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Pharmacological disruption of mSWI/SNF complex activity restricts SARS-CoV-2 infection
Bergwerk, M. et al. Covid-19 breakthrough infections in vaccinated health care workers. N. Engl. J. Med. 385, 1474–1484 (2021).
V’Kovski, P., Kratzel, A., Steiner, S., Stalder, H. & Thiel, V. Coronavirus biology and replication: implications for SARS-CoV-2. Nat. Rev. Microbiol. 19, 155–170 (2021).
Gandhi, S. et al. De novo emergence of a remdesivir resistance mutation during treatment of persistent SARS-CoV-2 infection in an immunocompromised patient: a case report. Nat. Commun. 13, 1547 (2022).
Heilmann, E. et al. SARS-CoV-2 3CLpro mutations selected in a VSV-based system confer resistance to nirmatrelvir, ensitrelvir, and GC376. Sci. Transl. Med. 15, eabq7360 (2023).
Hu, Y. et al. Naturally occurring mutations of SARS-CoV-2 main protease confer drug resistance to nirmatrelvir. Preprint at bioRxiv https://doi.org/10.1101/2022.06.28.497978 (2022).
Stevens, L. J. et al. Mutations in the SARS-CoV-2 RNA dependent RNA polymerase confer resistance to remdesivir by distinct mechanisms. Sci. Transl. Med. 14, eabo0718 (2022).
Zhou, Y. et al. Nirmatrelvir-resistant SARS-CoV-2 variants with high fitness in an infectious cell culture system. Sci. Adv. 8, eadd7197 (2022).
Zumla, A., Hui, D. S., Azhar, E. I., Memish, Z. A. & Maeurer, M. Reducing mortality from 2019-nCoV: host-directed therapies should be an option. Lancet 395, e35–e36 (2020).
Krause, P. R. et al. SARS-CoV-2 variants and vaccines. N. Engl. J. Med. 385, 179–186 (2021).
Meganck, R. M. & Baric, R. S. Developing therapeutic approaches for twenty-first-century emerging infectious viral diseases. Nat. Med. 27, 401–410 (2021).
Li, W. et al. Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. Nature 426, 450–454 (2003).
Hofmann, H. et al. Human coronavirus NL63 employs the severe acute respiratory syndrome coronavirus receptor for cellular entry. Proc. Natl Acad. Sci. USA 102, 7988–7993 (2005).
Raj, V. S. et al. Dipeptidyl peptidase 4 is a functional receptor for the emerging human coronavirus-EMC. Nature 495, 251–254 (2013).
Hoffmann, M. et al. SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor. Cell 181, 271–280 (2020).
Walls, A. C. et al. Structure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein. Cell 181, 281–292 (2020).
Yan, R. et al. Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2. Science 367, 1444–1448 (2020).
Zang, R. et al. TMPRSS2 and TMPRSS4 promote SARS-CoV-2 infection of human small intestinal enterocytes. Sci. Immunol. 5, eabc3582 (2020).
Hoffmann, M., Kleine-Weber, H. & Pöhlmann, S. A multibasic cleavage site in the spike protein of SARS-CoV-2 is essential for infection of human lung cells. Mol. Cell 78, 779–784 (2020).
Snijder, E. J. et al. Unique and conserved features of genome and proteome of SARS-coronavirus, an early split-off from the coronavirus group 2 lineage. J. Mol. Biol. 331, 991–1004 (2003).
Stertz, S. et al. The intracellular sites of early replication and budding of SARS-coronavirus. Virology 361, 304–315 (2007).
Knoops, K. et al. SARS-coronavirus replication is supported by a reticulovesicular network of modified endoplasmic reticulum. PLoS Biol. 6, e226 (2008).
Wei, J. et al. Genome-wide CRISPR screens reveal host factors critical for SARS-CoV-2 infection. Cell 184, 76–91 (2021).
Rebendenne, A. et al. Bidirectional genome-wide CRISPR screens reveal host factors regulating SARS-CoV-2, MERS-CoV and seasonal HCoVs. Nat. Genet. 54, 1090–1102 (2022).
Daniloski, Z. et al. Identification of required host factors for SARS-CoV-2 infection in human cells. Cell 184, 92–105 (2021).
Schneider, W. M. et al. Genome-scale identification of SARS-CoV-2 and pan-coronavirus host factor networks. Cell 184, 120–132 (2021).
Kadoch, C. & Crabtree, G. R. Mammalian SWI/SNF chromatin remodeling complexes and cancer: mechanistic insights gained from human genomics. Sci. Adv. 1, e1500447 (2015).
Kadoch, C. et al. Proteomic and bioinformatic analysis of mammalian SWI/SNF complexes identifies extensive roles in human malignancy. Nat. Genet. 45, 592–601 (2013).
Clapier, C. R. & Cairns, B. R. The biology of chromatin remodeling complexes. Annu. Rev. Biochem. 78, 273–304 (2009).
Mashtalir, N. et al. Modular organization and assembly of SWI/SNF family chromatin remodeling complexes. Cell 175, 1272–1288 (2018).
Michel, B. C. et al. A non-canonical SWI/SNF complex is a synthetic lethal target in cancers driven by BAF complex perturbation. Nat. Cell Biol. 20, 1410–1420 (2018).
Mashtalir, N. et al. Chromatin landscape signals differentially dictate the activities of mSWI/SNF family complexes. Science 373, 306–315 (2021).
Khavari, P. A., Peterson, C. L., Tamkun, J. W., Mendel, D. B. & Crabtree, G. R. BRG1 contains a conserved domain of the SWI2/SNF2 family necessary for normal mitotic growth and transcription. Nature 366, 170–174 (1993).
Mashtalir, N. et al. A structural model of the endogenous human BAF complex informs disease mechanisms. Cell 183, 802–817 (2020).
Pan, J. et al. The ATPase module of mammalian SWI/SNF family complexes mediates subcomplex identity and catalytic activity-independent genomic targeting. Nat. Genet. 51, 618–626 (2019).
Valencia, A. M. et al. Recurrent SMARCB1 mutations reveal a nucleosome acidic patch interaction site that potentiates mSWI/SNF complex chromatin remodeling. Cell 179, 1342–1356 (2019).
Nakayama, R. T. et al. SMARCB1 is required for widespread BAF complex-mediated activation of enhancers and bivalent promoters. Nat. Genet. 49, 1613–1623 (2017).
Kelso, T. W. R. et al. Chromatin accessibility underlies synthetic lethality of SWI/SNF subunits in ARID1A-mutant cancers. eLife 6, e30506 (2017).
Wang, X. et al. SMARCB1-mediated SWI/SNF complex function is essential for enhancer regulation. Nat. Genet. 49, 289–295 (2017).
Valencia, A. M. & Kadoch, C. Chromatin regulatory mechanisms and therapeutic opportunities in cancer. Nat. Cell Biol. 21, 152–161 (2019).
Versteege, I. et al. Truncating mutations of hSNF5/INI1 in aggressive paediatric cancer. Nature 394, 203–206 (1998).
Santen, G. W. E., Kriek, M. & van Attikum, H. SWI/SNF complex in disorder: SWItching from malignancies to intellectual disability. Epigenetics 7, 1219–1224 (2012).
Pan, J. et al. Interrogation of mammalian protein complex structure, function, and membership using genome-scale fitness screens. Cell Syst. 6, 555–568 (2018).
Xie, X. et al. An infectious cDNA clone of SARS-CoV-2. Cell Host Microbe 27, 841–848 (2020).
Bultman, S. J., Gebuhr, T. C. & Magnuson, T. A Brg1 mutation that uncouples ATPase activity from chromatin remodeling reveals an essential role for SWI/SNF-related complexes in β-globin expression and erythroid development. Genes Dev. 19, 2849–2861 (2005).
Hodges, H. C. et al. Dominant-negative SMARCA4 mutants alter the accessibility landscape of tissue-unrestricted enhancers. Nat. Struct. Mol. Biol. 25, 61–72 (2018).
Bultman, S. et al. A Brg1 null mutation in the mouse reveals functional differences among mammalian SWI/SNF complexes. Mol. Cell 6, 1287–1295 (2000).
Hota, S. K. & Bruneau, B. G. ATP-dependent chromatin remodeling during mammalian development. Development 143, 2882–2897 (2016).
Santen, G. W. E. et al. Coffin–Siris syndrome and the BAF complex: genotype–phenotype study in 63 patients. Hum. Mutat. 34, 1519–1528 (2013).
Kaya-Okur, H. S. et al. CUT&Tag for efficient epigenomic profiling of small samples and single cells. Nat. Commun. 10, 1930 (2019).
Corces, M. R. et al. An improved ATAC–seq protocol reduces background and enables interrogation of frozen tissues. Nat. Methods 14, 959–962 (2017).
Buenrostro, J. D., Giresi, P. G., Zaba, L. C., Chang, H. Y. & Greenleaf, W. J. Transposition of native chromatin for fast and sensitive epigenomic profiling of open chromatin, DNA-binding proteins and nucleosome position. Nat. Methods 10, 1213–1218 (2013).
Tomei, L., Cortese, R. & De Francesco, R. A POU-A related region dictates DNA binding specificity of LFB1/HNF1 by orienting the two XL-homeodomains in the dimer. EMBO J. 11, 4119–4129 (1992).
Mendel, D. B. et al. Characterization of a cofactor that regulates dimerization of a mammalian homeodomain protein. Science 254, 1762–1767 (1991).
Mendel, D. B., Hansen, L. P., Graves, M. K., Conley, P. B. & Crabtree, G. R. HNF-1α and HNF-1β (vHNF-1) share dimerization and homeo domains, but not activation domains, and form heterodimers in vitro. Genes Dev. 5, 1042–1056 (1991).
Papillon, J. P. N. et al. Discovery of orally active inhibitors of Brahma homolog (BRM)/SMARCA2 ATPase activity for the treatment of Brahma related gene 1 (BRG1)/SMARCA4-mutant cancers. J. Med. Chem. 61, 10155–10172 (2018).
Farnaby, W. et al. BAF complex vulnerabilities in cancer demonstrated via structure-based PROTAC design. Nat. Chem. Biol. 15, 672–680 (2019).
Remillard, D. et al. Degradation of the BAF complex factor BRD9 by heterobifunctional ligands. Angew. Chem. Int. Ed. Engl. 56, 5738–5743 (2017).
Schauer, R. Sialic acids as regulators of molecular and cellular interactions. Curr. Opin. Struct. Biol. 19, 507–514 (2009).
Gottschalk, A. On the mechanism underlying initiation of influenza virus infection. Ergeb. Mikrobiol. Immunitatsforsch Exp. Ther. 32, 1–22 (1959).
Zhou, J. et al. Infection of bat and human intestinal organoids by SARS-CoV-2. Nat. Med. 26, 1077–1083 (2020).
Wilen, C. B. et al. Tropism for tuft cells determines immune promotion of norovirus pathogenesis. Science 360, 204–208 (2018).
Orchard, R. C. et al. Discovery of a proteinaceous cellular receptor for a norovirus. Science 353, 933–936 (2016).
Marsh, M. & Helenius, A. Virus entry: open sesame. Cell 124, 729–740 (2006).
Grove, J. & Marsh, M. The cell biology of receptor-mediated virus entry. J. Cell Biol. 195, 1071–1082 (2011).
Chow, R. D., Majety, M. & Chen, S. The aging transcriptome and cellular landscape of the human lung in relation to SARS-CoV-2. Nat. Commun. 12, 4 (2021).
Almeida-da-Silva, C. L. C., Matshik Dakafay, H. & Liu, K. Cigarette smoke stimulates SARS-CoV-2 internalization by activating AhR and increasing ACE2 expression in human gingival epithelial cells. Int. J. Mol. Sci. 22, 7669 (2021).
Onabajo, O. O. et al. Interferons and viruses induce a novel truncated ACE2 isoform and not the full-length SARS-CoV-2 receptor. Nat. Genet. 52, 1283–1293 (2020).
Lee, H. K., Jung, O. & Hennighausen, L. JAK inhibitors dampen activation of interferon-stimulated transcription of ACE2 isoforms in human airway epithelial cells. Commun. Biol. 4, 654 (2021).
Jankowski, J., Lee, H. K., Wilflingseder, J. & Hennighausen, L. JAK inhibitors dampen activation of interferon-activated transcriptomes and the SARS-CoV-2 receptor ACE2 in human renal proximal tubules. iScience 24, 102928 (2021).
Curfman, G. Renin-angiotensin-aldosterone inhibitors and susceptibility to and severity of COVID-19. JAMA 324, 177–178 (2020).
Mancia, G., Rea, F., Ludergnani, M., Apolone, G. & Corrao, G. Renin–angiotensin–aldosterone system blockers and the risk of Covid-19. N. Engl. J. Med. 382, 2431–2440 (2020).
Reynolds, H. R. et al. Renin–angiotensin–aldosterone system inhibitors and risk of Covid-19. N. Engl. J. Med. 382, 2441–2448 (2020).
Wysocki, J., Lores, E., Ye, M., Soler, M. J. & Batlle, D. Kidney and lung ACE2 expression after an ACE inhibitor or an Ang II receptor blocker: implications for COVID-19. J. Am. Soc. Nephrol. 31, 1941–1943 (2020).
Baggen, J. et al. Genome-wide CRISPR screening identifies TMEM106B as a proviral host factor for SARS-CoV-2. Nat. Genet. 53, 435–444 (2021).
Biering, S. B. et al. Genome-wide bidirectional CRISPR screens identify mucins as host factors modulating SARS-CoV-2 infection. Nat. Genet. 54, 1078–1089 (2022).
Wang, R. et al. Genetic screens identify host factors for SARS-CoV-2 and common cold coronaviruses. Cell 184, 106–119 (2021).
Zhu, Y. et al. A genome-wide CRISPR screen identifies host factors that regulate SARS-CoV-2 entry. Nat. Commun. 12, 961 (2021).
Harries, L. W., Brown, J. E. & Gloyn, A. L. Species-specific differences in the expression of the HNF1A, HNF1B and HNF4A genes. PLoS ONE 4, e7855 (2009).
Ledford, H. Coronavirus breakthrough: dexamethasone is first drug shown to save lives. Nature 582, 469 (2020).
Ho, J. S. Y. et al. TOP1 inhibition therapy protects against SARS-CoV-2-induced lethal inflammation. Cell 184, 2618–2632(2021).
Zhou, H. et al. Identification of novel bat coronaviruses sheds light on the evolutionary origins of SARS-CoV-2 and related viruses. Cell 184, 4380–4391 (2021).
Ge, X.-Y. et al. Isolation and characterization of a bat SARS-like coronavirus that uses the ACE2 receptor. Nature 503, 535–538 (2013).
Li, H. et al. Human–animal interactions and bat coronavirus spillover potential among rural residents in Southern China. Biosaf. Health 1, 84–90 (2019).
Menachery, V. D. et al. SARS-like WIV1-CoV poised for human emergence. Proc. Natl Acad. Sci. USA 113, 3048–3053 (2016).
Wang, N. et al. Serological evidence of bat SARS-related coronavirus infection in humans, China. Virol. Sin. 33, 104–107 (2018).
Ravindra, N. G. et al. Single-cell longitudinal analysis of SARS-CoV-2 infection in human airway epithelium identifies target cells, alterations in gene expression, and cell state changes. PLoS Biol. 19, e3001143 (2021).
Ettayebi, K. et al. Replication of human noroviruses in stem cell-derived human enteroids. Science 353, 1387–1393 (2016).
Co, J. Y. et al. Controlling epithelial polarity: a human enteroid model for host–pathogen interactions. Cell Rep. 26, 2509–2520 (2019).
Riva, L. et al. Discovery of SARS-CoV-2 antiviral drugs through large-scale compound repurposing. Nature 586, 113–119 (2020).
Pérez-Then, E. et al. Neutralizing antibodies against the SARS-CoV-2 Delta and Omicron variants following heterologous CoronaVac plus BNT162b2 booster vaccination. Nat. Med. 28, 481–485 (2022).
Avanzato, V. A. et al. A structural basis for antibody-mediated neutralization of Nipah virus reveals a site of vulnerability at the fusion glycoprotein apex. Proc. Natl Acad. Sci. USA 116, 25057–25067 (2019).
Buenrostro, J. D., Wu, B., Chang, H. Y. & Greenleaf, W. J. ATAC–seq: a method for assaying chromatin accessibility genome-wide. Curr. Protoc. Mol. Biol. 109, 21.29.1–21.29.9 (2015).
Dobin, A. et al. STAR: ultrafast universal RNA-seq aligner. Bioinformatics 29, 15–21 (2013).
Ramírez, F. et al. deepTools2: a next generation web server for deep-sequencing data analysis. Nucleic Acids Res. 44, W160–W165 (2016).
Robinson, M. D., McCarthy, D. J. & Smyth, G. K. edgeR: a Bioconductor package for differential expression analysis of digital gene expression data. Bioinformatics 26, 139–140 (2010).
Bolger, A. M., Lohse, M. & Usadel, B. Trimmomatic: a flexible trimmer for Illumina sequence data. Bioinformatics 30, 2114–2120 (2014).
Langmead, B. & Salzberg, S. L. Fast gapped-read alignment with Bowtie 2. Nat. Methods 9, 357–359 (2012).
Li, H. et al. The Sequence Alignment/Map format and SAMtools. Bioinformatics 25, 2078–2079 (2009).
Zhang, Y. et al. Model-based analysis of ChIP–Seq (MACS). Genome Biol. 9, R137 (2008).
Kuhn, R. M., Haussler, D. & Kent, W. J. The UCSC genome browser and associated tools. Brief. Bioinformatics 14, 144–161 (2013).
Zhu, Q., Liu, N., Orkin, S. H. & Yuan, G.-C. CUT&RUNTools: a flexible pipeline for CUT&RUN processing and footprint analysis. Genome Biol. 20, 192 (2019).
Shen, L., Shao, N., Liu, X. & Nestler, E. ngs.plot: quick mining and visualization of next-generation sequencing data by integrating genomic databases. BMC Genomics 15, 284 (2014).
Quinlan, A. R. & Hall, I. M. BEDTools: a flexible suite of utilities for comparing genomic features. Bioinformatics 26, 841–842 (2010).
Schäfer, J. & Strimmer, K. A shrinkage approach to large-scale covariance matrix estimation and implications for functional genomics. Stat. Appl. Genet. Mol. Biol. https://doi.org/10.2202/1544-6115.1175 (2005).
Opgen-Rhein, R. & Strimmer, K. Accurate ranking of differentially expressed genes by a distribution-free shrinkage approach. Stat. Appl. Genet. Mol. Biol. https://doi.org/10.2202/1544-6115.1252 (2007).
Grant, C. E., Bailey, T. L. & Noble, W. S. FIMO: scanning for occurrences of a given motif. Bioinformatics 27, 1017–1018 (2011).
Grossman, S. R. et al. Positional specificity of different transcription factor classes within enhancers. Proc. Natl Acad. Sci. USA 115, E7222–E7230 (2018).
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