Pharmacological Chaperoning: A Potential Treatment for PMM2-CDG

Hum Mutat. 2017 Feb;38(2):160-168. doi: 10.1002/humu.23138. Epub 2016 Nov 21.

Abstract

The congenital disorder of glycosylation (CDG) due to phosphomannomutase 2 deficiency (PMM2-CDG), the most common N-glycosylation disorder, is a multisystem disease for which no effective treatment is available. The recent functional characterization of disease-causing mutations described in patients with PMM2-CDG led to the idea of a therapeutic strategy involving pharmacological chaperones (PC) to rescue PMM2 loss-of-function mutations. The present work describes the high-throughput screening, by differential scanning fluorimetry, of 10,000 low-molecular-weight compounds from a commercial library, to search for possible PCs for the enzyme PMM2. This exercise identified eight compounds that increased the thermal stability of PMM2. Of these, four compounds functioned as potential PCs that significantly increased the stability of several destabilizing and oligomerization mutants and also increased PMM activity in a disease model of cells overexpressing PMM2 mutations. Structural analysis revealed one of these compounds to provide an excellent starting point for chemical optimization since it passed tests based on a number of pharmacochemical quality filters. The present results provide the first proof-of-concept of a possible treatment for PMM2-CDG and describe a promising chemical structure as a starting point for the development of new therapeutic agents for this severe orphan disease.

Keywords: CDG; PMM2; misfolding proteins; pharmacological chaperones.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alleles
  • Congenital Disorders of Glycosylation / drug therapy
  • Congenital Disorders of Glycosylation / genetics*
  • Drug Discovery
  • Enzyme Activation
  • Fibroblasts / metabolism
  • Genotype
  • High-Throughput Screening Assays
  • Humans
  • Loss of Function Mutation
  • Molecular Targeted Therapy
  • Mutation
  • Phosphotransferases (Phosphomutases) / chemistry
  • Phosphotransferases (Phosphomutases) / genetics*
  • Phosphotransferases (Phosphomutases) / isolation & purification
  • Protein Stability
  • Proteolysis
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / isolation & purification
  • Recombinant Fusion Proteins / metabolism
  • Small Molecule Libraries
  • Structure-Activity Relationship

Substances

  • Recombinant Fusion Proteins
  • Small Molecule Libraries
  • Phosphotransferases (Phosphomutases)
  • phosphomannomutase 2, human