Molecular structure and properties of lectin from tomato fruit

Biosci Biotechnol Biochem. 2008 Oct;72(10):2640-50. doi: 10.1271/bbb.80310. Epub 2008 Oct 7.


A cDNA encoding tomato fruit lectin was cloned from an unripe cherry-tomato fruit cDNA library. The isolated lectin cDNA contained an open reading frame encoding 365 amino acids, including peptides that were sequenced. The deduced sequence consisted of three distinct domains: (i) an N-terminal short extensin-like domain; (ii) a Cys-rich carbohydrate binding domain composed of four almost identical chitin-binding domains; (iii) an internal extensin-like domain of 101 residues containing 15 SerPro(4) motifs inserted between the first and second chitin-binding domains. The molecular weight of the lectin was 65,633 and that of the deglycosylated lectin was 32,948, as determined by matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry (MALDI-TOF MS). This correlated with the estimated molecular weight of the deduced sequence. Recombinant tomato lectin expressed in Pichia pastoris possessed chitin-binding but not hemagglutinating activity. These findings confirmed that the cDNA encoded tomato lectin.

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Chromatography, Gel
  • Conserved Sequence
  • DNA, Complementary / genetics
  • Fruit / chemistry*
  • Fruit / genetics
  • Fruit / metabolism*
  • Gene Expression
  • Glycosylation
  • Molecular Sequence Data
  • Molecular Weight
  • Pichia / genetics
  • Pichia / metabolism
  • Plant Lectins / chemistry*
  • Plant Lectins / genetics
  • Plant Lectins / metabolism*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Sequence Alignment
  • Solanum lycopersicum / chemistry*
  • Solanum lycopersicum / genetics
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization


  • DNA, Complementary
  • Plant Lectins
  • Recombinant Proteins
  • tomato lectin