This application is directed generally to foot-and-mouth disease virus (FMDV) 3C proteases that have been modified by mutating a polynucleotide sequence coding for the FMDV 3C protease. The modified FMDV proteases exhibit proteolytic activity on FMDV P 1 precursor protein and exhibit a reduction in one or more toxic or inhibitory properties associated with an unmodified FMDV 3C protease on a host cell used to recombinantly produce it. Vectors carrying polynucleotides encoding modified FMDV 3C protease sequences can induce production of FMDV virus-like particles in a host cell when expressed in the host cell. The modified FMDV 3C proteases can generally be used to produce immunogenic FMDV preparations capable of inducing an immune response against FMDV.

This application is directed generally to foot-and-mouth disease virus (FMDV) 3C proteases that have been modified by mutating a polynucleotide sequence coding for the FMDV 3C protease. The modified FMDV proteases exhibit proteolytic activity on FMDV P1 precursor protein and exhibit a reduction in one or more toxic or inhibitory properties associated with an unmodified FMDV 3C protease on a host cell used to recombinantly produce it. Vectors carrying polynucleotides encoding modified FMDV 3C protease sequences can induce production of FMDV virus-like particles in a host cell when expressed in the host cell. The modified FMDV 3C proteases can generally be used to produce immunogenic FMDV preparations capable of inducing an immune response against FMDV.

Polynucleotide constructs that express an engineered foot-and-mouth disease (FMDV) P1 precursor protein and a non-FMDV TEV protease and methods for safe and efficient recombinant production of FMDV antigens and immunogens. Recombinant production of FMDV antigens avoids the need to culture highly-infectious FMDV, while conventional culture methods for producing FMDV antigens rely on the native FMDV 3C protease which exerts toxic effects on host cells. The inventors have developed a new system that efficiently and safely processes FMDV P1 precursor without the FMDV 3C protease, thus avoiding the toxic effects associated with use of the 3C protease. The invention is also directed to the FMDV antigens and virus-like particles produced by this system as well as to FMDV vaccines, diagnostics and other biologics.

Polynucleotide constructs that express an engineered foot-and-mouth disease (FMDV) P1 precursor protein and a non-FMDV TEV protease and methods for safe and efficient recombinant production of FMDV antigens and immunogens. Recombinant production of FMDV antigens avoids the need to culture highly-infectious FMDV, while conventional culture methods for producing FMDV antigens rely on the native FMDV 3C protease which exerts toxic effects on host cells. The inventors have developed a new system that efficiently and safely processes FMDV P1 precursor without the FMDV 3C protease, thus avoiding the toxic effects associated with use of the 3C protease. The invention is also directed to the FMDV antigens and virus-like particles produced by this system as well as to FMDV vaccines, diagnostics and other biologics.

The present invention relates to the stabilization of foot-and-mouth disease virus (FMDV) capsids, by specific substitution of amino acids in a specific region of FMDV VP2. The invention provides stabilized FMDV capsids and vaccines against FMD.

The present invention relates to the stabilisation of foot-and-mouth disease virus (FMDV) capsids, by specific substitution of amino acids in a specific region of FMDV VP2. The invention provides stabilised FMDV capsids and vaccines against FMD.

Foot-and-mouth disease virus like particles, the particles including a structural protein VP0, a structural protein VP1 including a mineralization peptide, a structural protein VP3, and a calcium phosphate coat. The structural protein VP1 including a mineralization peptide is encoded by a gene sequence represented by SEQ ID NO. 7, SEQ ID NO. 8 or SEQ ID NO. 9. The structural protein VP0 is encoded by a gene sequence represented by SEQ ID NO. 2. The structural protein VP3 is encoded by a gene sequence represented by SEQ ID NO. 3. The calcium phosphate coat covers the structural protein VP0, the structural protein VP1 including a mineralization peptide, and the structural protein VP3.

The present disclosure encompasses canine parvovirus (CPV) vaccines or compositions. The vaccine or composition may be a vaccine or composition containing CPV virus-like particle (VLP), and a preparation method and a use thereof. The CPV VLPs are formed by the CPV VP2 protein. Further, the disclosure broadly encompasses vaccines comprising combinations of MLV and VLP, which are capable of overcoming MDA against a variety of pathogens, which infect a variety of different species.

A vaccine composition is disclosed. The vaccine composition comprises: (a) a therapeutically effective amount of an influenza virus-like particle (VLP) comprising: (i) influenza M1, influenza M2, influenza hemagglutinin (HA), and influenza neuraminidase (NA) proteins; (b) Foot-and-mouth disease virus (FMDV) capsid protein VP3, recombinant FMDV VP3 (rVP3), VP3 peptide, or SUMO VP3; and (c) alum. Also disclosed is use of a vaccine composition according to the invention in the manufacture of a medicament for inducing an immunogenic response in a subject in need thereof.

This application is directed generally to minicircle DNA vectors for the vaccination of foot-and-mouth disease (FMD). The transgene expression cassette in the minicircle DNA vector includes: a eukaryotic translation initiation nucleotide sequence, a mutant nucleotide sequence that encodes a foot-and-mouth disease virus (FMDV) capsid polyprotein precursor that contains at least one mutation to eliminate a restriction enzyme recognition site, a nucleotide sequence that encodes a protease that cleaves the FMDV capsid polyprotein precursor into a plurality of FMDV capsid proteins and a translational regulatory element to regulate the expression of the protease. The minicircle DNA vectors can be transfected directly into the cell of a mammalian host. When transfected into the mammalian host cell, virus-like particles can be produced intrinsically to stimulate the mammalian host's immune system to develop adaptive immunity toward foot-and-mouth disease.