Twonovel triterpene sulfates have been isolated from Fusarium compactumby bioactivitydirected fractionation using an assay which measures the inhibition ofproteolytic activity ofrhinovirus 3C protease on a fluorogenic peptide substrate. The compounds were purified by countercurrent and reverse phase chromatographies. NMR,MS, UVand IR studies revealed two triterpene sulfates, uncommon metabolites of terrestrial fungi.In the course of screening microorganisms for the production of bioactive metabolites, a Fusarium compactum sp., isolated from an ant hill soil sample collected near the village of Rantan, Nigeria, was found to produce rhinovirus 3C protease inhibition activity. The 3C protease, one of two virally encoded proteases, is responsible for cleaving the initially translated rhinoviral polyprotein at eight locations to form the mature structural proteins and viral replicative enzymes. 1} There are more than 100 known serotypes of human rhinovirus,2) and they are thought to be responsible for 40~60% of the common colds.3) In principle, compoundswhich inhibit the proteolytic action of the 3C protease would disrupt replication of the rhinovirus, and could lead to an effective drug treatment for the common cold.Using an assay which measures the inhibition of 3Cprotease activity on a synthetic fluorogenic substrate, bioactivity-directed fractionation of a stationary fermentation extract of Fusarium compactum (AB 21941-103) provided two triterpene sulfates. Triterpene sulfates had not been reported as bioactive metabolites from terrestrial fungi until Vesonder and Burmeister isolated them from several Fusarium species in a search for potentially phytotoxic secondary metabolites.4'5) It was found that these metabolites are produced in relative abundancewhenterrestrial Fusarium species are grown on grain substrates.5) In our study, Shredded Wheat was used as a solid support for the growth of the fungus.