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J Gen Virol 71 (1990), 1585-1590; DOI 10.1099/0022-1317-71-7-1585
© 1990 Society for General Microbiology

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Interaction of canine distemper virus nucleocapsid variants with 70K heat-shock proteins

M. Oglesbee, S. Ringler and S. Krakowka

The Department of Veterinary Pathobiology, The Ohio State University, 1925 Coffey Road, Columbus, Ohio 43210, U.S.A.

Cytoplasmic nucleocapsid (NC) isolated from Vero (V) cells infected in the logarithmic phase of growth with Onderstepoort canine distemper virus consists of light-NC (L-NC) and dense-NC (D-NC), encapsidating full-length genomic RNA, and defective-NC (Df-NC), encapsidating variably truncated RNAs. The 70K host cell protein constituent of L-NC and Df-NC was shown to be a member of the 70K heat-shock protein (70K hsp) family. Specifically, 72K hsp is associated with L-NC, and 72K and 73K hsp are associated with Df-NC. Variable L-NC production by three different Vero cell sublines was compared to cellular 70K hsp levels. V141 supported the highest level of L-NC production and expressed high basal levels of 70K hsp in uninfected cells. These high basal levels correspond to a large distribution of log phase V141s in the S phase of the cell cycle. V138-L and V138-H cells produced lower amounts of L-NC and exhibited similar low basal levels of 70K hsp expression, corresponding to low percentages of log phase cells in the S phase cell cycle compartment. Heat shock was effective in inducing L-NC expression in V138-H, which otherwise produced D-NC. Similar cell subline differences in L-NC production were obtained for eight different virus pools derived from the same plaque-purified parental stock. Enhanced biological activity was associated with L-NC based on correlation between L-NC production, viral titre, and plaque areas measured over infected cells.

Received 29 August 1989; accepted 26 February 1990.


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