Provided herein is a human monoclonal antibody 8D6 against hepatitis C virus (HCV) infection. The antibody binds to the E2 subunit of HCV capsid protein, and can prevent HCV from infecting susceptible host cells. By using the antibody variable region gene or the complementary determining region (CDR) gene, different forms of genetic engineering antibodies have been transformed and produced in any expression system of the prokaryotic and eukaryotic cells as therapeutics to prevent or treat HCV infection.

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 present disclosure provides methods, kits, and compositions for detecting subject anti-HCV antibodies in a sample using NS3 capture peptides. In certain embodiments, at least two NS3 helicase (NS3h) capture peptides and at least two conjugate peptides (e.g., NS3h conjugate peptides) are employed together, which allows for a broad dynamic range of subject antibody detection in a one-step type assay. In other embodiments, methods are provided of detecting NS3-specific subject antibodies without the use of a reducing agent. In some embodiments, NS3-specific subject antibodies are detected with a double shot of NS3 conjugate peptide (e.g., conjugate peptide added to a sample both before and after washing).

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.

Disclosed herein are recombinant baculoviruses suitable for detecting the presence of arthropod-borne viruses in a biological sample of a test subject. The information derived from the detection may also be used to render a diagnosis on whether the test subject is infected with the arthropod-borne viruses or not, so that proper course of treatment may be assigned to the subject.

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.

Disclosed herein are recombinant baculoviruses suitable for detecting the presence of arthropod-borne viruses in a biological sample of a test subject. The information derived from the detection may also be used to render a diagnosis on whether the test subject is infected with the arthropod-borne viruses or not, so that proper course of treatment may be assigned to the subject.

The present invention relates to measurement of immunological parameters as a means to predict time-to-viral clearance in patients with chronic Hepatitis C Virus (HCV) infection under direct acting antiviral (DAA) therapy. The present invention provides a principle and methods for stratifying individuals into suitable treatment groups and personalized methods of treatment for such individuals.

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.

The present disclosure provides detection methods employing HCV core lipid binding domain and DNA binding domain monoclonal antibodies. In certain embodiments, the lipid binding domain monoclonal antibody recognizes an epitope in amino acids 141 to 161 of HCV core protein.