Peptide inhibitors of activation of hepatitis C virus (HCV) NS3 protease are disclosed. They are analogs of the activation peptide HCV NS4 of residues 21-33 of SEQ ID NO: 2 and contain non-proteinogenic amino acids. Competitive binding studies showed the peptide analogs bind HCV NS3 protease at the activation site.

Peptide inhibitors of activation of hepatitis C virus (HCV) NS3 protease are disclosed. They are analogs of the activation peptide HCV NS4 of residues 21-33 of SEQ ID NO: 2 and contain non-proteinogenic amino acids. Competitive binding studies showed the peptide analogs bind HCV NS3 protease at the activation site.

The technology described herein is directed to CAR polypeptides and systems comprising repressible proteases. In combination with a specific protease inhibitor, the activity of said CAR polypeptides and systems and cells comprising them can be modulated. Also described herein are methods of using said CAR polypeptides and systems, for example to treat various diseases and disorders.

Modified hepatitis C virus polypeptides are described. The polypeptides include the HCV NS4a domain and modified NS3 domain. The polypeptides retain conformational epitopes. HCV immunoassays including the polypeptides are also described.

The present disclosure relates to constructs useful in expressing biotinylated monomers and tetramers produced from these monomers. Specifically, the disclosure provides a construct useful in expressing biotinylated antigen monomers, said construct comprising a viral protein of an ectodomain of Hepatitis C Virus (HCV) envelope glycoprotein E2 or Human Immunodeficiency Virus (HIV) gp140. Further disclosed are methods for production and use of these tetramers in identifying and isolating antigen specific B cells and cloning antibodies thereto.

The present application relates to novel administration regimens for poxviral vectors comprising nucleic acid constructs encoding antigenic proteins and invariant chains. In particular the use of said poxviral vectors for priming or for boosting an immune response is disclosed.

The disclosure relates to a multi-epitope fusion protein as well as to its use as calibrator and/or control in an in vitro diagnostics immunoassay for detecting HCV core antigen. The multi-epitope fusion protein has two to six different non-overlapping linear peptides present in the amino acid sequence of hepatitis C virus (HCV) core protein, wherein each of the peptides is separated from the other peptides by a spacer consisting of a non-HCV amino acid sequence and having a chaperone amino acid sequence. No further HCV specific amino acid sequences are present in the polypeptide. A further aspect relates to a reagent kit for detecting HCV core antigen containing said multi-epitope fusion protein as calibrator or control or both.

Modified non-human mammalian hepatoma cell lines that express hepatitis C virus (HCV) antigens and which are capable of generating tumours in a syngeneic animal model are provided. The cell lines are generated by genomic integration of an expression construct that comprises one or more HCV antigen-encoding sequences under the control of a constitutive promoter. The expression construct further comprises a selectable marker and a reporter gene under the control of the same promoter. The cell lines are useful for testing prophylactic and therapeutic vaccines against HCV either in vitro or in vivo.

Provided is an antigen fused with a porcine Fc fragment, a vaccine composition having a self-adjuvanting effect by binding an Fc fragment to various antigens, and a method of producing the antigen.

Provided is a recombinant vector including a porcine Fc fragment. By fusing the porcine Fc fragment with various target proteins by using the recombinant vector of the present invention, not only target proteins may be expressed using various hosts including plants, but the productivity and stability of target proteins may also be increased.