The Hepatitis C Virus Encodes a Serine Protease Involved in Processing of the Putative Nonstructural Proteins from the Viral Polyprotein Precursor

Eckart, Michael; Selby, Mark; Masiarz, Frank R.; Lee, C.; Berger, Kimberly; Crawford, Kenneth A.; Kuo, C.; Kuo, George; Houghton, Michael; Choo, Qui‐Lim

doi:10.1006/bbrc.1993.1429

Cited by 182 publications

(117 citation statements)

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“…[32][33][34][35] These NS3-deleted expression plasmids were used in coimmunoprecipitation assays, to show that the helicase domain, but not the protease domain of NS3, binds TBK1 (Fig. 4A).…”

Section: Resultsmentioning

confidence: 99%

Interaction between the HCV NS3 protein and the host TBK1 protein leads to inhibition of cellular antiviral responses

et al. 2005

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Section: Resultsmentioning

confidence: 99%

Interaction between the HCV NS3 protein and the host TBK1 protein leads to inhibition of cellular antiviral responses

et al. 2005

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“…All the H C V strains heretofore molecularly cloned have this structure in common in their NS3 region (Grakoui et al, 1993;Hijikata et al, 1993;Miller & Purcell, 1990;Pizzi et al, 1994). Many studies of cell-free transcription/translation of HCV cDNAs and their expression in cultured cells support this (Bartenschlager et al, 1993;Eckart et al, 1993;Grakoui et al, 1993;Hijikata et al, 1993;Tomei et al, 1993). It has been demonstrated that there are at least four cleavage events in HCV polyprotein processing by viral serine proteinase residing in the N-terminal third of NS3.…”

Section: Discussionmentioning

confidence: 99%

In vivo and in vitro trans-cleavage activity of hepatitis C virus serine proteinase expressed by recombinant baculoviruses

Suzuki¹,

Sato²,

Chieda³

et al. 1995

Journal of General Virology

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By the use of recombinant baculoviruses, the transcleavage of hepatitis C virus (HCV) non-structural polyprotein was studied. The viral serine proteinase encoded by the NS3 gene was expressed efficiently in insect cells infected with a baculovirus recombined with HCV cDNA corresponding to amino acids 1046-1243 and the signal sequence of the rabies virus G protein.Coinfection studies showed the in vivo trans-cleavage activity of the expressed protein by the use of a recombinant producing NS5 as a substrate. We also fou ad that the partially purified NS3 serine proteinase prepared from the recombinant-infected cells could cleave NS5A/5B substrate. Characterization of the proteinase obtained will provide basic knowledge on processing of the HCV polyprotein.

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“…Fax +44 181 633 3532. of serine proteases. Recombinant DNA clones coding for the non-structural proteins have been constructed and when translated the precursor protein is rapidly and efficiently cleaved into mature viral proteins both in vitro (Bartenschlager et al, 1993;Hijikata et al, 1993;D'Souza et aL, 1994) and in cellular systems (Eckart et al, 1993;Grakoui et al, 1993b). This processing was abolished by specific mutation of Ser-1165 in NS3, which supports a serine protease catalytic mechanism.…”

Section: Introductionmentioning

confidence: 99%

In vitro cleavage of hepatitis C virus polyprotein substrates by purified recombinant NS3 protease

D'Souza

Grace

Sangar

et al. 1995

Journal of General Virology

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The non-structural protein NS3 of hepatitis C virus has been expressed in bacteria as a polyhistidine fusion protein which can be produced in a soluble form and easily purified by affinity chromatography. Using an in vitro transcription and translation system we have been able to demonstrate that this protein can proteolytically process substrate molecules derived from the nonstructural region of the polyprotein. Using this assay system we have been able to optimize basic biochemical characteristics of the purified enzyme. Parallel experiments show that the full-length NS3 protein also possesses ATPase activity, indicating the bifunctional nature of the protein. In contrast, purified NS3 in which the predicted catalytic serine has been mutated loses protease but retains ATPase activity.

show abstract

The Hepatitis C Virus Encodes a Serine Protease Involved in Processing of the Putative Nonstructural Proteins from the Viral Polyprotein Precursor

Cited by 182 publications

References 0 publications

Interaction between the HCV NS3 protein and the host TBK1 protein leads to inhibition of cellular antiviral responses

Interaction between the HCV NS3 protein and the host TBK1 protein leads to inhibition of cellular antiviral responses

In vivo and in vitro trans-cleavage activity of hepatitis C virus serine proteinase expressed by recombinant baculoviruses

In vitro cleavage of hepatitis C virus polyprotein substrates by purified recombinant NS3 protease

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