Inhibitory effect of N-phenyl-N?-aryl- or alkylthiourea derivatives on the multiplication of some picornaviruses (Coxsackie B1, ECHO 19, and foot-and-mouth disease virus) in cell cultures

1972 ◽  
Vol 38 (2-3) ◽  
pp. 159-166 ◽  
Author(s):  
A. Galabov ◽  
L. Shindarov ◽  
G. Vassilev ◽  
R. Vassileva
Keyword(s):  
Disease Virus ◽  
Cell Cultures ◽  
Foot And Mouth Disease ◽  
Inhibitory Effect ◽  
Mouth Disease ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals Degradation of Nuclear Factor Kappa B during Foot-and-Mouth Disease Virus Infection

2007 ◽  
Vol 81 (23) ◽  
pp. 12803-12815 ◽  
Author(s):  
Teresa de los Santos ◽  
Fayna Diaz-San Segundo ◽  
Marvin J. Grubman
Keyword(s):  
Disease Virus ◽  
Nuclear Translocation ◽  
Inflammatory Responses ◽  
Foot And Mouth Disease ◽  
Inhibitory Effect ◽  
Mouth Disease ◽  
Innate Immune ◽  
Nuclear Factor ◽  
Mouth Disease Virus ◽  
Foot And Mouth

ABSTRACT We have previously shown that the leader proteinase (Lpro) of foot-and-mouth disease virus (FMDV) interferes with the innate immune response by blocking the translation of interferon (IFN) protein and by reducing the immediate-early induction of beta IFN mRNA and IFN-stimulated genes. Here, we report that Lpro regulates the activity of nuclear factor κB (NF-κB). Analysis of NF-κB-dependent reporter gene expression in BHK-21 cells demonstrated that infection with wild-type (WT) virus has an inhibitory effect compared to infection with a genetically engineered mutant lacking the leader coding region. The expression of endogenous NF-κB-dependent genes tumor necrosis factor alpha and RANTES is also reduced in WT virus-infected primary porcine cells. This inhibitory effect is neither the result of a decrease in the level of the mRNA of p65/RelA, a subunit of NF-κB, nor a block on the nuclear translocation of p65/RelA, but instead appears to be a consequence of the degradation of accumulated p65/RelA. Viral Lpro is localized to the nucleus of infected cells, and there is a correlation between the translocation of Lpro and the decrease in the amount of nuclear p65/RelA. By using a recombinant cardiovirus expressing Lpro, we demonstrate that the disappearance of p65/RelA takes place in the absence of any other FMDV product. The observation that Lpro disrupts the integrity of NF-κB suggests a global mechanism by which FMDV antagonizes the cellular innate immune and inflammatory responses to viral infection.

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