Abstract
Отримання рекомбінантного дефензину 1 сосни звичайної та його антифунгальна активність
Highlights
Defensins are evolutionally conservative molecules of innate immunity of plants, mollusks, insects and animals which are characterized by small size (< 10 kD), and amphipathic, b-layers-rich structure and stabilized disulfide bridges [1, 2]
We describe subcloning of PsDef1 mature form into bacterial expression vector pET 42à(+) and the expression of recombinant GST/PsDef1 in Escherichia coli
The presence of an endoplasmic reticulum signal peptide, which is removed during the protein processing, is a feature of all plant defensins [3]
Summary
Defensins are evolutionally conservative molecules of innate immunity of plants, mollusks, insects and animals which are characterized by small size (< 10 kD), and amphipathic, b-layers-rich structure and stabilized disulfide bridges [1, 2]. Affinity purification of the recombinant GST/PsDef1 on glutathione-sepharose column and proteolytic removal of GST moiety with Factor Xa allowed us to generate functionally active preparations of recombinant PsDef1. The antimicrobial activity of recombinant PsDef1 was found to be comparable to that of endogenous Scots pine defensin.
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