Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Apoptosis*
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Camptothecin / metabolism
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Caspase 3
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Caspases / metabolism
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Cell Line, Tumor
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Epithelial Cells / virology*
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Etoposide / metabolism
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Herpesvirus 2, Human / chemistry*
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Herpesvirus 2, Human / growth & development
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Herpesvirus 2, Human / pathogenicity*
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Humans
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Osmotic Pressure
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Poly(ADP-ribose) Polymerases / metabolism
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Staurosporine / metabolism
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Viral Proteins / genetics
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Viral Proteins / physiology*
Substances
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UL14 protein, Human herpesvirus 1
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Viral Proteins
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Etoposide
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Poly(ADP-ribose) Polymerases
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CASP3 protein, human
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Caspase 3
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Caspases
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Staurosporine
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Camptothecin