FHL1 is a major host factor for chikungunya virus infection.
Animals
Cells, Cultured
Chikungunya Fever
/ drug therapy
Chikungunya virus
/ drug effects
Female
Fibroblasts
/ virology
HEK293 Cells
Host-Derived Cellular Factors
/ genetics
Host-Pathogen Interactions
Humans
Intracellular Signaling Peptides and Proteins
/ deficiency
LIM Domain Proteins
/ deficiency
Male
Mice
Muscle Proteins
/ deficiency
Myoblasts
/ virology
O'nyong-nyong Virus
/ growth & development
Protein Binding
RNA, Viral
/ biosynthesis
Viral Nonstructural Proteins
/ genetics
Virus Replication
Journal
Nature
ISSN: 1476-4687
Titre abrégé: Nature
Pays: England
ID NLM: 0410462
Informations de publication
Date de publication:
10 2019
10 2019
Historique:
received:
19
02
2019
accepted:
19
08
2019
pubmed:
27
9
2019
medline:
30
11
2019
entrez:
27
9
2019
Statut:
ppublish
Résumé
Chikungunya virus (CHIKV) is a re-emerging alphavirus that is transmitted to humans by mosquito bites and causes musculoskeletal and joint pain
Identifiants
pubmed: 31554973
doi: 10.1038/s41586-019-1578-4
pii: 10.1038/s41586-019-1578-4
doi:
Substances chimiques
FHL1 protein, human
0
Host-Derived Cellular Factors
0
Intracellular Signaling Peptides and Proteins
0
LIM Domain Proteins
0
Muscle Proteins
0
RNA, Viral
0
Viral Nonstructural Proteins
0
nsp3 protein, alphavirus
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
259-263Références
Burt, F. J. et al. Chikungunya virus: an update on the biology and pathogenesis of this emerging pathogen. Lancet Infect. Dis. 17, e107–e117 (2017).
doi: 10.1016/S1473-3099(16)30385-1
Silva, L. A. & Dermody, T. S. Chikungunya virus: epidemiology, replication, disease mechanisms, and prospective intervention strategies. J. Clin. Invest. 127, 737–749 (2017).
doi: 10.1172/JCI84417
Greene, W. K., Baker, E., Rabbitts, T. H. & Kees, U. R. Genomic structure, tissue expression and chromosomal location of the LIM-only gene, SLIM1. Gene 232, 203–207 (1999).
doi: 10.1016/S0378-1119(99)00125-0
Schessl, J., Feldkirchner, S., Kubny, C. & Schoser, B. Reducing body myopathy and other FHL1-related muscular disorders. Semin. Pediatr. Neurol. 18, 257–263 (2011).
doi: 10.1016/j.spen.2011.10.007
Gueneau, L. et al. Mutations of the FHL1 gene cause Emery–Dreifuss muscular dystrophy. Am. J. Hum. Genet. 85, 338–353 (2009).
doi: 10.1016/j.ajhg.2009.07.015
Ooi, Y. S., Stiles, K. M., Liu, C. Y., Taylor, G. M. & Kielian, M. Genome-wide RNAi screen identifies novel host proteins required for alphavirus entry. PLoS Pathog. 9, e1003835 (2013).
doi: 10.1371/journal.ppat.1003835
Karlas, A. et al. A human genome-wide loss-of-function screen identifies effective chikungunya antiviral drugs. Nat. Commun. 7, 11320 (2016).
doi: 10.1038/ncomms11320
Zhang, R. et al. Mxra8 is a receptor for multiple arthritogenic alphaviruses. Nature 557, 570–574 (2018).
doi: 10.1038/s41586-018-0121-3
Tanaka, A. et al. Genome-wide screening uncovers the significance of N-sulfation of heparan sulfate as a host cell factor for chikungunya virus infection. J. Virol. 91, 1–22 (2017).
doi: 10.1128/JVI.00432-17
Schuffenecker, I. et al. Genome microevolution of chikungunya viruses causing the Indian Ocean outbreak. PLoS Med. 3, e263 (2006).
doi: 10.1371/journal.pmed.0030263
Shathasivam, T., Kislinger, T. & Gramolini, A. O. Genes, proteins and complexes: the multifaceted nature of FHL family proteins in diverse tissues. J. Cell. Mol. Med. 14, 2702–2720 (2010).
doi: 10.1111/j.1582-4934.2010.01176.x
Brown, S. et al. Characterization of two isoforms of the skeletal muscle LIM protein 1, SLIM1. Localization of SLIM1 at focal adhesions and the isoform slimmer in the nucleus of myoblasts and cytoplasm of myotubes suggests distinct roles in the cytoskeleton and in nuclear–cytoplasmic communication. J. Biol. Chem. 274, 27083–27091 (1999).
doi: 10.1074/jbc.274.38.27083
Krempler, A., Kollers, S., Fries, R. & Brenig, B. Isolation and characterization of a new FHL1 variant (FHL1C) from porcine skeletal muscle. Cytogenet. Cell Genet. 90, 106–114 (2000).
doi: 10.1159/000015643
Pen, A. E. et al. A novel single nucleotide splice site mutation in FHL1 confirms an Emery–Dreifuss plus phenotype with pulmonary artery hypoplasia and facial dysmorphology. Eur. J. Med. Genet. 58, 222–229 (2015).
doi: 10.1016/j.ejmg.2015.02.003
Chan, K. K. et al. Molecular cloning and characterization of FHL2, a novel LIM domain protein preferentially expressed in human heart. Gene 210, 345–350 (1998).
doi: 10.1016/S0378-1119(97)00644-6
Couderc, T. et al. A mouse model for chikungunya: young age and inefficient type-I interferon signaling are risk factors for severe disease. PLoS Pathog. 4, e29 (2008).
doi: 10.1371/journal.ppat.0040029
Roberts, G. C. et al. Evaluation of a range of mammalian and mosquito cell lines for use in Chikungunya virus research. Sci. Rep. 7, 14641 (2017).
doi: 10.1038/s41598-017-15269-w
Kim, D. Y. et al. New World and Old World Alphaviruses have evolved to exploit different components of stress granules, FXR and G3BP proteins, for assembly of viral replication complexes. PLoS Pathog. 12, e1005810 (2016).
doi: 10.1371/journal.ppat.1005810
Jose, J., Taylor, A. B. & Kuhn, R. J. Spatial and temporal analysis of alphavirus replication and assembly in mammalian and mosquito cells. mBio 8, e02294-16 (2017).
doi: 10.1128/mBio.02294-16
Götte, B., Liu, L. & McInerney, G. M. The enigmatic alphavirus non-structural protein 3 (nsP3) revealing its secrets at last. Viruses 10, 105 (2018).
doi: 10.3390/v10030105
Meshram, C. D. et al. Multiple host factors interact with the hypervariable domain of chikungunya virus nsP3 and determine viral replication in cell-specific mode. J. Virol. 92, e00838-18 (2018).
doi: 10.1128/JVI.00838-18
Mutso, M. et al. Mutation of CD2AP and SH3KBP1 binding motif in alphavirus nsP3 hypervariable domain results in attenuated virus. Viruses 10, 226 (2018).
doi: 10.3390/v10050226
Scholte, F. E. M. et al. Stress granule components G3BP1 and G3BP2 play a proviral role early in chikungunya virus replication. J. Virol. 89, 4457–4469 (2015).
doi: 10.1128/JVI.03612-14
Schessl, J. et al. Proteomic identification of FHL1 as the protein mutated in human reducing body myopathy. J. Clin. Invest. 118, 904–912 (2008).
pubmed: 18274675
pmcid: 2242623
Bonne, G., Leturcq, F. & Ben Yaou, R. in GeneReviews (eds Adam, M. P. et al.) (University of Washington, 1993).
Medina, F. et al. Dengue virus: isolation, propagation, quantification, and storage. Curr. Protoc. Microbiol. 15, 15D.2.1–15D.2.24 (2012).
doi: 10.1002/9780471729259.mc15d02s27
Meertens, L. et al. The TIM and TAM families of phosphatidylserine receptors mediate dengue virus entry. Cell Host Microbe 12, 544–557 (2012).
doi: 10.1016/j.chom.2012.08.009
Shalem, O. et al. Genome-scale CRISPR–Cas9 knockout screening in human cells. Science 343, 84–87 (2014).
doi: 10.1126/science.1247005
Li, W. et al. MAGeCK enables robust identification of essential genes from genome-scale CRISPR/Cas9 knockout screens. Genome Biol. 15, 554 (2014).
doi: 10.1186/s13059-014-0554-4
Joung, J. et al. Genome-scale CRISPR–Cas9 knockout and transcriptional activation screening. Nat. Protoc. 12, 828–863 (2017).
doi: 10.1038/nprot.2017.016
Pellet, J. et al. ViralORFeome: an integrated database to generate a versatile collection of viral ORFs. Nucleic Acids Res. 38, D371–D378 (2010).
doi: 10.1093/nar/gkp1000
Gläsker, S. et al. Virus replicon particle based chikungunya virus neutralization assay using Gaussia luciferase as readout. Virol. J. 10, 235 (2013).
doi: 10.1186/1743-422X-10-235
Kümmerer, B. M., Grywna, K., Gläsker, S., Wieseler, J. & Drosten, C. Construction of an infectious chikungunya virus cDNA clone and stable insertion of mCherry reporter genes at two different sites. J. Gen. Virol. 93, 1991–1995 (2012).
doi: 10.1099/vir.0.043752-0
Plaskon, N. E., Adelman, Z. N. & Myles, K. M. Accurate strand-specific quantification of viral RNA. PLoS ONE 4, e7468 (2009).
doi: 10.1371/journal.pone.0007468
Domenighetti, A. A. et al. Loss of FHL1 induces an age-dependent skeletal muscle myopathy associated with myofibrillar and intermyofibrillar disorganization in mice. Hum. Mol. Genet. 23, 209–225 (2014).
doi: 10.1093/hmg/ddt412