Herpes simplex virus UL14 protein blocks apoptosis.
We report that an HSV-2 UL14 protein expressing cell line (14/HEp-2) was more resistant to apoptosis induced by osmotic shock and certain drugs than its parental cell line. Furthermore, HSV-1 UL14 protein deletion virus (UL14D) showed weaker inhibition of apoptosis compared to the rescued virus UL14R. The protein's anti-apoptotic function may derive from its heat shock protein-like properties.
Yamauchi
Yohei
Y
Laboratory of Virology, Institute for Disease Mechanism and Control, Nagoya University School of Medicine, Nagoya, Aichi 466-8550, Japan.
Daikoku
Tohru
T
Goshima
Fumi
F
Nishiyama
Yukihiro
Y
D017209:Apoptosis; D002166:Camptothecin / Q000378:metabolism; D053148:Caspase 3; D020169:Caspases / Q000378:metabolism; D045744:Cell Line, Tumor; D004847:Epithelial Cells / Q000821:virology*; D005047:Etoposide / Q000378:metabolism; D018258:Herpesvirus 2, Human / Q000737:chemistry* / Q000254:growth & development / Q000472:pathogenicity*; D006801:Humans; D009997:Osmotic Pressure; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism; D019311:Staurosporine / Q000378:metabolism; D014764:Viral Proteins / Q000235:genetics / Q000502:physiology*
C402639:UL14 protein, Human herpesvirus 1; D014764:Viral Proteins; D005047:Etoposide; D011065:Poly(ADP-ribose) Polymerases; C505407:CASP3 protein, human; D053148:Caspase 3; D020169:Caspases; D019311:Staurosporine; D002166:Camptothecin