Pea lectin is correctly processed, stable and active in leaves of transgenic potato plants

Plant Mol Biol. 1991 Jul;17(1):89-100. doi: 10.1007/BF00036809.

Abstract

A gene encoding the preproprotein of the pea (Pisum sativum) lectin was expressed in transgenic potato plants using a cauliflower mosaic virus (CaMV) 35S promoter or a tobacco ribulose bisphosphate carboxylase small subunit (ssRubisco) promoter. Presence of the pea lectin to levels greater than 1% of total soluble leaf protein was detected by radioimmunoassay (RIA). The pattern of expression derived from the two promoters was established using both RIA and a squash-blot immunolocalisation technique. Western blotting demonstrated that the preproprotein was correctly processed, generating alpha and beta subunits that assembled to give an isolectin form observed in pea seeds and roots. It was also found that the haemagglutination activity and specificity of pea lectin synthesised in transgenic potato leaves was comparable to purified lectin from pea cotyledons.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Blotting, Northern
  • Blotting, Southern
  • Blotting, Western
  • Cloning, Molecular
  • Hemagglutination Tests
  • Isoelectric Focusing
  • Lectins / genetics*
  • Lectins / metabolism
  • Plant Lectins
  • Plasmids
  • Protein Precursors / genetics
  • Protein Processing, Post-Translational*
  • Rabbits
  • Radioimmunoassay
  • Regeneration
  • Ribulose-Bisphosphate Carboxylase / genetics
  • Solanum tuberosum / genetics
  • Transformation, Genetic

Substances

  • Lectins
  • Plant Lectins
  • Protein Precursors
  • pea lectin
  • Ribulose-Bisphosphate Carboxylase