MeSH terms
- SAM Domain and HD Domain-Containing Protein 1, Carrier Proteins, Cells, Cultured, Humans, Macrophages, Nuclear Proteins, HIV-1, HIV Infections, Protein Serine-Threonine Kinases, Monomeric GTP-Binding Proteins, Ubiquitin-Protein Ligases, Proteasome Endopeptidase Complex, Viral Regulatory and Accessory Proteins, HEK293 Cells
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