Literature DB >> 24698316

Hypomorphic homozygous mutations in phosphoglucomutase 3 (PGM3) impair immunity and increase serum IgE levels.

Atfa Sassi1, Sandra Lazaroski2, Gang Wu3, Stuart M Haslam3, Manfred Fliegauf2, Fethi Mellouli4, Turkan Patiroglu5, Ekrem Unal6, Mehmet Akif Ozdemir6, Zineb Jouhadi7, Khadija Khadir7, Leila Ben-Khemis1, Meriem Ben-Ali1, Imen Ben-Mustapha1, Lamia Borchani8, Dietmar Pfeifer9, Thilo Jakob10, Monia Khemiri11, A Charlotta Asplund12, Manuela O Gustafsson12, Karin E Lundin12, Elin Falk-Sörqvist13, Lotte N Moens13, Hatice Eke Gungor14, Karin R Engelhardt15, Magdalena Dziadzio15, Hans Stauss15, Bernhard Fleckenstein16, Rebecca Meier2, Khairunnadiya Prayitno2, Andrea Maul-Pavicic2, Sandra Schaffer2, Mirzokhid Rakhmanov2, Philipp Henneke2, Helene Kraus2, Hermann Eibel2, Uwe Kölsch17, Sellama Nadifi18, Mats Nilsson13, Mohamed Bejaoui4, Alejandro A Schäffer19, C I Edvard Smith12, Anne Dell3, Mohamed-Ridha Barbouche1, Bodo Grimbacher20.   

Abstract

n class="abstract_title">BACKGROUND: Recurrent bacterial and fungal infections, eczema, and increased serum IgE levels characterize patients with the hyper-IgE syndrome (HIES). Known genetic causes for HIES are mutations in signal transducer and activator of transcription 3 (STAT3) and dedicator of cytokinesis 8 (DOCK8), which are involved in signal transduction pathways. However, glycosylation defects have not been described in patients with HIES. One crucial enzyme in the glycosylation pathway is phosphoglucomutase 3 (PGM3), which catalyzes a key step in the synthesis of uridine diphosphate N-acetylglucosamine, which is required for the biosynthesis of N-glycans.
OBJECTIVE: We sought to elucidate the genetic cause in patients with HIES who do not carry mutations in STAT3 or DOCK8.
METHODS: After establishing a linkage interval by means of SNPchip genotyping and homozygosity mapping in 2 families with HIES from Tunisia, mutational analysis was performed with selector-based, high-throughput sequencing. Protein expression was analyzed by means of Western blotting, and glycosylation was profiled by using mass spectrometry.
RESULTS: Mutational analysis of candidate genes in an 11.9-Mb linkage region on chromosome 6 shared by 2 multiplex families identified 2 homozygous mutations in PGM3 that segregated with disease status and followed recessive inheritance. The mutations predict amino acid changes in PGM3 (p.Glu340del and p.Leu83Ser). A third homozygous mutation (p.Asp502Tyr) and the p.Leu83Ser variant were identified in 2 other affected families, respectively. These hypomorphic mutations have an effect on the biosynthetic reactions involving uridine diphosphate N-acetylglucosamine. Glycomic analysis revealed an aberrant glycosylation pattern in leukocytes demonstrated by a reduced level of tri-antennary and tetra-antennary N-glycans. T-cell proliferation and differentiation were impaired in patients. Most patients had developmental delay, and many had psychomotor retardation.
CONCLUSION: Impairment of PGM3 function leads to a novel primary (inborn) error of development and immunity because biallelic hypomorphic mutations are associated with impaired glycosylation and a hyper-IgE-like phenotype. Published by Mosby, Inc.

Entities:  

Keywords:  Hyper-IgE syndrome; Staphylococcus aureus; dedicator of cytokinesis 8; glycosylation; phosphoglucomutase 3; signal transducer and activator of transcription 3

Mesh:

Substances:

Year:  2014        PMID: 24698316      PMCID: PMC4825677          DOI: 10.1016/j.jaci.2014.02.025

Source DB:  PubMed          Journal:  J Allergy Clin Immunol        ISSN: 0091-6749            Impact factor:   10.793


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