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Abstract
A single-chained antifungal protein with a molecular weight of 6.5 kDa and displaying
a novel N-terminal sequence was isolated from dried juvenile cicadas which are used
in traditional Chinese medicine, by using ion exchange chromatography on DEAE-cellulose,
affinity chromatography on Affi-gel blue gel, ion exchange chromatography on SP-Sepharose
and then gel filtration on a Superdex peptide column. The peptide, designated cicadin,
exerted potent antifungal activity with IC(50) values at nonomolar concentrations
against a variety of fungi including Botrytis cinerea, Mycosphaerella arachidicola,
Fusarium oxysporum, Rhizoctonia solani and Coprinus comatus. Cicadin suppressed the
activity of HIV-1 reverse transcriptase and stimulated the proliferation of murine
splenocytes.