A comparison of the protective effect against Mengo virus infection in mice of interferons induced by polyI: C and Mengo virus

1971 ◽  
Vol 17 (12) ◽  
pp. 1525-1532 ◽  
Author(s):  
J. B. Campbell ◽  
Julieta G. Buera

PolyI: C (complexed polyinosinic and polycytidylic acids) has been demonstrated to protect mice against infection with lethal doses of a highly virulent mutant of Mengo virus. However, the serum interferon titers it induced were considerably lower and of much shorter duration than the interferon titers induced by infection with the Mengo virus mutant. Evidence has been obtained that the interferon induced by polyI: C is as effective against Mengo virus infection as polyI: C itself. It has also been shown that, unit for unit (measured by the plaque reduction of vesicular stomatitis virus), the polyI: C-induced interferon is much more effective against Mengo virus infection than the Mengo virus-induced interferon itself.

Author(s):  
Wendy Balemans ◽  
Wim Van Hul ◽  
Marian Valko ◽  
Jan Moncol ◽  
Lee A. Denson ◽  
...  

2000 ◽  
Vol 216 (9) ◽  
pp. 1399-1404 ◽  
Author(s):  
Lisa'Marie Kim ◽  
Paul S. Morley ◽  
Brian J. McCluskey ◽  
Elizabeth L. Mumford ◽  
Sabrina L. Swenson ◽  
...  

2020 ◽  
Vol 217 (7) ◽  
Author(s):  
Qingchen Zhu ◽  
Tao Yu ◽  
Shucheng Gan ◽  
Yan Wang ◽  
Yifei Pei ◽  
...  

Ubiquitination is an essential mechanism in the control of antiviral immunity upon virus infection. Here, we identify a series of ubiquitination-modulating enzymes that are modulated by vesicular stomatitis virus (VSV). Notably, TRIM24 is down-regulated through direct transcriptional suppression induced by VSV-activated IRF3. Reducing or ablating TRIM24 compromises type I IFN (IFN-I) induction upon RNA virus infection and thus renders mice more sensitive to VSV infection. Mechanistically, VSV infection induces abundant TRIM24 translocation to mitochondria, where TRIM24 binds with TRAF3 and directly mediates K63-linked TRAF3 ubiquitination at K429/K436. This modification of TRAF3 enables its association with MAVS and TBK1, which consequently activates downstream antiviral signaling. Together, these findings establish TRIM24 as a critical positive regulator in controlling the activation of antiviral signaling and describe a previously unknown mechanism of TRIM24 function.


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