Abstract
An inhibitor activity that prevents the proteolytic processing of Cowpea Mosaic Virus (CPMV) polyprotein has been discovered in crude wheat germ extracts. CPMV is a comovirus that replicates via the synthesis of two polyproteins which are subsequently cleaved by a viral proteinase to yield the functional viral proteins. Since this scheme of replication is common to many other viral groups, a potential target for antivirals is the proteinase responsible for polyprotein processing. A partial purification of this wheat germ inhibitor activity has been accomplished by classical protein purification methods which include ammonium sulfate precipitation, heat treatment, ion exchange, size exclusion chromatography, hydroxylapatite chromatography and hydrophobic interaction. Some biochemical properties of the inhibitor were characterized and its ability to inhibit several cellular proteinases was investigated. The ability of the inhibitor to prevent processing in other viral polyproteins was also tested.
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