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Identification of Host Proteins Required for HIV Infection Through a Functional Genomic Screen
Abstract
HIV-1 exploits multiple host proteins during infection. We performed a large-scale small interfering RNA screen to identify host factors required by HIV-1 and identified more than 250 HIV-dependency factors (HDFs). These proteins participate in a broad array of cellular functions and implicate new pathways in the viral life cycle. Further analysis revealed previously unknown roles for retrograde Golgi transport proteins (Rab6 and Vps53) in viral entry, a karyopherin (TNPO3) in viral integration, and the Mediator complex (Med28) in viral transcription. Transcriptional analysis revealed that HDF genes were enriched for high expression in immune cells, suggesting that viruses evolve in host cells that optimally perform the functions required for their life cycle. This effort illustrates the power with which RNA interference and forward genetics can be used to expose the dependencies of human pathogens such as HIV, and in so doing identify potential targets for therapy.
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“Host proteins with potential functions in the viral lifecycle have also been identified using siRNA-based screens (125-127).”
From Role of host tRNAs and aminoacyl-tRNA synthetases in retroviral replication (2019) · cites this paper as [127]
In the citing paper
“| Mixed pattern of regulation upon HIV-1 infection | GlyRS | 127 |”
From Role of host tRNAs and aminoacyl-tRNA synthetases in retroviral replication (2019) · cites this paper as [127]
In the citing paper
“The five ARSs listed exhibit a significant decrease (Ն16-fold) in transcript levels.”
From Role of host tRNAs and aminoacyl-tRNA synthetases in retroviral replication (2019) · cites this paper as [127]
In the citing paper
“| Levels of transcripts decrease upon HIV-1 infection b | EPRS a , TyrRS, MetRS a , HisRS, PheRS | 127 |”
From Role of host tRNAs and aminoacyl-tRNA synthetases in retroviral replication (2019) · cites this paper as [127]
In the citing paper
“| Levels of transcripts increase upon HIV-1 infection | AsnRS, CysRS | 127 |”
From Role of host tRNAs and aminoacyl-tRNA synthetases in retroviral replication (2019) · cites this paper as [127]
In the citing paper
“Five other ARSs, AlaRS, IleRS, LysRS, ValRS, and GlnRS, exhibit a moderate decrease (ϳ4fold) in HIV-1-infected cells.”
From Role of host tRNAs and aminoacyl-tRNA synthetases in retroviral replication (2019) · cites this paper as [127]
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Host factors exploited by retroviruses
Goff, S. P. (2007) · Nature Reviews Microbiology · doi:10.1038/nrmicro1541 · Cited by 247
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Items 401–500 of 1,000
A Cyclophilin Homology Domain-Independent Role for Nup358 in HIV-1 Infection
Meehan, A. M., Saenz, D. T., Guevara, R. B., Morrison, J. H., Peretz, M., Fadel, H. J., Hamada, M., van Deursen, J., & Poeschla, E. M. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1003969 · Cited by 56
“Our results are in agreement with previous knockdown studies in concluding that acute depletion of Nup358 does clearly inhibit HIV-1 infection [19,20,24,26,28,29].”
BackgroundResultCodlin, S., & Mole, S. (2009) · Journal of Cell Science · doi:10.1242/jcs.038323 · Cited by 51
Yang, S., Chen, F., Lian, X., Dong, X., & Zhang, Z. (2019) · mSystems · doi:10.1128/msystems.00303-18 · Cited by 54
Huang, H., Santoso, N. G., Power, D. G., Simpson, S., Dieringer, M., Miao, H., Gurova, K. V., Giam, C., Elledge, S. J., & Zhu, J. K. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.652339 · Cited by 59
Self-citationEspeseth, A. S., Fishel, R., Hazuda, D. J., Huang, Q., Xu, M., Yoder, K. E., & Zhou, H. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017612 · Cited by 57
“Comparing our results with a targeted siRNA screen to those of genome scale screens reveals that although the genome scale screens all identified DNA repair factors, there was no overlap in the specific DNA repair factors identified, and no indication of which DNA repair pathway(s) may be most relevant for HIV replica…”
ResultGenetic Variants in Nuclear-Encoded Mitochondrial Genes Influence AIDS Progression
Hendrickson, S. L., Lautenberger, J. A., Chinn, L. W., Malasky, M., Sezgın, E., Kingsley, L., Goedert, J. J., Kirk, G. D., Gomperts, E. D., Buchbinder, S., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012862 · Cited by 55
“We also examined NEMPs that were previously reported as cellular gene products required for HIV-infection in screens using siRNAs [16,17,18], mRNA expression [21], or proteomics [19,20] for SNPs associated with AIDS-1987.”
BackgroundInfluentialIdentifying potential survival strategies of HIV-1 through virus-host protein interaction networks
van Dijk, D., Ertaylan, G., Boucher, C. A., & Sloot, P. M. A. (2010) · BMC Systems Biology · doi:10.1186/1752-0509-4-96 · Cited by 36
“In addition to the NCBI database there are three other independent data-sets available as a result of small interfering RNA (siRNA) screens [23-25].”
The Overlap of Small Molecule and Protein Binding Sites within Families of Protein Structures
Davis, F. P., & Šali, A. (2010) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000668 · Cited by 47
“In addition, a therapeutic application that is becoming increasingly relevant is the targeting of host–pathogen protein interactions, which have been the subject of recent investigations using highthroughput experimental [48,49] and computational [50,51] methods.”
BackgroundX Chromosomal Variation Is Associated with Slow Progression to AIDS in HIV-1-Infected Women
Siddiqui, R. A., Sauermann, U., Altmüller, J., Fritzer, E., Nothnagel, M., Dalibor, N., Fellay, J., Kaup, F., Stahl‐Hennig, C., Nürnberg, P., et al. (2009) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2009.07.013 · Cited by 48
Clinical effectiveness of dolutegravir in the treatment of HIV/AIDS
Taha, H., Das, A., & Das, S. (2015) · Infection and Drug Resistance · doi:10.2147/idr.s68396 · Cited by 49
Host Factors in Retroviral Integration and the Selection of Integration Target Sites
Craigie, R., & Bushman, F. D. (2014) · Microbiology Spectrum · doi:10.1128/microbiolspec.mdna3-0026-2014 · Cited by 49
Positive selection of primate genes that promote HIV-1 replication
Meyerson, N. R., Rowley, P. A., Swan, C. H., Le, D. T., Wilkerson, G. K., & Sawyer, S. L. (2014) · Virology · doi:10.1016/j.virol.2014.02.029 · Cited by 54
“Collectively, these screens uncovered approximately a thousand genes that lead to reduced HIV replication when their expression is decreased (Brass et al., 2008; König et al., 2008; Yeung et al., 2009; Zhou et al., 2008).”
Bernier, A., Cleret‐Buhot, A., Zhang, Y., Goulet, J.-P., Monteiro, P., Gosselin, A., DaFonseca, S., Wacleche, V. S., Jenabian, M.-A., Routy, J., et al. (2013) · Retrovirology · doi:10.1186/1742-4690-10-160 · Cited by 53
Hori, T., Takeuchi, H., Saito, H., Sakuma, R., Inagaki, Y., & Yamaoka, S. (2013) · Journal of Virology · doi:10.1128/jvi.00124-13 · Cited by 48
Quantitative proteomic analysis of exosomes from HIV-1 infected lymphocytic cells
Li, M., Aliotta, J., Asara, J. M., Tucker, L., Quesenberry, P., Lally, M., & Ramratnam, B. (2012) · Proteomics · doi:10.1002/pmic.201100376 · Cited by 49
“For example, a recent genome-wide small interfering RNA screen identified more than 250 host factors required by HIV-1 to complete its life cycle [1].”
BackgroundMethodVerrier, E. R., Weiss, A., Bach, C., Heydmann, L., Turon-Lagot, V., Kopp, A., el Saghire, H., Crouchet, E., Pessaux, P., Garcia, T., et al. (2019) · Gut · doi:10.1136/gutjnl-2018-317065 · Cited by 48
“15 16 Functional pathway analysis using KEGG pathways identified a network of host factors belonging to HSPG biosynthesis, including EXT1 and EXT2 (figure 2A,B).”
Role of Microtubules and Microtubule-Associated Proteins in HIV-1 Infection
Dharan, A., & Campbell, E. M. (2018) · Journal of Virology · doi:10.1128/jvi.00085-18 · Cited by 52
Cellular fatty acid synthase is required for late stages of HIV-1 replication
Kulkarni, M., Ratcliff, A. N., Bhat, M., Alwarawrah, Y., Hughes, P. F., Arcos, J., Loiselle, D. R., Torrelles, J. B., Funderburg, N., Haystead, T., et al. (2017) · Retrovirology · doi:10.1186/s12977-017-0368-z · Cited by 51
Nakaya, H. I., & Pulendran, B. (2011) · Current Opinion in HIV and AIDS · doi:10.1097/coh.0b013e32834dc37b · Cited by 53
RNAi Screen Indicates Widespread Biological Function for Human Natural Antisense Transcripts
Faghihi, M. A., Kocerha, J., Modarresi, F., Engström, P. G., Chalk, A. M., Brothers, S. P., Koesema, E., Laurent, G. S., & Wahlestedt, C. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013177 · Cited by 46
“Among these, RNA interference (RNAi) can be used to expedite genome-wide loss-of-function (LOF) screens in mammalian systems [26,27,28,29].”
Cellular and viral determinants of retroviral nuclear entry
Hamid, F. B., Kim, J., & Shin, C.-G. (2016) · Canadian Journal of Microbiology · doi:10.1139/cjm-2015-0350 · Cited by 48
“…family, including 252 NUP358/RAN BP2, NUP153, NUP98, and NUP214/CAN (NUP 50, 62, 85, 107, 133, 155,160, 253 210, ELYS, and TRP) (Ebina et al. 2004; Brass et al. 2008; König et al. 2008; Woodward et al. 254 2009; Lee et al. 2010; Zhang et al. 2010; Matreyek and Engelman 2011, 2013a; Di Nunzio et…”
HIV-1 requires capsid remodelling at the nuclear pore for nuclear entry and integration
Guedán, A., Donaldson, C. D., Caroe, E. R., Cosnefroy, O., Taylor, I. A., & Bishop, K. N. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009484 · Cited by 47
“Furthermore, both proteins have previously been described to bind HIV-1 CA directly and to be involved in HIV-1 replication [25,26,30].”
BackgroundNuclear Envelope Protein SUN2 Promotes Cyclophilin-A-Dependent Steps of HIV Replication
Lahaye, X., Satoh, T., Gentili, M., Cerboni, S., Silvin, A., Conrad, C., Ahmed‐Belkacem, A., Rodriguez, E. C., Guichou, J., Dereuddre‐Bosquet, N., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.03.074 · Cited by 53
Deffrasnes, C., Marsh, G. A., Foo, C. H., Rootes, C. L., Gould, C. M., Grusovin, J., Monaghan, P., Lo, M. K., Tompkins, S. M., Adams, T. E., et al. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005478 · Cited by 61
Ty3, a Position-specific Retrotransposon in Budding Yeast
Sandmeyer, S., Patterson, K., & Bilanchone, V. (2015) · Microbiology spectrum · doi:10.1128/microbiolspec.mdna3-0057-2014 · Cited by 47
Henning, M. S., Dubose, B. N., Burse, M. J., Aiken, C., & Yamashita, M. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1003868 · Cited by 46
“Since MLV is blocked in non-dividing cells [12,13] at nuclear entry [14], HIV-1 must be equipped with a CA-dependent mechanism to utilize the host nuclear transport machinery to infect non-dividing cells.”
BackgroundInfluentialDifferential Trends in the Codon Usage Patterns in HIV-1 Genes
Pandit, A., & Sinha, S. (2011) · PLoS ONE · doi:10.1371/journal.pone.0028889 · Cited by 43
Mascarenhas, A. P., & Musier-Forsyth, K. (2009) · The FEBS Journal · doi:10.1111/j.1742-4658.2009.07315.x · Cited by 47
NHEJ pathway is involved in post-integrational DNA repair due to Ku70 binding to HIV-1 integrase
Knyazhanskaya, E., Anisenko, A., Shadrina, O., Kalinina, A., Zatsepin, T., Zalevsky, A., Mazurov, D., & Gottikh, M. (2019) · Retrovirology · doi:10.1186/s12977-019-0492-z · Cited by 46
Insights Into Persistent HIV-1 Infection and Functional Cure: Novel Capabilities and Strategies
Ta, T. M., Malik, S., Anderson, E. M., Jones, A. D., Perchik, J., Freylikh, M., Sardo, L., Klase, Z. A., & Izumi, T. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.862270 · Cited by 61
Regulation of HIV-1 Latency by Chromatin Structure and Nuclear Architecture
Lušić, M., & Giacca, M. (2014) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.07.022 · Cited by 43
miRNA-1236 Inhibits HIV-1 Infection of Monocytes by Repressing Translation of Cellular Factor VprBP
Ma, L., Shen, C., Cohen, É. A., Xiong, S., & Wang, J.-H. (2014) · PLoS ONE · doi:10.1371/journal.pone.0099535 · Cited by 49
Cell-based genomic screening: elucidating virus-host interactions
Panda, D., & Cherry, S. (2012) · Current Opinion in Virology · doi:10.1016/j.coviro.2012.10.007 · Cited by 46
Inhibition of HIV-1 Integration in Ex Vivo-Infected CD4 T Cells from Elite Controllers
Buzón, M., Seiss, K., Weiss, R., Brass, A., Rosenberg, E., Pereyra, F., Yu, X. G., & Lichterfeld, M. (2011) · Journal of Virology · doi:10.1128/jvi.05327-11 · Cited by 46
“were infected with a yellow fluorescence protein (YFP)-encoding vesicular stomatitis virus G protein (VSV-G) pseudotyped HIV-1 virus (3) (50% tissue culture infective dose [TCID50] of 5,000) that infects cells independently of coreceptor-mediated entry processes and causes only a single round of infection, thus allowi…”
MethodSelf-citationFactors Affecting Reproducibility between Genome-Scale siRNA-Based Screens
Barrows, N. J., Sommer, C., García-Blanco, M. A., & Pearson, J. L. (2010) · SLAS DISCOVERY · doi:10.1177/1087057110374994 · Cited by 39
Nucleic Acids-Based Therapeutics in the Battle Against Pathogenic Viruses
Haasnoot, J., & Berkhout, B. (2008) · Handbook of experimental pharmacology · doi:10.1007/978-3-540-79086-0_9 · Cited by 43
“(2008) published a large-scale siRNA screen to identify host factors required for HIV-1 replication (Brass et al. 2008).”
BackgroundA functional map of HIV-host interactions in primary human T cells
Hiatt, J. B., Hultquist, J. F., McGregor, M., Bouhaddou, M., Leenay, R. T., Simons, L. M., Young, J. M., Haas, P., Roth, T. L., Tobin, V. R., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-29346-w · Cited by 53
Protein-protein interactions of human viruses
Goodacre, N., Devkota, P., Bae, E. H., Wuchty, S., & Uetz, P. (2018) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2018.07.018 · Cited by 60
“compared their interaction data with four published RNAi screens [36, [39] [40] [41] that found a total of 1,071 human genes, of which only 55 overlapped with the 435 proteins found by AP/MS.”
Autophagy in Mycobacterium tuberculosis and HIV infections
Espert, L., Beaumelle, B. D., & Vergne, I. (2015) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2015.00049 · Cited by 53
“Indeed, while it becomes obvious that autophagy has an anti-HIV effect, a genome-wide RNAi screen has demonstrated that some ATG proteins are required for HIV1 replication (Brass et al., 2008).”
BackgroundFleta-Soriano, E., Martínez, J., Hinkelmann, B., Gerth, K., Washausen, P., Díez, J., Frank, R., Sasse, F., & Meyerhans, A. (2014) · Microbial Cell Factories · doi:10.1186/1475-2859-13-17 · Cited by 45
“Since the TZM-bl infection-assay is based on the luc if rase expression induced upon HIV infection [28], the calculated inhibitory values for th e test compounds could be biased.”
MethodHIV trafficking in host cells: motors wanted!
Gaudin, R., de Alencar, B. C., Arhel, N. J., & Benaroch, P. (2013) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.09.004 · Cited by 63
Navare, A., Sova, P., Purdy, D. E., Weiss, J. M., Wolf‐Yadlin, A., Korth, M. J., Chang, S. T., Proll, S. C., Jahan, T. A., Krasnoselsky, A. L., et al. (2012) · Virology · doi:10.1016/j.virol.2012.03.026 · Cited by 45
The Cargo-Binding Domain of Transportin 3 Is Required for Lentivirus Nuclear Import
Logue, E. C., Taylor, K. T., Goff, P., & Landau, N. (2011) · Journal of Virology · doi:10.1128/jvi.05384-11 · Cited by 45
“We found that the TNPO3 knockdown had a minor effect on MLV and FIV, an intermediate effect on HIV-1, and the largest effect on SIVmac239 and EIAV (Fig.”
BackgroundInfluentialGenotoxicity of retroviral hematopoietic stem cell gene therapy
Trobridge, G. D. (2011) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.2011.562496 · Cited by 45
“RNA interference screens have identified numerous other host cell proteins that affect viral replication [40,41].”
BackgroundMolecular aspects of cyclophilins mediating therapeutic actions of their ligands
Gałat, A., & Búa, J. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0437-0 · Cited by 44
“The whole-genome siRNA interference experiments have pinpointed numerous intracellular targets that are crucial for different stages of the HIV-1 live cycle such as uncoating of the HIV-1 virus, its intracellular transport and integration with the host DNA, transcription of its 15 genes, assembly of genetic material a…”
BackgroundWielens, J., Headey, S. J., Jeevarajah, D., Rhodes, D. I., Deadman, J. J., Chalmers, D. K., Scanlon, M. J., & Parker, M. W. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.03.016 · Cited by 42
“A variety of other cellular binding partners for IN have been identified, including transportin 3 (TNP03) [43], embryonic ectoderm development (EED) protein [44,45], SNF 5 [46–48] and the C-terminal domain of nucleoporin 153 [49].”
BackgroundSubramanya, S., Kim, S. S., Manjunath, N., & Shankar, P. (2010) · Expert Opinion on Biological Therapy · doi:10.1517/14712590903448158 · Cited by 47
“In addition to viral gene targets, many host molecules that play an important role in the HIV-1 life cycle [58] can be transiently perturbed to delay primary infection or curb viral dissemination or even reverse latency by use of antagonists to cellular microRNA that modulate HIV gene expression [132].”
BackgroundResultInfluentialCRISPR-Cas Targeting of Host Genes as an Antiviral Strategy
Chen, S., Yu, X., & Guo, D. (2018) · Viruses · doi:10.3390/v10010040 · Cited by 54
“Through electroporation of CRISPR/Cas9 ribonucleoproteins (RNPs) in primary CD4+ T cells, Hultquist et al. successfully knocked-out LEDGF or TNPO3, causing a tropism-independent reduction in HIV-1 infection [70].”
BackgroundHarmon, B., Bird, S. W., Schudel, B. R., Hatch, A. V., Rasley, A., & Negrete, O. A. (2016) · Journal of Virology · doi:10.1128/jvi.00543-16 · Cited by 44
SUN2 Overexpression Deforms Nuclear Shape and Inhibits HIV
Donahue, D. A., Amraoui, S., Nunzio, F. D., Kieffer, C., Porrot, F., Opp, S., Diaz‐Griffero, F., Casartelli, N., & Schwartz, O. (2016) · Journal of Virology · doi:10.1128/jvi.03202-15 · Cited by 51
Membrane dynamics associated with viral infection
de Armas‐Rillo, L., Valera, M., Marrero‐Hernández, S., & Valenzuela-Fernández, A. (2016) · Reviews in Medical Virology · doi:10.1002/rmv.1872 · Cited by 50
“Atg7, Atg8—LC3 is its best characterized mammalian homologue—Atg12 and Atg16L2—responsible for vesicle elongation) [63].”
BackgroundDeorphanizing the human transmembrane genome: A landscape of uncharacterized membrane proteins
Babcock, J. J., & Li, M. (2013) · Acta Pharmacologica Sinica · doi:10.1038/aps.2013.142 · Cited by 44
PROGRESS IN COMPUTATIONAL STUDIES OF HOST–PATHOGEN INTERACTIONS
Zhou, H., Jin, J., & Wong, L. (2012) · Journal of Bioinformatics and Computational Biology · doi:10.1142/s0219720012300018 · Cited by 46
COPI Is Required for Enterovirus 71 Replication
Wang, J., Wu, Z., & Jin, Q. (2012) · PLoS ONE · doi:10.1371/journal.pone.0038035 · Cited by 44
“Genome-wide RNA interference screening revealed that picorna-like virus, Drosophila C virus (DCV), also recruited COPI proteins to achieve viral replication [32].”
MethodMutations affecting interaction of integrase with TNPO3 do not prevent HIV-1 cDNA nuclear import
Cribier, A., Ségéral, E., Delelis, O., Parissi, V., Simon, A., Ruff, M., Bénarous, R., & Emiliani, S. (2011) · Retrovirology · doi:10.1186/1742-4690-8-104 · Cited by 48
“Using genome-wide RNAi knock down approaches, TNPO3 was recently identified as a HIV-dependency factor involved at a stage between reverse transcription and integration [53,55].”
Current progress in the development of RNAi-based therapeutics for HIV-1
Zhou, J.-H., & Rossi, J. J. (2011) · Gene Therapy · doi:10.1038/gt.2011.149 · Cited by 44
Cobos-Jiménez, V., Booiman, T., Hamann, J., & Kootstra, N. (2011) · Current Opinion in HIV and AIDS · doi:10.1097/coh.0b013e3283497203 · Cited by 44
Bol, S. M., Moerland, P., Limou, S., van Remmerden, Y., Coulonges, C., van Manen, D., Herbeck, J., Fellay, J., Síeberer, M., Sietzema, J. G., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017190 · Cited by 44
“Recently, a large number of host proteins that might be good targets for novel drugs to inhibit HIV-1 replication was identified”
BackgroundDinkins, C., Arko‐Mensah, J., & Deretic, V. P. (2010) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2010.04.004 · Cited by 46
Rato, S., Maia, S., Brito, P., Resende, L., Pereira, C. F., Moita, C. F., Freitas, R. P., Moniz-Pereira, J., Hacohen, N., Moita, L., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009276 · Cited by 44
“…relationships and possible function in the cell, we observed that the canonical pathways more represented in our screen (Figure S2B and Table S4) are also clearly represented in the previous studies [7–10], indicating a possible overlap of signal pathways instead of a direct overlap of genes.”
BackgroundMethodResultInfluentialIdentifying HIV-1 host cell factors by genome-scale RNAi screening.
Pache, L., König, R., & Chanda, S. (2011) · Methods · doi:10.1016/j.ymeth.2010.07.009 · Cited by 44
Börner, K., Hermle, J., Sommer, C., Brown, N. P., Knapp, B., Glass, B., Kunkel, J., Torralba, G., Reymann, J., Beil, N., et al. (2010) · Biotechnology Journal · doi:10.1002/biot.200900226 · Cited by 43
Zhuang, S., & Torbett, B. E. (2021) · Viruses · doi:10.3390/v13030417 · Cited by 53
Pak, A. J., Grime, J. M. A., Yu, A., & Voth, G. A. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b01413 · Cited by 50
Specific Inhibition of HIV Infection by the Action of Spironolactone in T Cells
Lacombe, B., Morel, M., Margottin-Goguet, F., & Ramirez, B. (2016) · Journal of Virology · doi:10.1128/jvi.01722-16 · Cited by 43
“However, with HIV LTR-encoding viruses, as in this study and in previous reports (23, 24), the results reflect the role of XPB in LTR-dependent viral gene expression and highlight a positive effect of XPB on the virus.”
BackgroundResultBulli, L., Apolonia, L., Kutzner, J., Pollpeter, D., Goujon, C., Herold, N., Schwarz, S.-M., Giernat, Y., Keppler, O. T., Malim, M. H., et al. (2016) · Journal of Virology · doi:10.1128/jvi.00458-16 · Cited by 46
An In Vivo RNAi Screening Approach to Identify Host Determinants of Virus Replication
Varble, A., Benitez, A. A., Schmid, S., Sachs, D. M., Shim, J. V., Barrueco, R. R., Panis, M., Crumiller, M., Silva, J. M., Sachidanandam, R., et al. (2013) · Cell Host & Microbe · doi:10.1016/j.chom.2013.08.007 · Cited by 40
“…of host factors that impact the replication capacity of influenza A virus (IAV), dengue virus, hepatitis C virus (HCV), West Nile virus (WNV), and human immunodeficiency virus (HIV) (Brass et al., 2008; König et al., 2008, 2010; Krishnan et al., 2008; Li et al., 2009; Sessions et al., 2009).”
BackgroundDetection of the HIV-1 Minus-Strand-Encoded Antisense Protein and Its Association with Autophagy
Torresilla, C., Larocque, É., Landry, S., Halin, M., Coulombe, Y., Masson, J., Mesnard, J.-M., & Barbeau, B. (2013) · Journal of Virology · doi:10.1128/jvi.00225-13 · Cited by 44
MicroSCALE Screening Reveals Genetic Modifiers of Therapeutic Response in Melanoma
Wood, K. C., Konieczkowski, D. J., Johannessen, C. M., Boehm, J. S., Tamayo, P., Botvinnik, O. B., Mesirov, J. P., Hahn, W. C., Root, D. E., Garraway, L. A., et al. (2012) · Science Signaling · doi:10.1126/scisignal.2002612 · Cited by 36
Reconstructing signaling pathways from RNAi data using probabilistic Boolean threshold networks
Kaderali, L., Dazert, E., Zeuge, U., Frese, M., & Bartenschlager, R. (2009) · Bioinform. · doi:10.1093/bioinformatics/btp375 · Cited by 43
“Readouts for large-scale RNAi screens are typically based on single reporters such as viability (Boutros et al., 2004) or staining of particular proteins (Brass et al., 2008).”
BackgroundChaudhary, P., Khan, S. Z., Rawat, P., Augustine, T., Raynes, D. A., Guerriero, V., & Mitra, D. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1151 · Cited by 41
The emerging role of long non-coding RNAs in HIV infection
Lazar, D. C., Morris, K. V., & Saayman, S. M. (2015) · Virus Research · doi:10.1016/j.virusres.2015.07.023 · Cited by 48
“Several seminal studies conducting genome-wide siRNA screens were conducted to identify HIV host dependency factors which are implicated in viral infection (Brass et al., 2008; Konig et al., 2008; Zhou et al., 2008).”
BackgroundThe dual role of tetraspanin CD63 in HIV-1 replication
Li, G., Endsley, M. A., Somasunderam, A., Gbota, S. L., Mbaka, M. I., Murray, J. L., & Ferguson, M. R. (2014) · Virology Journal · doi:10.1186/1743-422x-11-23 · Cited by 37
Critical role for the kinesin KIF3A in the HIV life cycle in primary human macrophages
Gaudin, R., de Alencar, B. C., Jouve, M. J., Berrè, S., Bouder, E. L., Schindler, M., Varthaman, A., Gobert, F.-X., & Benaroch, P. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201201144 · Cited by 58
“Two genome-wide RNAi screens have identified two kinesin chains, KIF3A and KIF3C, as host proteins involved in the HIV-1 cycle in cell lines (Brass et al., 2008; Zhou et al., 2008).”
BackgroundYamashita, M., & Emerman, M. (2009) · Journal of Virology · doi:10.1128/jvi.01084-09 · Cited by 42
A Critical Role for CD63 in HIV Replication and Infection of Macrophages and Cell Lines
Chen, H., Dziuba, N., Friedrich, B. M., von Lindern, J. J., Murray, J., Rojo, D. R., Hodge, T., O'Brien, W., & Ferguson, M. (2008) · Virology · doi:10.1016/j.virol.2008.06.029 · Cited by 42
“A recent large-scale siRNA screen revealed over 250 candidate host factors which may aid successive steps in the viral replication cycle (Brass et al., 2008).”
BackgroundMüller, B., & Kräusslich, H. (2009) · Handbook of Experimental Pharmacology · doi:10.1007/978-3-540-79086-0_1 · Cited by 42
“2005; Damm and Pelkmans 2006), and very recently a genome wide siRNA screen has identified potential cellular interaction partners of HIV (Brass et al. 2008).”
BackgroundAhammad, F., Rashid, T. R. T. A., Mohamed, M., Tanbin, S., & Fuad, F. A. A. (2019) · Microorganisms · doi:10.3390/microorganisms7090296 · Cited by 41
da Silveira, W. A., Palma, P. V. B., Sicchieri, R. D., Villacis, R. A. R., Mandarano, L. R. M., de Oliveira, T. M. G., Antônio, H. M. R., de Andrade, J. M., Muglia, V. F., Rogatto, S. R., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-02761-6 · Cited by 45
“Information about ZNF831 is scarce in the literature 35 .”
RNA interference in mammals: behind the screen
Campeau, E., & Gobeil, S. (2011) · Briefings in Functional Genomics · doi:10.1093/bfgp/elr018 · Cited by 40
Evaluation of specific delivery of chimeric phi29 pRNA/siRNAnanoparticles to multiple tumor cells
Li, L., Liu, J., Diao, Z., Shu, D., Guo, P., & Shen, G. (2009) · Molecular BioSystems · doi:10.1039/b903428e · Cited by 38
Factors that mold the nuclear landscape of HIV-1 integration
Bedwell, G. J., & Engelman, A. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa1207 · Cited by 42
Self-citationVpr and Its Cellular Interaction Partners: R We There Yet?
Fábryová, H., & Strebel, K. (2019) · Cells · doi:10.3390/cells8111310 · Cited by 46
Jiang, X., Wu, G., Zalloum, W. A., Meuser, M. E., Dick, A., Sun, L., Chen, C., Kang, D., Jing, L., Jia, R., et al. (2019) · RSC Advances · doi:10.1039/c9ra05869a · Cited by 59
Proteasomal Degradation Machinery: Favorite Target of HIV-1 Proteins
Lata, S., Mishra, R., & Banerjea, A. C. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.02738 · Cited by 58
Ramljak, I. C., Datler, J., Real-Hohn, A., Dreier, D., Wimmer, L., Redlberger‐Fritz, M., Fischl, W., Klingel, K., Mihovilovič, M. D., Blaas, D., et al. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1007203 · Cited by 46
RNA Interference Therapies for an HIV-1 Functional Cure
Scarborough, R. J., & Gatignol, A. (2017) · Viruses · doi:10.3390/v10010008 · Cited by 53
Evaluating the potential of IL-27 as a novel therapeutic agent in HIV-1 infection
Swaminathan, S., Dai, L., Lane, H. C., & Imamichi, T. (2013) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2013.07.001 · Cited by 33
Getting the whole picture: combining throughput with content in microscopy
Rimon, N., & Schuldiner, M. (2011) · Journal of Cell Science · doi:10.1242/jcs.087486 · Cited by 40
“The use of fluorescently tagged antibodies is the classic method for specifically labeling cellular components, and this technique is also widely used in HCS (Brass et al., 2008; Desbordes et al., 2008; Moffat et al., 2006; Prudencio et al., 2008).”
BackgroundMethodCellular targets for influenza drugs
Min, J.-Y., & Subbarao, K. (2010) · Nature Biotechnology · doi:10.1038/nbt0310-239 · Cited by 40
Global Approaches To Study Protein–Protein Interactions Among Viruses and Hosts
Mendez-Rios, J. D., & Uetz, P. (2010) · Future Microbiology · doi:10.2217/fmb.10.7 · Cited by 37
“Several recent studies have systematically investigated which human genes are required for HIV infection and replication [26,27].”
BackgroundAutophagy in Mammalian antiviral immunity.
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Genome-wide RNAi screening identifies host restriction factors critical for in vivo AAV transduction
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Discovery of Novel Small-Molecule Inhibitors of LIM Domain Kinase for Inhibiting HIV-1
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TRIM5α and Species Tropism of HIV/SIV
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The Base Excision Repair Pathway Is Required for Efficient Lentivirus Integration
Yoder, K. E., Espeseth, A. S., Wang, X.-H., Fang, Q., Russo, M. T., Lloyd, R. S., Hazuda, D. J., Sobol, R. W., & Fishel, R. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017862 · Cited by 45
“Several siRNA library screens have been performed to identify host factors necessary for HIV infection”
BackgroundInsights into Cellular Factors That Regulate HIV-1 Replication in Human Cells
Lever, A. M. L., & Jeang, K. (2011) · Biochemistry · doi:10.1021/bi101805f · Cited by 35
Nishitsuji, H., Hayashi, T., Takahashi, T., Miyano, M., Kannagi, M., & Masuda, T. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007825 · Cited by 38
“SIP1 was noticed as one of the host factors required for HIV-1 infection in the genome-wide screening analysis [46].”
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HIV immunology needs a new direction
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Metadata
- Authors
- Brass, A. L., Dykxhoorn, D. M., Benita, Y., Yan, N., Engelman, A., Xavier, R. J., Lieberman, J., & Elledge, S. J.
- Affiliations
- Brigham and Women's Hospital (US)
- ORCID
- Venue
- Science
- Published
- 2008-02-15
- Volume
- 319
- Issue
- 5865
- Pages
- 921-926
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2145848202
- Cited by
- 1,449
- References
- 0
- Citations by year
- 2026: 12 · 2025: 18 · 2024: 26 · 2023: 28 · 2022: 38 · 2021: 38 · 2020: 52 · 2019: 59 · 2018: 71 · 2017: 53 · 2016: 62 · 2015: 96 · 2014: 90 · 2013: 150 · 2012: 148
- FWCI
- 57.05
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institute of Allergy and Infectious Diseases (U19AI056900, AI052014, AI 062773, R01AI062773, R01AI052014, P30AI060354)
- National Institute of Diabetes and Digestive and Kidney Diseases (P30DK040561)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Virus-based gene therapy research
- Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
- Keywords
- HIV-1, host factors, host-virus interaction, Rab6, viral entry, karyopherins, TNPO3, viral integration, Mediator complex, MED28, viral transcription, antiviral drug targets
- MeSH terms
- Cytoskeletal Proteins, Humans, Proteins, Transcription, Genetic, Virus Replication, HIV-1, HIV Infections, Virus Integration, Computational Biology, rab GTP-Binding Proteins, Genomics, Karyopherins, Vesicular Transport Proteins, RNA Interference, RNA, Small Interfering, Cell Line, Tumor, Intracellular Signaling Peptides and Proteins, Virus Internalization, Human Immunodeficiency Virus Proteins, Host-Pathogen Interactions, Mediator Complex
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