Mutations in RNU7-1 Weaken Secondary RNA Structure, Induce MCP-1 and CXCL10 in CSF, and Result in Aicardi-Goutières Syndrome with Severe End-Organ Involvement.


Journal

Journal of clinical immunology
ISSN: 1573-2592
Titre abrégé: J Clin Immunol
Pays: Netherlands
ID NLM: 8102137

Informations de publication

Date de publication:
07 2022
Historique:
received: 06 10 2021
accepted: 07 01 2022
pubmed: 24 3 2022
medline: 27 8 2022
entrez: 23 3 2022
Statut: ppublish

Résumé

Aicardi-Goutières syndrome (AGS) is a type I interferonopathy usually characterized by early-onset neurologic regression. Biallelic mutations in LSM11 and RNU7-1, components of the U7 small nuclear ribonucleoprotein (snRNP) complex, have been identified in a limited number of genetically unexplained AGS cases. Impairment of U7 snRNP function results in misprocessing of replication-dependent histone (RDH) pre-mRNA and disturbance of histone occupancy of nuclear DNA, ultimately driving cGAS-dependent type I interferon (IFN-I) release. We performed a clinical, genetic, and immunological workup of 3 unrelated patients with uncharacterized AGS. Whole exome sequencing (WES) and targeted Sanger sequencing of RNU7-1 were performed. Primary fibroblasts were used for mechanistic studies. IFN-I signature and STAT1/2 phosphorylation were assessed in peripheral blood. Cytokines were profiled on serum and cerebrospinal fluid (CSF). Histopathology was examined on brain and kidney tissue. Sequencing revealed compound heterozygous RNU7-1 mutations, resulting in impaired RDH pre-mRNA processing. The 3' stem-loop mutations reduced stability of the secondary U7 snRNA structure. A discrete IFN-I signature in peripheral blood was paralleled by MCP-1 (CCL2) and CXCL10 upregulation in CSF. Histopathological analysis of the kidney showed thrombotic microangiopathy. We observed dysregulated STAT phosphorylation upon cytokine stimulation. Clinical overview of all reported patients with RNU7-1-related disease revealed high mortality and high incidence of organ involvement compared to other AGS genotypes. Targeted RNU7-1 sequencing is recommended in genetically unexplained AGS cases. CSF cytokine profiling represents an additional diagnostic tool to identify aberrant IFN-I signaling. Clinical follow-up of RNU7-1-mutated patients should include screening for severe end-organ involvement including liver disease and nephropathy.

Sections du résumé

BACKGROUND
Aicardi-Goutières syndrome (AGS) is a type I interferonopathy usually characterized by early-onset neurologic regression. Biallelic mutations in LSM11 and RNU7-1, components of the U7 small nuclear ribonucleoprotein (snRNP) complex, have been identified in a limited number of genetically unexplained AGS cases. Impairment of U7 snRNP function results in misprocessing of replication-dependent histone (RDH) pre-mRNA and disturbance of histone occupancy of nuclear DNA, ultimately driving cGAS-dependent type I interferon (IFN-I) release.
OBJECTIVE
We performed a clinical, genetic, and immunological workup of 3 unrelated patients with uncharacterized AGS.
METHODS
Whole exome sequencing (WES) and targeted Sanger sequencing of RNU7-1 were performed. Primary fibroblasts were used for mechanistic studies. IFN-I signature and STAT1/2 phosphorylation were assessed in peripheral blood. Cytokines were profiled on serum and cerebrospinal fluid (CSF). Histopathology was examined on brain and kidney tissue.
RESULTS
Sequencing revealed compound heterozygous RNU7-1 mutations, resulting in impaired RDH pre-mRNA processing. The 3' stem-loop mutations reduced stability of the secondary U7 snRNA structure. A discrete IFN-I signature in peripheral blood was paralleled by MCP-1 (CCL2) and CXCL10 upregulation in CSF. Histopathological analysis of the kidney showed thrombotic microangiopathy. We observed dysregulated STAT phosphorylation upon cytokine stimulation. Clinical overview of all reported patients with RNU7-1-related disease revealed high mortality and high incidence of organ involvement compared to other AGS genotypes.
CONCLUSIONS
Targeted RNU7-1 sequencing is recommended in genetically unexplained AGS cases. CSF cytokine profiling represents an additional diagnostic tool to identify aberrant IFN-I signaling. Clinical follow-up of RNU7-1-mutated patients should include screening for severe end-organ involvement including liver disease and nephropathy.

Identifiants

pubmed: 35320431
doi: 10.1007/s10875-022-01209-5
pii: 10.1007/s10875-022-01209-5
pmc: PMC9402729
doi:

Substances chimiques

CXCL10 protein, human 0
Chemokine CXCL10 0
Histones 0
Lsm11 protein, human 0
RNA Precursors 0
RNA, Small Nuclear 0
RNA-Binding Proteins 0
U7 small nuclear RNA 0
RNA 63231-63-0
Interferons 9008-11-1

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

962-974

Investigateurs

Steven Callens (S)
Bart Dermaut (B)
Wim Terryn (W)
Nika Schuermans (N)
Bruce Poppe (B)

Informations de copyright

© 2022. The Author(s).

Références

McNab F, Mayer-Barber K, Sher A, Wack A, O’Garra A. Type I interferons in infectious disease. Nat Rev Immunol. 2015;15:87–103.
doi: 10.1038/nri3787
Aicardi J, Goutières F. A progressive familial encephalopathy in infancy with calcifications of the basal ganglia and chronic cerebrospinal fluid lymphocytosis. Ann Neurol. 1984;15:49–54.
doi: 10.1002/ana.410150109
Livingston JH, Crow YJ. Neurologic phenotypes associated with mutations in TREX1, RNASEH2A, RNASEH2B, RNASEH2C, SAMHD1, ADAR1, and IFIH1: Aicardi-Goutières syndrome and beyond. Neuropediatrics. 2016;47:355–60.
doi: 10.1055/s-0036-1592307
Rice GI, Forte GM, Szynkiewicz M, et al. Assessment of interferon-related biomarkers in Aicardi-Goutières syndrome associated with mutations in TREX1, RNASEH2A, RNASEH2B, RNASEH2C, SAMHD1, and ADAR: a case-control study. Lancet Neurol. 2013;12:1159–69.
doi: 10.1016/S1474-4422(13)70258-8
La Piana R, Uggetti C, Roncarolo F, et al. Neuroradiologic patterns and novel imaging findings in Aicardi-Goutières syndrome. Neurology. 2016;86:28–35.
doi: 10.1212/WNL.0000000000002228
Crow YJ, Manel N. Aicardi-Goutières syndrome and the type I interferonopathies. Nat Rev Immunol. 2015;15:429–40.
doi: 10.1038/nri3850
Uggenti C, Lepelley A, Depp M, et al. cGAS-mediated induction of type I interferon due to inborn errors of histone pre-mRNA processing. Nat Genet. 2020;52:1364–72.
doi: 10.1038/s41588-020-00737-3
Vandeweyer G, Van Laer L, Loeys B, Van den Bulcke T, Kooy RF. VariantDB: a flexible annotation and filtering portal for next generation sequencing data. Genome Med. 2014;6:74.
doi: 10.1186/s13073-014-0074-6
Kolev NG, Steitz JA. In vivo assembly of functional U7 snRNP requires RNA backbone flexibility within the Sm-binding site. Nat Struct Mol Biol. 2006;13:347–53.
doi: 10.1038/nsmb1075
Gruber AR, Lorenz R, Bernhart SH, Neuböck R, Hofacker IL. The Vienna RNA websuite. Nucleic Acids Res. 2008;36:W70–4.
doi: 10.1093/nar/gkn188
Molnarfi N, Hyka-Nouspikel N, Gruaz L, Dayer JM, Burger D. The production of IL-1 receptor antagonist in IFN-beta-stimulated human monocytes depends on the activation of phosphatidylinositol 3-kinase but not of STAT1. J Immunol. 2005;174:2974–80.
doi: 10.4049/jimmunol.174.5.2974
Duncan CJA, Thompson BJ, Chen R, et al. Severe type I interferonopathy and unrestrained interferon signaling due to a homozygous germline mutation in STAT2. Sci Immunol. 2019;4.
Marzluff WF, Wagner EJ, Duronio RJ. Metabolism and regulation of canonical histone mRNAs: life without a poly(A) tail. Nat Rev Genet. 2008;9:843–54.
doi: 10.1038/nrg2438
Karczewski KJ, Francioli LC, Tiao G, et al. The mutational constraint spectrum quantified from variation in 141,456 humans. Nature. 2020;581:434–43.
doi: 10.1038/s41586-020-2308-7
Michalski S, de Oliveira Mann CC, Stafford CA, et al. Structural basis for sequestration and autoinhibition of cGAS by chromatin. Nature. 2020;587:678–82.
doi: 10.1038/s41586-020-2748-0
Volkman HE, Cambier S, Gray EE, Stetson DB. Tight nuclear tethering of cGAS is essential for preventing autoreactivity. Elife. 2019;8.
Du M, Chen ZJ. DNA-induced liquid phase condensation of cGAS activates innate immune signaling. Science. 2018;361:704–9.
doi: 10.1126/science.aat1022
de Oliveira Mann CC, Hopfner KP. Nuclear cGAS: guard or prisoner. EMBO J. 2021;40:e108293.
doi: 10.15252/embj.2021108293
Lodi L, Melki I, Bondet V, et al. Differential expression of interferon-alpha protein provides clues to tissue specificity across type I interferonopathies. J Clin Immunol. 2021;41:603–9.
doi: 10.1007/s10875-020-00952-x
van Heteren JT, Rozenberg F, Aronica E, Troost D, Lebon P, Kuijpers TW. Astrocytes produce interferon-alpha and CXCL10, but not IL-6 or CXCL8, in Aicardi-Goutières syndrome. Glia. 2008;56:568–78.
doi: 10.1002/glia.20639
Arimoto KI, Löchte S, Stoner SA, et al. STAT2 is an essential adaptor in USP18-mediated suppression of type I interferon signaling. Nat Struct Mol Biol. 2017;24:279–89.
doi: 10.1038/nsmb.3378
Duncan CJA, Hambleton S. Human disease phenotypes associated with loss and gain of function mutations in STAT2: viral susceptibility and type I interferonopathy. J Clin Immunol. 2021;41:1446–56.
doi: 10.1007/s10875-021-01118-z
Ho J, Pelzel C, Begitt A, et al. STAT2 is a pervasive cytokine regulator due to its inhibition of STAT1 in multiple signaling pathways. PLoS Biol. 2016;14:e2000117.
doi: 10.1371/journal.pbio.2000117
Löchte S, Waichman S, Beutel O, You C, Piehler J. Live cell micropatterning reveals the dynamics of signaling complexes at the plasma membrane. J Cell Biol. 2014;207:407–18.
doi: 10.1083/jcb.201406032
Crow YJ, Chase DS, Lowenstein Schmidt J, et al. Characterization of human disease phenotypes associated with mutations in TREX1, RNASEH2A, RNASEH2B, RNASEH2C, SAMHD1, ADAR, and IFIH1. Am J Med Genet A. 2015;167A:296–312.
doi: 10.1002/ajmg.a.36887
Skrajna A, Yang XC, Bucholc K, et al. U7 snRNP is recruited to histone pre-mRNA in a FLASH-dependent manner by two separate regions of the stem-loop binding protein. RNA. 2017;23:938–51.
doi: 10.1261/rna.060806.117

Auteurs

Leslie Naesens (L)

Department of Internal Medicine and Pediatrics, Ghent University, 9000, Ghent, Belgium.
Primary Immunodeficiency Research Lab, Jeffrey Modell Diagnosis and Research Center, Ghent University Hospital, 9000, Ghent, Belgium.

Josephine Nemegeer (J)

VIB-UGent Center for Inflammation Research, 9052, Ghent, Belgium.
Department of Biomedical Molecular Biology, Ghent University, 9052, Ghent, Belgium.

Filip Roelens (F)

Department of Pediatrics, Algemeen Ziekenhuis Delta, 8800, Roeselare, Belgium.

Lore Vallaeys (L)

Department of Pediatrics, Algemeen Ziekenhuis Groeninge, 8500, Kortrijk, Belgium.

Marije Meuwissen (M)

Department of Medical Genetics, University of Antwerp, 2000, Antwerp, Belgium.
Department of Medical Genetics, Antwerp University Hospital, 2650, Antwerp, Belgium.

Katrien Janssens (K)

Department of Medical Genetics, University of Antwerp, 2000, Antwerp, Belgium.
Department of Medical Genetics, Antwerp University Hospital, 2650, Antwerp, Belgium.

Patrick Verloo (P)

Department of Pediatrics, Division of Pediatric Neurology, University Hospital Ghent, 9000, Ghent, Belgium.

Benson Ogunjimi (B)

Department of Pediatrics, Antwerp University Hospital, 2650, Edegem, Belgium.
Centre for Health Economics Research & Modeling Infectious Diseases (CHERMID), Vaccine & Infectious Disease Institute (VAXINFECTIO), University of Antwerp, 2610, Antwerp, Belgium.

Dimitri Hemelsoet (D)

Department of Neurology, Ghent University Hospital, 9000, Ghent, Belgium.

Levi Hoste (L)

Department of Internal Medicine and Pediatrics, Ghent University, 9000, Ghent, Belgium.
Primary Immunodeficiency Research Lab, Jeffrey Modell Diagnosis and Research Center, Ghent University Hospital, 9000, Ghent, Belgium.

Lisa Roels (L)

Department of Internal Medicine and Pediatrics, Ghent University, 9000, Ghent, Belgium.
Primary Immunodeficiency Research Lab, Jeffrey Modell Diagnosis and Research Center, Ghent University Hospital, 9000, Ghent, Belgium.

Marieke De Bruyne (M)

Center for Medical Genetics, Ghent University Hospital, 9000, Ghent, Belgium.
Department of Biomolecular Medicine, Ghent University, 9000, Ghent, Belgium.

Elfride De Baere (E)

Center for Medical Genetics, Ghent University Hospital, 9000, Ghent, Belgium.
Department of Biomolecular Medicine, Ghent University, 9000, Ghent, Belgium.

Jo Van Dorpe (J)

Department of Pathology, Ghent University Hospital, 9000, Ghent, Belgium.

Amélie Dendooven (A)

Department of Pathology, Ghent University Hospital, 9000, Ghent, Belgium.
Department of Pathology, Antwerp University Hospital, 9000, Ghent, Belgium.

Anne Sieben (A)

Department of Neurology, Ghent University Hospital, 9000, Ghent, Belgium.
Department of Pathology, Antwerp University Hospital, 9000, Ghent, Belgium.

Gillian I Rice (GI)

Division of Evolution, Infection and Genomics, School of Biological Sciences, Faculty of Biology, Medicine and Health, The University of Manchester, Manchester, UK.

Tessa Kerre (T)

Department of Hematology, Jeffrey Modell Diagnosis and Research Center, Ghent University Hospital, 9000, Ghent, Belgium.

Rudi Beyaert (R)

Department of Biomedical Molecular Biology, Ghent University, 9052, Ghent, Belgium.
VIB-UGent Center for Inflammation Research, Laboratory of Molecular Signal Transduction in Inflammation, VIB, 9052, Ghent, Belgium.

Carolina Uggenti (C)

MRC Human Genetics Unit, Institute of Genetics and Cancer, The University of Edinburgh, Edinburgh, UK.

Yanick J Crow (YJ)

MRC Human Genetics Unit, Institute of Genetics and Cancer, The University of Edinburgh, Edinburgh, UK.
Laboratory of Neurogenetics and Neuroinflammation, University of Paris, Imagine Institute, Paris, France.

Simon J Tavernier (SJ)

Primary Immunodeficiency Research Lab, Jeffrey Modell Diagnosis and Research Center, Ghent University Hospital, 9000, Ghent, Belgium.
Department of Biomedical Molecular Biology, Ghent University, 9052, Ghent, Belgium.
Center for Medical Genetics, Ghent University Hospital, 9000, Ghent, Belgium.
VIB-UGent Center for Inflammation Research, Laboratory of Molecular Signal Transduction in Inflammation, VIB, 9052, Ghent, Belgium.

Jonathan Maelfait (J)

VIB-UGent Center for Inflammation Research, 9052, Ghent, Belgium.
Department of Biomedical Molecular Biology, Ghent University, 9052, Ghent, Belgium.

Filomeen Haerynck (F)

Department of Internal Medicine and Pediatrics, Ghent University, 9000, Ghent, Belgium. filomeen.haerynck@uzgent.be.
Primary Immunodeficiency Research Lab, Jeffrey Modell Diagnosis and Research Center, Ghent University Hospital, 9000, Ghent, Belgium. filomeen.haerynck@uzgent.be.
Department of Pediatric Pulmonology, Infectious Diseases and Immunology, Ghent University Hospital, Corneel Heymanslaan 10, Ghent, Belgium. filomeen.haerynck@uzgent.be.

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