Proteolytic processing of human cytomegalovirus glycoprotein B (gpUL55) is mediated by the human endoprotease furin.
Virology
; 206(1): 746-9, 1995 Jan 10.
Article
em En
| MEDLINE
| ID: mdl-7726996
Inhibition of endoproteolytic cleavage of glycoprotein B (gB; gpUL55) of human cytomegalovirus was achieved by treatment of 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 x K/R R. Uncleaved gB precursor 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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Subtilisinas
/
Processamento de Proteína Pós-Traducional
/
Proteínas do Envelope Viral
/
Citomegalovirus
Limite:
Humans
Idioma:
En
Revista:
Virology
Ano de publicação:
1995
Tipo de documento:
Article
País de afiliação:
Alemanha
País de publicação:
Estados Unidos