Nonstructural protein C

Peste-des-petits ruminants (PPR) is an economically devastating viral disease of sheep and goats. In the present study, we have evaluated the reactivity profile of the recombinant non-structural protein C of PPR virus with vaccinated and convalescent goat sera in an indirect ELISA. The antibody against this protein is getting produced in both vaccinated as well as in convalescent animals.

6p kethamoi4 16-04-2020 9 1   Download

Peste-des-petits-ruminants (PPR) is a transboundary viral disease of small ruminants. In the present study, the full length C gene was amplified from PPR vaccine virus (Sungri/96) and expressed in a prokaryotic expression system. Specificity of the recombinant C protein was confirmed through immune-blot using anti-His conjugate and hyperimmune sera from goats. The immunogenicity of the protein was assessed using monospecific sera raised in goats. The recombinant C protein produced in this study will be useful for the development of DIVA enabled vaccine and diagnostics.

6p kethamoi4 16-04-2020 5 1   Download

All-oral combination of direct-acting antivirals could lead to higher sustained virologic response (SVR) in hepatitis C virus (HCV)-infected patients. In the present study, we examined the efficacy and safety of the dual oral treatment with HCV nonstructural protein (NS) 5A inhibitor daclatasvir (DCV) plus HCV NS3/4A inhibitor asunaprevir (ASV) for 24 weeks in real-world HCV genotype 1-infected Japanese individuals.

6p viwashington2711 04-12-2019 8 0   Download

Classical swine fever virus nonstructural protein 5B (NS5B) encodes an RNA-dependent RNA polymerase, a key enzyme of the viral replication complex. To better under-stand the initiation of viral RNA synthesis and to establish anin vitroreplication system, a recombinant NS5B protein, lacking the C-terminal 24-amino acid hydrophobic domain, was expressed inEscherichia coli.

10p fptmusic 12-04-2013 45 2   Download

This study of the full-length bifunctional nonstructural protein 3 from hep-atitis C virus (HCV) has revealed that residues in the helicase domain affect the inhibition of the protease. Two residues (Q526 and H528), appar-ently located in the interface between the S2 and S4 binding pockets of the substrate binding site of the protease, were selected for modification, and three enzyme variants (Q526A, H528A and H528S) were expressed, puri-fied and characterized.

8p media19 05-03-2013 33 3   Download

Since the discovery of hepatitis C virus (HCV) in 1989, there has been an explosion of research and information on the virus. This is evidenced by the more than 20 000 papers onHCV(as of December, 2000), as well as the numerous reviews in journals and edited books. The purpose of this book is to present an overview of the diVerent disciplines that have contributed to an understanding of the virus, its diseases, current and proposed treatments, and much more.

272p gian_anh 18-10-2012 49 6   Download