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  4. A novel form of complete IL-12/IL-23 receptor beta1 deficiency with cell surface-expressed nonfunctional receptors
 
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Titre

A novel form of complete IL-12/IL-23 receptor beta1 deficiency with cell surface-expressed nonfunctional receptors

Type
article
Institution
Externe
Périodique
Blood  
Auteur(s)
Fieschi, C.
Auteure/Auteur
Bosticardo, M.
Auteure/Auteur
de Beaucoudrey, L.
Auteure/Auteur
Boisson-Dupuis, S.
Auteure/Auteur
Feinberg, J.
Auteure/Auteur
Santos, O. F.
Auteure/Auteur
Bustamante, J.
Auteure/Auteur
Levy, J.
Auteure/Auteur
Candotti, F.
Auteure/Auteur
Casanova, J. L.
Auteure/Auteur
Liens vers les personnes
Candotti, Fabio  
ISSN
0006-4971
Statut éditorial
Publié
Date de publication
2004
Volume
104
Numéro
7
Première page
2095
Dernière page/numéro d’article
101
Langue
anglais
Notes
Fieschi, Claire
Bosticardo, Marita
de Beaucoudrey, Ludovic
Boisson-Dupuis, Stephanie
Feinberg, Jacqueline
Santos, Orchidee Filipe
Bustamante, Jacinta
Levy, Jacov
Candotti, Fabio
Casanova, Jean-Laurent
eng
Case Reports
Research Support, Non-U.S. Gov't
Blood. 2004 Oct 1;104(7):2095-101. Epub 2004 Jun 3.
Résumé
Complete interleukin-12/interleukin-23 receptor beta1 (IL-12Rbeta1) deficiency is the most frequent known genetic etiology of the syndrome of Mendelian susceptibility to mycobacterial disease. The patients described to date lack IL-12Rbeta1 at the surface of their natural killer (NK) and T cells due to IL12RB1 mutations, which either interrupt the open reading frame or disrupt protein folding. We describe a patient with a large in-frame deletion of 12165 nucleotides (nt) in IL12RB1, encompassing exons 8 to 13 and resulting in the surface expression of nonfunctional IL-12Rbeta1. These 6 exons encode the proximal NH2-terminal half of the extracellular domain downstream from the cytokine-binding domain. Five of 6 monoclonal anti-IL-12Rbeta1 antibodies tested recognized the internally truncated chain on the cell surface. However, IL-12 and IL-23 did not bind normally to the patient's IL-12Rbeta1-containing respective heterodimeric receptors. As a result, signal transducer and activator of transcription-4 (STAT4) was not phosphorylated and interferon-gamma (IFN-gamma) production was not induced in the patient's cells upon stimulation with even high doses of IL-12 or IL-23. The functional defect was completely rescued by retrovirus-mediated IL-12Rbeta1 gene transfer. Thus, the detection of IL-12Rbeta1 on the cell surface does not exclude the possibility of complete IL-12Rbeta1 deficiency in patients with mycobacteriosis or salmonellosis. Paradoxically, the largest IL12RB1 mutation detected is associated with the cell surface expression of nonfunctional IL-12Rbeta1, defining a novel genetic form of IL-12Rbeta1 deficiency.
Sujets

Antibodies, Monoclona...

Cell Membrane/*metabo...

Cells, Cultured

Child

Cytokines/metabolism

DNA, Complementary/me...

DNA-Binding Proteins/...

Enzyme-Linked Immunos...

Exons

Flow Cytometry

Gene Deletion

Gene Transfer Techniq...

Humans

Interferon-gamma/meta...

Interleukin-12/metabo...

Interleukin-23

Interleukin-23 Subuni...

Interleukins/*metabol...

Killer Cells, Natural...

Male

Models, Genetic

Mutation

Open Reading Frames

Phenotype

Phosphorylation

Polymerase Chain Reac...

Protein Folding

Protein Structure, Te...

RNA/metabolism

Receptors, Interleuki...

Receptors, Interleuki...

Retroviridae/genetics...

STAT4 Transcription F...

Time Factors

Trans-Activators/meta...

PID Serval
serval:BIB_78BD5FBBC6CC
DOI
10.1182/blood-2004-02-0584
PMID
15178580
Permalien
https://iris.unil.ch/handle/iris/162693
Date de création
2017-11-01T09:29:21.966Z
Date de création dans IRIS
2025-05-20T23:28:00Z
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