Characterization of the UL16 gene product of herpes simplex virus type 2 |
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Authors: | S Oshima T Daikoku S Shibata H Yamada F Goshima Y Nishiyama |
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Institution: | (1) Laboratory of Virology, Research Institute for Disease Mechanism and Control, Nagoya University School of Medicine, Nagoya, Japan, JP;(2) Virus Division, Nagoya City Public Health Research Institute, Nagoya, Japan, JP |
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Abstract: | Summary. We have raised rabbit polyclonal antisera against a His-tagged herpes simplex virus type 1 (HSV-1) UL16 fusion protein, one
of which very specifically reacted with 40 kDa and 41 kDa proteins in the lysates of HSV-1 and HSV-2-infected cells, respectively.
Since its reactivity to the 41 kDa protein was clearly eliminated by pre-adsorption with E. coli lysates expressing the UL16 fusion protein, the antiserum was used to characterize the UL16 products of HSV-2. The HSV-2
UL16 protein was produced at the late phase of infection in a manner highly dependent on viral DNA synthesis and was distributed
in both the nuclei and the cytoplasma of infected cells. In immunofluorescence studies, the UL16-specific fluorescence in
the nuclei was shown to be detected as small discrete granules. On the other hand, the cytoplasmic fluorescence was diffusely
distributed around the nucleus at 8 h postinfection but, at later times of infection, it was mainly detected as a mass at
a perinuclear region. The analysis on its association with capsids has revealed that the UL16 protein copurified with C capsids
but not B and A capsids, and that the association with C capsids was not tight. Moreover, our experiments have shown that
a detectable level of the UL16 protein was not associated with extracellular virions, and that the partially purified UL16
proteins had a DNA-binding activity. These observations are consistent with the hypothesis that the UL16 protein plays a role
in capsid maturation including DNA packaging/cleavage. We have also determined the complete nucleotide sequence of the HSV-2
UL16 gene and found that a nonstandard initiation codon may be used for its translation.
Accepted January 12, 1998 Received October 31, 1997 |
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