Ns5b Hcv Region
Mostrando 13-24 de 71 artigos, teses e dissertações.
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13. Oligomerization and Cooperative RNA Synthesis Activity of Hepatitis C Virus RNA-Dependent RNA Polymerase
The NS5B RNA-dependent RNA polymerase encoded by hepatitis C virus (HCV) plays a key role in viral replication. Reported here is evidence that HCV NS5B polymerase acts as a functional oligomer. Oligomerization of HCV NS5B protein was demonstrated by gel filtration, chemical cross-linking, temperature sensitivity, and yeast cell two-hybrid analysis. Mutagenes
American Society for Microbiology.
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14. Hepatitis C virus NS3 serine proteinase: trans-cleavage requirements and processing kinetics.
The hepatitis C virus H strain (HCV-H) polyprotein is cleaved to produce at least 10 distinct products, in the order of NH2-C-E1-E2-p7-NS2-NS3-NS4A-NS4B-NS5A-NS5B -COOH. An HCV-encoded serine proteinase activity in NS3 is required for cleavage at four sites in the nonstructural region (3/4A, 4A/4B, 4B/5A, and 5A/5B). In this report, the HCV-H serine proteina
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15. Comparison of full-length sequences of interferon-sensitive and resistant hepatitis C virus 1b. Sensitivity to interferon is conferred by amino acid substitutions in the NS5A region.
We have previously demonstrated that sensitivity to interferon is different among hepatitis C virus (HCV) quasispecies simultaneously detected in same individuals and that interferon-resistant HCV quasispecies are selected during the treatment. To determine the genetic basis of their resistance to interferon, HCV genotype-1b was obtained from serum of three
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16. Evidence of subtype-specific antibodies to antigenic epitopes in the NS5 region of hepatitis C virus in the circulation of patients with chronic hepatitis C.
The antigenicity of the NS5 region of type 1 hepatitis C virus (HCV) was investigated by epitope mapping of the region spanning amino acids 2530 to 2723 of the HCV polyprotein. Six antigenic regions were recognized by anti-HCV positive sera from individuals with chronic hepatitis C in a modified enzyme-linked immunosorbent assay with synthetic oligopeptides.
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17. Hepatitis C virus (HCV) subtype prevalence in Chiang Mai, Thailand, and identification of novel subtypes of HCV major type 6.
Subtype analysis of hepatitis C viruses (HCVs) obtained from patients with chronic liver disease in Chiang Mai, Thailand, was performed. Of 46 HCV isolates, 13 (28%) were shown to belong to HCV subtype 3a (HCV-3a), 10 (22%) to belong to HCV-1a, 7 (15%) to belong to HCV-1b, 1 (2%) to belong to HCV-3b, and 1 (2%) to belong to a variant group, as determined fro
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18. Antigenic structure of the complete nonstructural (NS) 2 and 5 proteins of hepatitis C virus (HCV): anti-HCV NS2 and NS5 antibody reactivities in relation to HCV serotype, presence of HCV RNA, and acute HCV infection.
Antigenic regions within the nonstructural (NS) 2 and 5 proteins of hepatitis C virus (HCV) were identified and characterized by the use of 127 overlapping synthetic peptides and a serum panel consisting of 167 human serum samples from persons with antibodies to HCV. Initially, 20 anti-HCV-positive serum samples were used to screen the peptides covering the
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19. Hepatitis C Virus Genotyping: Interrogation of the 5′ Untranslated Region Cannot Accurately Distinguish Genotypes 1a and 1b
Although the 5′ untranslated region (5′ UTR) is the most conserved region of the hepatitis C virus (HCV) genome, it has been suggested that interrogation of this region is sufficient for determination of the HCV genotype. We compared two methods of determination of the HCV genotype: (i) direct sequencing of the DNA of the NS-5b region and (ii) reverse li
American Society for Microbiology.
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20. Cellular RNA Helicase p68 Relocalization and Interaction with the Hepatitis C Virus (HCV) NS5B Protein and the Potential Role of p68 in HCV RNA Replication
Chronic infection by hepatitis C virus (HCV) can lead to severe hepatitis and cirrhosis and is closely associated with hepatocellular carcinoma. The replication cycle of HCV is poorly understood but is likely to involve interaction with host factors. In this report, we show that NS5B, the HCV RNA-dependent RNA polymerase (RdRp), interacts with a human RNA he
American Society for Microbiology.
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21. Comparison of Hepatitis C Virus NS5b and 5′ Noncoding Gene Sequencing Methods in a Multicenter Study
A national evaluation study was performed in 11 specialized laboratories with the objective of assessing their capacities to genotype hepatitis C virus (HCV) and define the applicability of a given genotyping method. The panel consisted of 14 samples positive for HCV RNA of different genotypes (including 3 samples with two different artificially mixed genoty
American Society for Microbiology.
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22. Template Requirements for De Novo RNA Synthesis by Hepatitis C Virus Nonstructural Protein 5B Polymerase on the Viral X RNA
The hepatitis C virus (HCV)-encoded NS5B protein is an RNA-dependent RNA polymerase which plays a substantial role in viral replication. We expressed and purified the recombinant NS5B of an HCV genotype 3a from Esherichia coli, and we investigated its ability to bind to the viral RNA and its enzymatic activity. The results presented here demonstrate that NS5
American Society for Microbiology.
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23. Clinical Evaluation of Two Methods for Genotyping Hepatitis C Virus Based on Analysis of the 5′ Noncoding Region
We compared the performance characteristics of a standardized direct sequencing method (TRUGENE HCV 5′NC; Visible Genetics Inc., Toronto, Ontario, Canada) and a reverse hybridization line probe assay (INNO-LiPA HCV II; Bayer Corp., Tarrytown, N.Y.) for genotyping of hepatitis C virus (HCV). Both methods are based on detection of sequence heterogeneity in t
American Society for Microbiology.
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24. Characterization of the hepatitis C virus-encoded serine proteinase: determination of proteinase-dependent polyprotein cleavage sites.
Processing of the hepatitis C virus (HCV) H strain polyprotein yields at least nine distinct cleavage products: NH2-C-E1-E2-NS2-NS3-NS4A-NS4B-NS5A-NS5B-CO OH. As described in this report, site-directed mutagenesis and transient expression analyses were used to study the role of a putative serine proteinase domain, located in the N-terminal one-third of the N