Vaccines, methods of producing, and methods of using are provided in which a protective response to Valley Fever disease is produced when administered to an animal. The vaccine provides for expression of Coccidioides sp. Ag2 polypeptide in a plant or plant part, linked to a promoter preferentially directing expression to seed tissue of the plant or plant part. Further embodiments provide the polypeptide is targeted to the cell wall, vacuole or endoplasmic reticulum. The polypeptide may be fused to a dendritic cell targeting dendritic cell or a heat labile enterotoxin. Increased expression levels in the plant or plant part are obtained. The vaccine comprising the plant-produced Ag2 polypeptide may be a glucan chitin particle comprising the Ag2 polypeptide. The plant or plant materials in an embodiment may be orally administered.

The present invention encompasses NDV vaccines. The vaccine may be a subunit vaccine based on HN of NDV. The NDV HN may be expressed in plants or algae including microalgae. The invention also encompasses recombinant vectors encoding and expressing NDV antigens, epitopes or immunogens which can be used to protect animals against NDV. It encompasses also a vaccination regime compatible with the DIVA strategy, including a prime-boost scheme using viral vector or inactivated vaccines and subunit vaccines.

The present invention provides edible vaccines comprising transgenic microalgae expressing at least one exogenous antigen or an intervening organism comprising the transgenic microalgae. The antigen expressing microalgae are used for oral delivery of the antigen to a target organism in its intact and functional form. The exogenous antigen, expressed in the microalgae, is characterized by exerting at least one immunogenic response in the subject consuming the vaccine.

Methods of vaccination of animals are provided. In an embodiment, a paired administration of a primer vaccine provides for non-oral administration of a vaccine and an oral administration of the vaccine and can be followed by a paired administration of a booster vaccine of a non-oral administration and an oral administration. Embodiments provide the non-oral and oral administration are within three days of each other. The methods provide for improved protective response in an animal compared to administration of a primer non-oral administered vaccine followed by three booster non-oral administered vaccines. An adjuvant is provided that is a microcrystalline polysaccharide-based adjuvant derived from delta inulin.

Vaccines, methods of producing, and methods of using are provided in which a protective response to Valley Fever disease is produced when administered to an animal. The vaccine provides for expression of Coccidioides sp. Ag2 polypeptide in a plant or plant part, linked to a promoter preferentially directing expression to seed tissue of the plant or plant part. Further embodiments provide the polypeptide is targeted to the cell wall, vacuole or endoplasmic reticulum. The polypeptide may be fused to a dendritic cell targeting dendritic cell or a heat labile enterotoxin. Increased expression levels in the plant or plant part are obtained. The vaccine comprising the plant-produced Ag2 polypeptide may be a glucan chitin particle comprising the Ag2 polypeptide. The plant or plant materials in an embodiment may be orally administered.

Provided are an NKG2A-targeting antibody, and a multispecific antibody, a chimeric receptor, an antibody conjugate, a pharmaceutical composition and a kit which comprise same, and the use thereof in the diagnosis/treatment/prevention of diseases associated with NKG2A expression.

Provided are edible vaccines including transgenic microalgae expressing at least one exogenous antigen or an intervening organism including the transgenic microalgae. The antigen expressing microalgae are used for oral delivery of the antigen to a target organism in its intact and functional form. The exogenous antigen, expressed in the microalgae, is characterized by exerting at least one immunogenic response in the subject consuming the vaccine.

The present disclosure relates to single domain antibodies (VHHs) against SARS-CoV-2, as well as to polypeptides comprising one or more of such VHHs. The disclosure also relates to nucleic acids encoding such VHHs and polypeptides; to methods of preparing such VHHs and polypeptides; to host cells expressing or capable of expressing such VHHs or polypeptides; to compositions comprising such VHHs, polypeptides, nucleic acids or host cells; and to uses of such VHHs, such polypeptides, such nucleic acids, such host cells or such compositions, in particular for prophylactic, therapeutic or diagnostic purposes.

A recombinant vector for transforming a plant, a plant transformed with the recombinant vector, a plant-made classical swine fever virus antigen pmE2 protein expressed in the plant and uses thereof is provided. By using a recombinant vector having a polynucleotide encoding a GP55 protein of CSFV according to the present invention; and a polynucleotide encoding a cellulose-binding domain protein; and a plant transformed with the recombinant vector, a plant-made classical swine fever virus antigen pmE2 protein may be produced with high efficiency, and has higher safety and stability than those achieved by other production methods. Also, since the plant-derived classical swine fever virus antigen protein pmE2 has a cellulose-binding domain (CBD) protein, it may be usefully used as an effective marker to determine a virus exposure pathway and an antibody producing pathway.

Increased antigenicity of a membrane-bound polypeptide produced from a plant is provided in a process in which extraction of the polypeptide or other compounds from the plant is such that phospholipids are associated with the polypeptide. Reducing fat by supercritical fluid extraction increases antigenicity of such plant-produced membrane-bound polypeptides. Methods and means of producing such membrane-bound polypeptides are provided. Methods to produce a protective response in animals are provided by administering to the animal the membrane-bound polypeptide. Binding of antibody specific to the membrane-bound polypeptide is increased. The process provides for increased preferred formation of the membrane-bound polypeptide. Stability of the membrane-bound polypeptide is increased when the plant material is defatted.