Identification of the human Lewis(a) carbohydrate motif in a secretory peroxidase from a plant cell suspension culture (Vaccinium myrtillus L.)

FEBS Lett. 1997 Sep 29;415(2):186-91. doi: 10.1016/s0014-5793(97)01121-6.

Abstract

This paper reports for the first time the presence of the human Lewis(a) type determinant in glycoproteins secreted by plant cells. A single glycopeptide was identified in the tryptic hydrolysis of the peroxidase VMPxC1 from Vaccinium myrtillus L. by HPLC/ESI-MS. The oligosaccharide structures were elucidated by ESI-MS-MS and by methylation analysis before and after removal of fucose by mild acid hydrolysis. The major structure determined is of the biantennary plant complex type containing the outer chain motif Lewis(a) [structure in text]. A corresponding fucosyltransferase activity catalyzing the formation of Lewis(a) type structures in vitro was identified in cellular extracts of the suspension cultures.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Carbohydrate Conformation
  • Carbohydrate Sequence
  • Cells, Cultured
  • Electrophoresis, Polyacrylamide Gel
  • Fucosyltransferases / analysis
  • Fucosyltransferases / metabolism
  • Glycopeptides / analysis
  • Glycopeptides / chemistry*
  • Glycopeptides / isolation & purification
  • Humans
  • Lewis Blood Group Antigens / analysis
  • Lewis Blood Group Antigens / chemistry*
  • Mass Spectrometry
  • Methylation
  • Molecular Sequence Data
  • Monosaccharides / analysis
  • Oligosaccharides / analysis
  • Oligosaccharides / chemistry
  • Oligosaccharides / isolation & purification
  • Peroxidases / chemistry*
  • Plant Proteins / chemistry
  • Plants / chemistry*
  • Plants / enzymology
  • Sequence Analysis
  • Trypsin / metabolism

Substances

  • Glycopeptides
  • Lewis Blood Group Antigens
  • Monosaccharides
  • Oligosaccharides
  • Plant Proteins
  • Peroxidases
  • Fucosyltransferases
  • Trypsin