Molecular Cloning of GAFP-1, an Antifungal Protein from Gastrodia elata

The cloning and sequencing of a full length cDNA of GAFP-1 ( Gastrodia antifungal protein), an antifungal protein from Gastrodia elata BI. f. fiavida S. Chow is reported. Degenerate primers were designed based on the N-terminal partial sequence from purified GAFP-1 to amplify the corresponding cDNA by rapid amplification of cDNA ends (RACE). A cDNA was obtained that contains an open reading frame for a peptide of 171 amino acids which matches the known peptide sequences. A 5'UTR (untranslated region) of 55 bp was found upstream from the translation initiation site. Two poly(A) adenylation sites were located downstream the stop codon. GAFP-1 cDNA and its deduced amino acid sequence share high homology with the mannose binding lectins from Epipactis helloborine, Listera ovata and snowdrop ( Galanthus nivalis ). The cDNA can now be used for testing the potential of GAFP-1 for engineering fungal resistance in crop plants.