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Background  Heterologous protein expression in microorganisms may contribute to identify and demonstrate antifungal activity of novel proteins. The  Solanum nigrum  osmotin-like protein (SnOLP) gene encodes a member of pathogenesis-related (PR) proteins, from the PR-5 sub-group, the last comprising several proteins with different functions, including antifungal activity. Based on deduced amino acid sequence of SnOLP, computer modeling produced a tertiary structure which is indicative of antifungal activity.    Results  To validate the potential antifungal activity of SnOLP, a hexahistidine-tagged mature SnOLP form was overexpressed in  Escherichia coli  M15 strain carried out by a pQE30 vector construction. The urea solubilized His 6 -tagged mature SnOLP protein was affinity-purified by immobilized-metal (Ni 2+ ) affinity column chromatography. As SnOLP requires the correct formation of eight disulfide bonds, not correctly formed in bacterial cells, we adapted an  in vitro  method to refold the  E. coli  expressed SnOLP by using reduced:oxidized gluthatione redox buffer. This method generated biologically active conformations of the recombinant mature SnOLP, which exerted antifungal action towards plant pathogenic fungi ( Fusarium solani  f. sp. glycines ,  Colletotrichum  spp.,  Macrophomina phaseolina ) and oomycete ( Phytophthora nicotiana var. parasitica ) under  in vitro  conditions.    Conclusion  Since SnOLP displays activity against economically important plant pathogenic fungi and oomycete, it represents a novel PR-5 protein with promising utility for biotechnological applications.

Expression in Escherichia coli, purification, refolding and antifungal activity of an osmotin from Solanum nigrum