Abstract
An antifungal protein fraction against Botrytis cinerea was purified from the leaves of Gentiana triflora. Polypeptides with molecular weight ca. 8.0 K (8.0 KP) and 7.0 K (7.0 KP) were detected by Tricine-SDS PAGE under reducing conditions. The deduced amino acid sequence of 8.0 KP cDNA showed amino acid identities with lipid transfer proteins from Apium graveolens (32.4%), Lycopersicon pennellii (31.5%), L. esculentum (31.5%), Nicotiana tabacum (30.7%), non-specific lipid transfer protein from L. esculentum (28.0%), and an unknown protein from Prosopis juliflora (30.7%) (GtLTP1). The deduced amino acid sequence of 7.0 KP showed amino acid identities with putative lipid transfer proteins from Arabidopsis thaliana (26.3% and 22.9%), Gossypium hirsutum (21.0%), Tamarix hispida (19.5%), Populus trichocarpa (15.9%) and an unknown protein from Vitis vinifera (17.2%) (GtLTP2). Both GtLTP1 and GtLTP2 were present as a multi-gene family in the genome and were strongly expressed in the roots and stems. Overexpression of GtLTP1 in tobacco plants improved tolerance against B. cinerea, demonstrating that GtLTP1 is a useful molecular tool for genetic engineering of disease-resistant plants.
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