Investigation of strategies with potential for producing a phosphorylcholine-free version of the filarial nematode immunomodulator, ES-62

J Helminthol. 2006 Sep;80(3):261-5.

Abstract

Phosphorylcholine (PC) is found attached to N-type glycans of proteins secreted by filarial nematodes, where it appears to act as an immunomodulator. Based on information on the structure and biosynthesis of the PC-glycan of a major secreted protein, ES-62, strategies were designed with potential for preparing PC-free material to better understand the importance of PC in filarial nematode immunomodulation. The strategies involve either enzymatic removal of PC or inhibition of its attachment during ES-62 synthesis. No method tested was found to be 100% effective although approximately 70% removal was obtained by culturing worms in Et18OCH3. Reasons for failure to obtain complete absence of PC moieties are discussed in relation to the structure and synthesis of PC-glycans and in addition PC-glycan biosynthesis is briefly commented on as a target for chemotherapy.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Enzyme Inhibitors / metabolism
  • Esterases / metabolism
  • Filariasis / immunology
  • Filariasis / metabolism
  • Filarioidea / immunology*
  • Filarioidea / metabolism
  • Helminth Proteins / biosynthesis
  • Helminth Proteins / immunology*
  • Immunologic Factors / immunology*
  • Immunologic Factors / metabolism
  • Phosphoric Diester Hydrolases / metabolism
  • Phosphorylcholine / immunology*
  • Phosphorylcholine / metabolism
  • Streptococcus pneumoniae / enzymology
  • beta-N-Acetylhexosaminidases / metabolism

Substances

  • ES-62 protein, Acanthocheilonema viteae
  • Enzyme Inhibitors
  • Helminth Proteins
  • Immunologic Factors
  • Phosphorylcholine
  • Esterases
  • Phosphoric Diester Hydrolases
  • beta-N-Acetylhexosaminidases