Cloning, characterization, and bacterial over-expression of an osmotin-like protein gene from Solanum nigrum L. with antifungal activity against three necrotrophic fungi.
A new osmotin-like protein gene from Solanum nigrum L. var indica (SindOLP) was cloned and overexpressed in Escherichia coli. The full-length intron-less gene is 744 bp, encoding a mature protein of 247 amino acids with a molecular mass of 26 kDa. The protein has an N-terminal cleavable signal sequence of 21 amino acids. There is the Thaumatin family signature pattern, with one each of amidation, N-myristoylation, casein kinase II phosphorylation, tyrosine kinase phosphorylation, and protein kinase C phosphorylation sites. Hydropathy plot showed that it has six transmembrane helices. It has antifungal activity and can permeabilize fungal hyphae and spores. SindOLP is most active at pH 8, 25 °C and its antifungal activity is retained after 75 °C for 30 min. SindOLP inhibits fungal spore germination. The protein however lacks glucanase activity. The potential for SindOLP in developing fungus-resistant, transgenic crops is discussed.