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J. Virol., 12 1996, 8485-8491, Vol 70, No. 12
S Moffatt, N Tanaka, K Tada, M Nose, M Nakamura, O Muraoka, T Hirano and K Sugamura
We examined the biological function of a nonstructural regulatory protein,
NS1, of human parvovirus B19. Because of the cytotoxic activity of NS1,
human hematopoietic cell lines, K562, Raji, and THP-1, were established as
transfectants which produce the viral NS1 protein upon induction by using
bacterial lactose repressor/operator system. NS1 was significantly produced
in the three transfectant cells in an inducer dose- and time-dependent
manner. Surprisingly, these three transfectants secreted an inflammatory
cytokine, interleukin-6 (IL-6), in response to induction. However, no
production of other related cytokines, IL-1beta, IL-8, or tumor necrosis
factor alpha, was seen. Moreover, NS1-primed IL-6 induction was transiently
demonstrated in primary human endothelial cells. Analysis with luciferase
reporter plasmids carrying IL-6 promoter mutant fragments demonstrated that
NS1 effect is mediated by a NF-kappaB binding site in the IL-6 promoter
region, strongly implying that NS1 functions as a trans-acting
transcriptional activator on the IL-6 promoter. Our novel finding, IL-6
induction by NS1, supports the possible relationship between parvovirus B19
infection and polyclonal activation of B cells in rheumatoid arthritis and
indicates that NS1 protein may play a significant role in the pathogenesis
of some B19-associated diseases by modulating the expression of host
cellular genes.
Copyright © 1996, American Society for Microbiology
A cytotoxic nonstructural protein, NS1, of human parvovirus B19 induces activation of interleukin-6 gene expression
Department of Microbiology, Tohoku University School of Medicine, Sendai, Japan.
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