caa a22 4500 475767403 CHVBK 20180406123610.0 cr unu---uuuuu 170329e20000201xx s 000 0 eng 10.1007/s007050050033 doi (NATIONALLICENCE)springer-10.1007/s007050050033 Herpes simplex virus UL17 protein is associated with B capsids and colocalizes with ICP35 and VP5 in infected cells [Elektronische Daten] [F. Goshima, D. Watanabe, H. Takakuwa, K. Wada, T. Daikoku, M. Yamada, Y. Nishiyama] Summary.:  A previous study using a mutant lacking the UL17 gene has suggested that the UL17 protein of herpes simplex virus type 1 (HSV-1) is required for the cleavage/packaging of viral DNA. In this study, we have raised a rabbit polyclonal antiserum which specifically reacted with the UL17 protein which has an apparent molecular mass of 78-kDa in the lysates of HSV types 1- and 2-infected Vero cells. Western blot analysis of intracellular capsids demonstrates that the UL17 protein was associated with B and C capsids. Indirect immunofluorescence studies reveal that it colocalized with the major capsid protein VP5 and the scaffoling protein ICP35 within the nucleus. These results suggest that the association of the UL17 protein with immature B-type capsids is important for its role in cleavage/packaging. 2000 Springer-Verlag/, Wien Goshima F. Laboratory of Virology, Research Institute for Disease Mechanism and Control, Nagoya University School of Medicine, Nagoya, Japan, JP aut Watanabe D. Laboratory of Virology, Research Institute for Disease Mechanism and Control, Nagoya University School of Medicine, Nagoya, Japan, JP aut Takakuwa H. Laboratory of Virology, Research Institute for Disease Mechanism and Control, Nagoya University School of Medicine, Nagoya, Japan, JP aut Wada K. Laboratory of Virology, Research Institute for Disease Mechanism and Control, Nagoya University School of Medicine, Nagoya, Japan, JP aut Daikoku T. Laboratory of Virology, Research Institute for Disease Mechanism and Control, Nagoya University School of Medicine, Nagoya, Japan, JP aut Yamada M. Department of Virology, Okayama University School of Medicine, Okayama, Japan, JP aut Nishiyama Y. Laboratory of Virology, Research Institute for Disease Mechanism and Control, Nagoya University School of Medicine, Nagoya, Japan, JP aut https://doi.org/10.1007/s007050050033 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s007050050033 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Goshima F. Laboratory of Virology, Research Institute for Disease Mechanism and Control, Nagoya University School of Medicine, Nagoya, Japan, JP aut NATIONALLICENCE 700 1- Watanabe D. Laboratory of Virology, Research Institute for Disease Mechanism and Control, Nagoya University School of Medicine, Nagoya, Japan, JP aut NATIONALLICENCE 700 1- Takakuwa H. Laboratory of Virology, Research Institute for Disease Mechanism and Control, Nagoya University School of Medicine, Nagoya, Japan, JP aut NATIONALLICENCE 700 1- Wada K. Laboratory of Virology, Research Institute for Disease Mechanism and Control, Nagoya University School of Medicine, Nagoya, Japan, JP aut NATIONALLICENCE 700 1- Daikoku T. Laboratory of Virology, Research Institute for Disease Mechanism and Control, Nagoya University School of Medicine, Nagoya, Japan, JP aut NATIONALLICENCE 700 1- Yamada M. Department of Virology, Okayama University School of Medicine, Okayama, Japan, JP aut NATIONALLICENCE 700 1- Nishiyama Y. Laboratory of Virology, Research Institute for Disease Mechanism and Control, Nagoya University School of Medicine, Nagoya, Japan, JP aut Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer