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

J Allergy Clin Immunol. 2014 May;133(5):1410-9, 1419.e1-13. doi: 10.1016/j.jaci.2014.02.025. Epub 2014 Apr 1.

Abstract

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.

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

Publication types

  • Clinical Trial
  • Multicenter Study
  • Research Support, N.I.H., Intramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Amino Acid Substitution
  • Cell Proliferation
  • Child
  • Chromosomes, Human, Pair 6 / genetics*
  • Chromosomes, Human, Pair 6 / metabolism
  • Female
  • Genetic Diseases, Inborn / enzymology
  • Genetic Diseases, Inborn / genetics*
  • Genetic Diseases, Inborn / immunology
  • Genetic Linkage
  • Glycosylation
  • Homozygote*
  • Humans
  • Immunity / genetics*
  • Immunoglobulin E*
  • Infant
  • Job Syndrome / enzymology
  • Job Syndrome / genetics*
  • Job Syndrome / immunology
  • Male
  • Mutation, Missense*
  • Phosphoglucomutase / genetics*
  • Phosphoglucomutase / immunology
  • Phosphoglucomutase / metabolism
  • T-Lymphocytes / enzymology
  • T-Lymphocytes / immunology
  • Tunisia

Substances

  • Immunoglobulin E
  • PGM3 protein, human
  • Phosphoglucomutase