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Papers In Press, published online ahead of print April 21, 2005
Department of Virology, Cleveland Clinic Foundation, Cleveland, OH 44195
Corresponding Author: neznann{at}ccf.org
Activation of NF-
J. Biol. Chem, 10.1074/jbc.M502303200
Submitted on March 1, 2005
Revised on April 20, 2005
Accepted on April 21, 2005
Proteolytic cleavage of the p65-RelA subunit of NF-
B during poliovirus infection
B during viral infection is one of the critical elements in innate immune response. Several virus-specific factors, such as double-stranded RNA, can trigger host defense mechanisms by inducing NF-B-mediated expression of cytokines and interferons. Early stages of poliovirus infection are also associated with degradation of IB
and translocation of NF-B into the nucleus. However, at later stages of poliovirus replication the p65-RelA component of the NF-B complex is undergoing a specific cleavage that coincides with the onset of intensive poliovirus protein synthesis and the appearance of the activity of poliovirus protease 3C. Indeed, the p65-RelA amino acid sequence contains the recognition site for 3C, and recombinant protein 3C was shown to be capable of proteolytic cleavage of p65-RelA generating truncated product similar to that observed during poliovirus infection. Cleavage of p65-RelA occurs during replication of ECHO-1 and rhinovirus 14, suggesting that inactivation of NF-B function by proteolytic cleavage of p65-RelA is the common mechanism by which picornaviruses suppress the innate immune response.
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