Identification of alg3 in the mushroom-forming fungus Schizophyllum commune and analysis of the ¿alg3 knockout mutant

E. Berends, L. Lehle, M. Henquet, T. Hesselink, H.A.B. Wösten, L.G. Lugones, H.J. Bosch

Research output: Contribution to journalArticleAcademicpeer-review

3 Citations (Scopus)

Abstract

Alg3 of Saccharomyces cerevisiae catalyzes the mannosyl transfer from Man-P-Dol to Man(5)GlcNAc(2)-PP-Dol resulting in the formation of Man(6)GlcNAc(2)-PP-Dol, which is then further processed to the final precursor oligosaccharide Glc(3)Man(9)GlcNAc(2) for N-glycosylation of proteins. Here, we identified the alg3 gene of the mushroom-forming fungus Schizophyllum commune by homology search. Its function was confirmed by the complementation of the Delta alg3 strain of S. cerevisiae. Inactivation of alg3 in S. commune resulted in the production of predominantly Man(3)GlcNAc(2) protein-linked N-glycans. No impact on growth nor a developmental phenotype due to the deletion was observed. This provides a first step toward engineering of a homogeneous, humanized N-glycosylation pattern for the production of therapeutic glycoproteins in mushrooms.
Original languageEnglish
Pages (from-to)147-154
Number of pages8
JournalGlycobiology
Volume23
Issue number2
DOIs
Publication statusPublished - 2013

Keywords

  • saccharomyces-cerevisiae
  • n-glycan
  • gene
  • glycoproteins
  • enzyme
  • mannosyltransferase
  • glucocerebrosidase
  • oligosaccharides
  • glycosylation
  • therapy

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