Mannosidase 2, alpha 1 deficiency is associated with ricin resistance in embryonic stem (ES) cells

PLoS One. 2011;6(8):e22993. doi: 10.1371/journal.pone.0022993. Epub 2011 Aug 23.

Abstract

Host gene products required for mediating the action of toxins are potential targets for reversing or controlling their pathogenic impact following exposure. To identify such targets libraries of insertional gene-trap mutations generated with a PiggyBac transposon in Blm-deficient embryonic stem cells were exposed to the plant toxin, ricin. Resistant clones were isolated and genetically characterised and one was found to be a homozygous mutant of the mannosidase 2, alpha 1 (Man2α1) locus with a matching defect in the homologous allele. The causality of the molecular lesion was confirmed by removal of the transposon following expression of PB-transposase. Comparative glycomic and lectin binding analysis of the Man2α1 (-/-) ricin resistant cells revealed an increase in the levels of hybrid glycan structures and a reduction in terminal β-galactose moieties, potential target receptors for ricin. Furthermore, naïve ES cells treated with inhibitors of the N-linked glycosylation pathway at the mannosidase 2, alpha 1 step exhibited either full or partial resistance to ricin. Therefore, we conclusively identified mannosidase 2, alpha 1 deficiency to be associated with ricin resistance.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • Cell Line
  • DNA Transposable Elements / genetics
  • Embryonic Stem Cells / drug effects*
  • Embryonic Stem Cells / enzymology*
  • Embryonic Stem Cells / ultrastructure
  • Gene Library
  • Glycomics
  • Glycosylation / drug effects
  • Molecular Sequence Data
  • Mutagenesis, Insertional / genetics
  • Polysaccharides / chemistry
  • Polysaccharides / metabolism
  • Ricin / toxicity*
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • alpha-Mannosidase / deficiency*
  • alpha-Mannosidase / metabolism

Substances

  • DNA Transposable Elements
  • Polysaccharides
  • Ricin
  • alpha-Mannosidase