The present invention regards a new and Improved HVT-vectored ND-IBD vaccine, comprising a recombinant HVT comprising the VP2 gene from IBDV and the F gene from NDV to a target animal. The recombinant HVT can be used in a vaccine for poultry, which displayed good viral vector replication, effective expression of the NDV F—and IBDV VP2 genes, improved immunoprotection against ND and IBD, and improved genetic stability over prior art constructs.

The present invention relates to vaccine compositions that are useful in a method of protecting a human subject against dengue disease.

Provided herein are immunogenic compositions comprising a recombinant modified vaccinia virus Ankara (MVA) comprising a nucleic acid sequence encoding a flagellin, and a nucleic acid sequence encoding a heterologous disease-associated antigen, wherein the immunogenic composition induces increased T-cell and antibody mediated immune responses specific for the heterologous disease-associated antigen when administered to a subject, e.g. a human subject, and related methods and uses.

Provided herein are immunogenic compositions comprising a recombinant modified vaccinia virus Ankara (MVA) comprising a nucleic acid sequence encoding a flagellin, and a nucleic acid sequence encoding a heterologous disease-associated antigen, wherein the immunogenic composition induces increased T-cell and antibody mediated immune responses specific for the heterologous disease-associated antigen when administered to a subject, e.g. a human subject, and related methods and uses.

In one aspect, the invention relates to a composition including a first polypeptide having the sequence set forth in SEQ ID NO: 1 and a second polypeptide having the sequence set forth in SEQ ID NO: 2. In one embodiment, the composition includes about 120 μg/ml of a first polypeptide including the amino acid sequence set forth in SEQ ID NO: 1, 120 μg/ml of a second polypeptide including the amino acid sequence set forth in SEQ ID NO: 2, about 2.8 molar ratio polysorbate-80 to the first polypeptide, about 2.8 molar ratio polysorbate-80 to the second polypeptide, about 0.5 mg/ml aluminum, about 10 mM histidine, and about 150 mM sodium chloride. In one embodiment, a dose of the composition is about 0.5 ml in total volume. In one embodiment, two-doses of the composition induce a bactericidal titer against diverse heterologous subfamily A and subfamily B strains in a human.

In one aspect, the invention relates to a composition including a first polypeptide having the sequence set forth in SEQ ID NO: 1 and a second polypeptide having the sequence set forth in SEQ ID NO: 2. In one embodiment, the composition includes about 120 μg/ml of a first polypeptide including the amino acid sequence set forth in SEQ ID NO: 1, 120 μg/ml of a second polypeptide including the amino acid sequence set forth in SEQ ID NO: 2, about 2.8 molar ratio polysorbate-80 to the first polypeptide, about 2.8 molar ratio polysorbate-80 to the second polypeptide, about 0.5 mg/ml aluminum, about 10 mM histidine, and about 150 mM sodium chloride. In one embodiment, a dose of the composition is about 0.5 ml in total volume. In one embodiment, two-doses of the composition induce a bactericidal titer against diverse heterologous subfamily A and subfamily B strains in a human.

A vaccine composition for birds comprising as an active ingredient a structure containing O-antigen derived from Gram-negative bacteria, provided that said structure does not contain a whole cell, and a process for preparing the same are provided. By using a structure containing O-antigen (e.g. lipopolysaccharide) derived from Gram-negative bacteria as an active ingredient in accordance with the present invention, alleviation of inoculation reaction and reduction in an amount of injection are attained as compared to the conventional whole-cells vaccine to thereby allow for the increase in the number of other antigens to be mixed therewith.

In this application is described a method for preparing nano-VLP composition, thereby permitting purification using chromatography and filtration. The nano-VLP composition has a more uniform size range of filovirus particles, roughly 230 nm diameter, allowing ease of manipulation of the composition, while retaining GP conformational integrity and the antigenic effectiveness of the vaccine. Additionally, the nano-VLP can be lyophilized without loss of nano-VLP structure, or GP immunogenicity. Lyophilized nano-VLP have greatly enhanced thermostability, allowing the creation of a filovirus nano-VLP vaccine without a cold chain requirement.

In this application is described a method for preparing nano-VLP composition, thereby permitting purification using chromatography and filtration. The nano-VLP composition has a more uniform size range of filovirus particles, roughly 230 nm diameter, allowing ease of manipulation of the composition, while retaining GP conformational integrity and the antigenic effectiveness of the vaccine. Additionally, the nano-VLP can be lyophilized without loss of nano-VLP structure, or GP immunogenicity. Lyophilized nano-VLP have greatly enhanced thermostability, allowing the creation of a filovirus nano-VLP vaccine without a cold chain requirement.

The invention provides a recombinant polypeptide comprising the EDIII domain of each of Dengue virus serotype DENV-1, DENV-2, DENV-3, and DENV-4 linked to the N-terminal of HBsAg.