The present disclosure relates to the pharmaceutical field. More specifically, it relates to methods for treating a tumor in a human subject in need thereof, said method comprising administering a therapeutically efficient amount of an anti-BTN3A antibody which induces the activation of Vγ9Vδ2 T cells, in combination with a therapeutically efficient amount of an anti-PD1/PDL1 treatment, wherein said subject is having relapsed or refractory tumors to anti-PD1/PDL1 treatment.

The present describes monoclonal antibody to MUC1*.

The invention described herein provides neutralizing antibodies against SARS-CoV-2 antigens (such as the S1 subunit of the S antigen) for use in treating human patients having COVID-19.

This disclosure provides compositions and methods for delivering a viral composition to cells, e.g., for cell surface receptor-mediated uptake, and enhanced viral transduction. Viral transduction can be achieved via a bifunctional bridging composition that includes a moiety that binds to a cell surface receptor ligand and a linked bridging moiety that binds to a viral composition. Also provided are modified viral compositions comprising a bridging composition specifically bound via its bridging moiety to the viral composition. Modified viral compositions and methods for reducing levels or titers of neutralizing antibodies in a subject in need of viral therapy, e.g., gene therapy, are provided. In some embodiments, the modified viral composition includes empty viral particles that bind and internalize neutralizing autoantibodies. Modified viral compositions including empty viral particles can be administered prior to viral therapy. Also provided are pharmaceutical compositions and kits including a bifunctional bridging composition and/or modified viral compositions.

The invention relates to multispecific antibody constructs comprising Fab fragments having a particular set of mutations at the interface of the CH1 and CL domains, the mutations preventing heavy chain/light chain mispairing.

The present invention provides a method of promoting local bone growth by administering a therapeutic amount of a Sost antagonist to a mammalian patient in need thereof. Preferably, the Sost antagonist is an antibody or FAB fragment selectively recognizing any one of SEQ ID NOS: 1-23. The Sost antagonist may be coadministered together or sequentially with a matrix conducive to anchoring new bone growth. Orthopedic and Periodontal devices comprising an implantable portion adapted to be permanently implanted within a mammalian body and bearing an external coating ofa Sost antagonist are also disclosed, as it a method ofincreasing bone density by administering to a mammalian patient a therapeutic amount ofa Sost antagonist together with an antiresorptive drug.

This invention relates to inhibition of the complement signaling using an anti-C5 antibody. Specifically, the invention relates to methods of treating a complement-mediated disease or complement-mediated disorder in an individual by contacting the individual with an anti-C5 antibody.

Aspects of the disclosure relate to complexes comprising a muscle-targeting agent covalently linked to a molecular payload. In some embodiments, the muscle-targeting agent specifically binds to an internalizing cell surface receptor on muscle cells. In some embodiments, the molecular payload inhibits expression or activity of DUX4. In some embodiments, the molecular payload is an oligonucleotide, such as an antisense oligonucleotide or RNAi oligonucleotide.

An anti-canine CD16 polypeptide generally includes a CDR region of SEQ ID NO:5, a CDR region of SEQ ID NO:9, or a functional variant of either CDR region. An anti-canine CD64 polypeptide generally includes a CDR region of SEQ ID NO:13, a CDR region of SEQ ID NO:17, or a functional variant of either CDR region. The anti-canine CD16 polypeptide and anti-canine CD64 polypeptide may be incorporated into a therapeutic compound, a multispecific compound, a targeted imaging compound, or a capture assay device.

Disclosed is a method for improving affinity of an antibody for an antigen, comprising, in an unmodified antibody, improving affinity for an antigen as compared to the unmodified antibody, by changing 17th, 18th and 20th amino acid residues of a light chain defined by Kabat method to charged amino acid residues.