Proteolytic processing of human cytomegalovirus glycoprotein B (gpUL55) is mediatedby the human endoprotease furin

Academic Article

Abstract

  • Inhibition of endoproteolytic cleavage of glycoprotein B (gB; gpUL55) of human cytomegalovirus was achieved by treatmentof infected fibroblasts with decanoyl peptidyl chloromethyl ketone (decRVKR-CMK), which inhibits the action of cellular subtilisin-like endoproteases with the amino acid recognition motif R × K/R R. Uncleaved gB precusor molecules of 160 kDa that were accumulated were endoglycosidase H resistant, suggesting that correct cellular transport occurred in the presence of the drug. The inhibitor also prevented endoproteolytic gB processing in CV-1 cells infected with a recombinant vaccinia virus-gB construct (VVgB). Evidence for direct involvement of the ubiquitous subtilisin-like endoprotease furin in gB cleavage was obtained from the observation that coinfection of CV-1 cells with WgB and a recombinant vaccinia-human furin construct reestablished endoproteolytic activity which was normally absent late after infection with WgB alone. © 1995 Academic Press, Inc.
  • Published In

  • Virology  Journal
  • Digital Object Identifier (doi)

    Pubmed Id

  • 8889610
  • Author List

  • Vey M; Schäfer W; Reis B; Ohuchi R; Britt W; Garten W; Klenk HD; Radsak K
  • Start Page

  • 746
  • End Page

  • 749
  • Volume

  • 206
  • Issue

  • 1