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Article

Active foamy virus proteinase is essential for virus infectivity but not for formation of a Pol polyprotein

1 Nov 1995

Abstract excerpt

To analyze proteolytic processing of foamy (spuma) retroviruses, two mutations were generated in the presumed active-site triplet Asp-Ser-Gly in the predicted proteinase (PR) region of the human foamy virus (HSRV). The mutations changed either the presumed catalytic aspartic acid residue to a catalytically incompetent alanine or the adjacent serine to a threonine found in most cellular and retroviral proteases at...

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PMID: 7474150
DOI: 10.1128/jvi.69.11.7264-7268.1995

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