Interplay between NS3 protease and human La protein regulates translation-replication switch of Hepatitis C virus
Upasana Ray,Saumitra Das +1 more
TLDR
It is demonstrated that the NS3 protease (NS3pro) domain alone can specifically bind to HCV-IRES RNA, predominantly in the SLIV region, and that this binding reduces translation in favor of RNA replication.Abstract:
HCV NS3 protein plays a central role in viral polyprotein processing and RNA replication. We demonstrate that the NS3 protease (NS3(pro)) domain alone can specifically bind to HCV-IRES RNA, predominantly in the SLIV region. The cleavage activity of the NS3 protease domain is reduced upon HCV-RNA binding. More importantly, NS3(pro) binding to the SLIV hinders the interaction of La protein, a cellular IRES-trans acting factor required for HCV IRES-mediated translation, resulting in inhibition of HCV-IRES activity. Although overexpression of both NS3(pro) as well as the full length NS3 protein decreased the level of HCV IRES mediated translation, replication of HCV replicon RNA was enhanced significantly. These observations suggest that the NS3(pro) binding to HCV IRES reduces translation in favor of RNA replication. The competition between the host factor (La) and the viral protein (NS3) for binding to HCV IRES might regulate the molecular switch from translation to replication of HCV.read more
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Internal ribosome entry sites in eukaryotic mRNA molecules
TL;DR: The molecular mechanisms of IRES-mediated initiation are discussed and how they are used by specific mRNAs to permit translation under physiological circumstances such as mitosis, apoptosis, hypoxia, and some viral infections when translation of most m RNAs is repressed.
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Poliovirus RNA Replication Requires Genome Circularization through a Protein–Protein Bridge
Jens Herold,Raul Andino +1 more
TL;DR: It is shown that a long-range interaction between ribonucleoprotein (RNP) complexes formed at the ends of the viral genome is necessary for RNA replication, and RNA circularization may be a general replication mechanism for positive stranded RNA viruses.
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Compensatory Mutations in E1, p7, NS2, and NS3 Enhance Yields of Cell Culture-Infectious Intergenotypic Chimeric Hepatitis C Virus
TL;DR: It is concluded that interactions between NS 2 and E1 and p7 as well as between NS2 and NS3 are essential for virus assembly and/or release and that each of these viral proteins plays an important role in this process.
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Lack of detection of negative-strand hepatitis C virus RNA in peripheral blood mononuclear cells and other extrahepatic tissues by the highly strand-specific rTth reverse transcriptase PCR.
TL;DR: Examining sera, liver, peripheral blood mononuclear cells, and other extrahepatic tissues from HCV-infected chimpanzees and humans demonstrated that within the limits of sensitivity of this highly strand-specific reverse transcriptase PCR method, no extrahePatic replication of HCV was detected.