Isolation and characterization of a jacalin-related mannose-binding lectin from salt-stressed rice (Oryza sativa) plants

Planta. 2000 May;210(6):970-8. doi: 10.1007/s004250050705.


A novel plant lectin was isolated from salt-stressed rice (Oryza sativa L.) plants and partially characterized. The lectin occurs as a natural mixture of two closely related isoforms consisting of two identical non-covalently linked subunits of 15 kDa. Both isoforms are best inhibited by mannose and exhibit potent mitogenic activity towards T-lymphocytes. Biochemical analyses and sequence comparisons further revealed that the rice lectins belong to the subgroup of mannose-binding jacalin-related lectins. In addition, it could be demonstrated that the lectins described here correspond to the protein products of previously described salt-stress-induced genes. Our results not only identify the rice lectin as a stress protein but also highlight the possible importance of protein-carbohydrate interactions in stress responses in plants.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Chromatography, Ion Exchange
  • Electrophoresis, Polyacrylamide Gel
  • Hemagglutination Tests
  • Humans
  • Lectins / chemistry
  • Lectins / isolation & purification*
  • Lectins / metabolism
  • Lectins / pharmacology
  • Mannose / metabolism*
  • Mannose-Binding Lectins*
  • Mass Spectrometry
  • Mice
  • Mice, Inbred BALB C
  • Mice, Inbred C57BL
  • Models, Molecular
  • Molecular Sequence Data
  • Oryza / metabolism*
  • Oryza / physiology
  • Plant Lectins
  • Plant Proteins / chemistry
  • Plant Proteins / isolation & purification*
  • Plant Proteins / metabolism
  • Plant Proteins / pharmacology
  • Protein Structure, Tertiary
  • Rabbits
  • Sequence Alignment
  • Sodium Chloride / metabolism*


  • Lectins
  • Mannose-Binding Lectins
  • Plant Lectins
  • Plant Proteins
  • jacalin
  • orysata protein, Oryza sativa
  • Sodium Chloride
  • Mannose