The present invention relates to compositions and methods for antibody-mediated therapy. In particular, provided herein are engineered immunoglobulins with altered half-life.

The present invention relates to glycosylated immunoglobulin variable domains, and in particular to glycosylated immunoglobulin single variable domains (the latter also being referred to herein by means of the abbreviation “ISF” or “ISVD”). The present invention relates to glycosylated immunoglobulin heavy-chain variable domains (also referred to herein as “VH domains”), and in particular to glycosylated immunoglobulin heavy-chain ISVD's. The invention in particular relates to immunoglobulin (single) variable domains that are glycosylated in such a way that the binding of said immunoglobulin (single) variable domains by so-called “pre-existing antibodies” is prevented and/or reduced (i.e. partially or essentially completely) compared to the same immunoglobulin (single) variable domain without the glycosylation of the invention being present. For example, the present invention relates to heavy-chain immunoglobulin variable domain, which contains a glycosylation site such that the amino acid residue at one of positions 10, 11, 12, 13, 14, 39, 40, 41, 42, 87, 89, 108, 110, 112, 113 or 114, and in particular one of positions 11, 13, 87, 89, 108, 110, 112, 113 or 114 (numbering according to Kabat) is or can be glycosylated.

The present invention provides molecules, including proteins, more particularly, immunoglobulins whose in vivo half-lives are altered (increased or decreased) by the presence of an IgG constant domain, or FcRn binding fragment thereof (e.g., an Fc region or hinge-Fc region) (e.g., from a human IgG, e.g., human IgG1), that have modifications of one or more of amino acid residues in at least the CH3 domain.

An immunogenic fusion protein for use as a mucosal vaccine is provided, which includes: i) one or more FcyR1-binding domains; ii) one or more antigens from one or more infectious disease organisms; and iii) one or more FcRn-binding domains.

The present invention is directed to molecules (e.g., an antibody, a diabody, an scFv, an antibody, a TandAb, etc.) capable of binding an epitope of human CD16 (a “CD16 Binding Molecule”). The present invention is further directed to CD 16 Binding Molecules that are capable of binding an epitope of human CD16 and one or more epitope(s) of a Disease Antigen (“DA”) (e.g., a “CD16×DA Binding Molecule”). The present invention is particularly directed to such CD16×DA Binding Molecules that are antibodies, or that comprise an Epitope Binding Domain thereof, or are diabodies (including DART® diabodies), bispecific antibodies, TandAbs, other multispecific binding molecules (e.g., trivalent TRIDENT™ molecules), etc. The invention particularly concerns CD16×DA Binding Molecules that are capable of binding a Disease Antigen that is a Cancer Antigen or a Pathogen-Associated Antigen in addition to being able to bind CD 16. The invention particularly concerns the use of such CD16 and CD16×DA Binding Molecules in the treatment of cancer and pathogen-associated diseases. The present invention is also directed to pharmaceutical compositions that comprise such molecule(s).

Disclosed is an antibody that selectively binds CD47 on tumor cells. Also disclosed is a method for treating cancer in a subject, comprising administering to the subject an effective amount of the antibody disclosed.

Provided are CD19 binding molecules, including anti-CD19 antibodies, including antibody fragments such as single-chain fragments, and chimeric receptors including the antibodies, such as chimeric antigen receptors (CARs). Among the antibodies are human antibodies, including those that compete for binding to CD19 with reference antibodies, such as murine antibodies. In some embodiments, the antibodies display similar functional properties to the reference antibodies, such as comparable binding affinities and/or competitive inhibition properties. Also provided are genetically engineered cells expressing the chimeric receptors, and uses of the binding molecules and cells adoptive cell therapy.

Provided are compositions for increasing the half-life of a polypeptide or polypeptides in a canine and methods of their use. The compositions involve variant canine IgG Fc regions.

The present invention relates to immunoglobulins that bind FcγRIIb+ cells and coengage the antigen on the cell's surface and an FcγRIIb on the cell's surface, methods for their generation, and methods for using the immunoglobulins.

The present disclosure provides binding proteins (e.g., antibodies or antigen binding fragments thereof) that specifically bind to Klebsiella pneumoniae O2 and induce opsonophagocytic killing of Klebsiella (e.g., Klebsiella pneumoniae) and/or protects mice from a lethal Klebsiella challenge. The present disclosure also provides methods of reducing Klebsiella (e.g., Klebsiella pneumoniae) or treating or preventing Klebsiella (e.g., Klebsiella pneumoniae) infection in a subject comprising administering the Klebsiella pneumoniae O2 binding proteins, (e.g., antibodies or antigen-binding fragments thereof) to the subject.