Journal of Virology, October 2001, p. 9165-9176, Vol. 75, No. 19
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.19.9165-9176.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Department of Microbiology, Mie University School of Medicine, Tsu-Shi, Mie-Ken 514-8507, Japan
Received 23 April 2001/Accepted 6 July 2001
Human parainfluenza type 2 virus (hPIV-2)-infected HeLa (HeLa-CA)
cells and hPIV-2 V-expressing HeLa (HeLa-V) cells show high resistance
to alpha/beta interferons (IFN-
/
) irrespective of whether
vesicular stomatitis virus or Sindbis virus is used as a challenge
virus. When Sindbis virus is used, these cells show high
susceptibility to human IFN-
. Furthermore, the multiplication of HeLa-V cells is not inhibited by IFN-
/
. HeLa cells
expressing the N-terminally truncated V protein show resistance to
IFN-
/
, showing that the IFN resistance determinant maps to
the cysteine-rich V-specific domain. A complete defect of Stat2 is
found in HeLa-CA and HeLa-V cells, whereas the levels of Stat1
expression are not significantly different among HeLa,
HeLa-CA, HeLa-P, and HeLa-V cells, indicating that
IFN-
/
resistance of HeLa-CA and HeLa-V cells is due to a defect
of Stat2. HeLa-SV41V cells show high resistance to all IFNs, and
no expression of Stat1 can be detected. Stat2 mRNA is fully
detected in HeLa-V cells. Stat2 was scarcely pulse-labeled in the
HeLa-V cells, indicating that synthesis of Stat2 is suppressed or Stat2
is very rapidly degraded in HeLa-V cells. The V protein suppresses the
in vitro translation of Stat2 mRNA more extensively than that of
Stat1 mRNA. An extremely small amount of Stat2 can be detected in
HeLa-V cells treated with proteasome inhibitors. The half-life of Stat2
is approximately 3.5 and 2 h in uninfected and hPIV-2-infected
HeLa cells, respectively. This study shows that synthesis of Stat2 may
be suppressed and Stat2 degradation is also enhanced in hPIV-2-infected
HeLa and HeLa-V cells.
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