C12N7/00

Methods of inactivation of viruses using n-methlyglucamide and its derivatives

This disclosure relates to methods for use in inactivating viruses. The methods of inactivating viruses with N-methylglucamides is applicable to the purification process of biologically-active drugs such as protein subunits, proteins (enzymes, factors, etc.), recombinant proteins, antibodies, vaccine or gene therapeutic products. The detergents used in this method are based on multiple N-methylglucamide homologs, consisting of a hydrophilic glucose moiety and hydrophobic fatty acid tail, linked by an amide bond. Additionally, these sugar-based detergents are nonionic by nature, which do not disrupt the drug protein, plasma biologies, non-enveloped viral vaccine or adeno associated viral particles. A method of purifying a biological product solution of interest having an unidentified enveloped virus contaminant, including incubating a biological product solution of interest with a standard solution, inactivating any potential enveloped virus contaminant present in the biological product solution of step (a), measuring the inactivated virus present in the final solution of step (b), incubating a separate biological product solution of interest with a N-methylglucamide solution, measuring the inactivated virus present in the final solution of step (d), and comparing the results of the final solutions of step (c) and step (e).

Methods of inactivation of viruses using n-methlyglucamide and its derivatives

This disclosure relates to methods for use in inactivating viruses. The methods of inactivating viruses with N-methylglucamides is applicable to the purification process of biologically-active drugs such as protein subunits, proteins (enzymes, factors, etc.), recombinant proteins, antibodies, vaccine or gene therapeutic products. The detergents used in this method are based on multiple N-methylglucamide homologs, consisting of a hydrophilic glucose moiety and hydrophobic fatty acid tail, linked by an amide bond. Additionally, these sugar-based detergents are nonionic by nature, which do not disrupt the drug protein, plasma biologies, non-enveloped viral vaccine or adeno associated viral particles. A method of purifying a biological product solution of interest having an unidentified enveloped virus contaminant, including incubating a biological product solution of interest with a standard solution, inactivating any potential enveloped virus contaminant present in the biological product solution of step (a), measuring the inactivated virus present in the final solution of step (b), incubating a separate biological product solution of interest with a N-methylglucamide solution, measuring the inactivated virus present in the final solution of step (d), and comparing the results of the final solutions of step (c) and step (e).

Stabilized RSV F proteins and uses thereof

The disclosure relates to stable RSV F proteins and immunogenic compositions containing the same, as well as methods of using the immunogenic compositions and compositions comprising the RSV F proteins.

Stabilized RSV F proteins and uses thereof

The disclosure relates to stable RSV F proteins and immunogenic compositions containing the same, as well as methods of using the immunogenic compositions and compositions comprising the RSV F proteins.

Intranasal vaccine that induces cellular immunity

The present invention provides a nanogel nasal vaccine that induces cell-mediated immunity. The present invention relates to a vaccine preparation comprising a complex of a nanogel, a vaccine antigen, and an adjuvant, wherein the vaccine preparation can efficiently induce the cell-mediated immunity, and can also induce a systemic and mucosal immune response.

Intranasal vaccine that induces cellular immunity

The present invention provides a nanogel nasal vaccine that induces cell-mediated immunity. The present invention relates to a vaccine preparation comprising a complex of a nanogel, a vaccine antigen, and an adjuvant, wherein the vaccine preparation can efficiently induce the cell-mediated immunity, and can also induce a systemic and mucosal immune response.

Expression of PEDV sequences in plants and plant produced vaccine for same

A plant produced vaccine for Porcine Epidemic Diarrhea Virus (PEDV) is provided where the Spike protein of the virus is expressed in a plant by introducing into a plant a construct comprising a promoter preferentially directing expression to seed of said plant, a nucleoic acid encoding the Spike protein and a nucleic acid targeting expression to the endoplasmic reticulum of the plant. The plant expresses the S1 polypeptide at levels of at least 10 mg/kg of seed of said plant. When orally administered to an animal, a protective response is observed including a serum antibody response.

Expression of PEDV sequences in plants and plant produced vaccine for same

A plant produced vaccine for Porcine Epidemic Diarrhea Virus (PEDV) is provided where the Spike protein of the virus is expressed in a plant by introducing into a plant a construct comprising a promoter preferentially directing expression to seed of said plant, a nucleoic acid encoding the Spike protein and a nucleic acid targeting expression to the endoplasmic reticulum of the plant. The plant expresses the S1 polypeptide at levels of at least 10 mg/kg of seed of said plant. When orally administered to an animal, a protective response is observed including a serum antibody response.

Scalable purification method for AAV1

A two-step chromatography purification scheme is described which selectively captures and isolates the genome-containing rAAV vector particles from the clarified, concentrated supernatant of a rAAV production cell culture. The process utilizes an affinity capture method performed at a high salt concentration followed by an anion exchange resin method performed at high pH to provide rAAV vector particles which are substantially free of rAAV intermediates.

Scalable purification method for AAV1

A two-step chromatography purification scheme is described which selectively captures and isolates the genome-containing rAAV vector particles from the clarified, concentrated supernatant of a rAAV production cell culture. The process utilizes an affinity capture method performed at a high salt concentration followed by an anion exchange resin method performed at high pH to provide rAAV vector particles which are substantially free of rAAV intermediates.