Mosquito defensin facilitates Japanese encephalitis virus infection by downregulating the C6/36 cell-surface antiviral protein HSC70B.

Japanese encephalitis virus (JEV) is a viral zoonosis that can cause viral encephalitis, death and disability whose primary vector is the Culex mosquito. Viral infection induces a series of antimicrobial peptide responses in mosquitoes, and the effector defensin enhances JEV replication in mosquitoes. However, the underlying mechanisms by which defensin enhances JEV are not fully understood.

Inactivated vaccine with adjuvants consisting of pattern recognition receptor agonists confers protection against avian influenza viruses in chickens.

Use of adjuvant containing pathogen pattern recognition receptor agonists is one of the effective strategies to enhance the efficacy of licensed vaccines. In this study, we investigated the efficacy of avian influenza vaccines containing an adjuvant (CVCVA5) which was composed of polyriboinosinic polyribocytidylic, resiquimod, imiquimod, muramyl dipeptide and levomisole. Avian influenza vaccines adjuvanted with CVCVA5 were found to induce significantly higher titers of hemagglutiniton inhibition antibodies (P≤0.

Chimaeric VP2 proteins from infectious bursal disease virus containing the N-terminal M2e of H9 subtype avian influenza virus induce neutralizing antibody responses to both viruses.

Subunit vaccines capable of inducing antibody against both infectious bursal disease virus (IBDV) and H9 subtype avian influenza virus (AIV) were developed. The VP2 protein of IBDV was used as a cargo protein to display a 12-amino-acid immunodominant epitope derived from the N-terminal M2 extracellular domain (nM2e) of the H9 subtype AIV. Two chimaeric proteins were constructed by insertion of one copy of the nM2e into the PBC region (VP2BCnM2e(H9)) or by fusing four copies of nM2e to the carboxyl terminal (VP2-4nM2e(H9)) of VP2.

Antiviral activity of rChIFN-α against vesicular stomatitis virus and Newcastle disease virus: a novel recombinant chicken interferon-α showed high antiviral activity.

The sequences of 27 chicken interferon-alpha (ChIFN-α) genes were obtained from GenBank. The gene sequences were compared and homology between them was determined by using a bio-software. On the basis of these results, a new rChIFN-α peptide sequence with 194 amino acids was assembled.