The invention discloses methods for the generation of chimaeric human-non-human antibodies and chimaeric antibody chains, antibodies and antibody chains so produced, and derivatives thereof including fully humanised antibodies; compositions comprising said antibodies, antibody chains and derivatives, as well as cells, non-human mammals and vectors, suitable for use in said methods.

The present invention provides a CD7 chimeric antigen receptor-modified NK-92MI cell and use thereof. In particular, the present invention provides an engineered NK cell expressing a chimeric antigen receptor (CAR), said CAR having an antigen-binding domain containing a nanobody VHH sequence targeting CD73. Said NK cell of the present invention can effectively kill tumor cells, especially T cell tumors, and has a good therapeutic effect on T cell leukemia (such as T-ALL).

The present disclosure relates to a multispecific binding moiety comprising a PD-1 binding domain and a TGF-βRII binding domain, wherein the PD-1 binding domain blocks PD-1 mediated signaling and the TGF-βRII binding domain blocks TGF-βRII-mediated signaling. The present disclosure further relates to a pharmaceutical composition comprising such multispecific binding moiety, a method of treatment using such multispecific binding moiety, and a cell producing such multispecific binding moiety.

The present invention relates to polypeptides directed against or specifically binding to C—X—C Motif chemokine receptor 2 (CXCR2) and in particular to polypeptides capable of modulating signal transduction from CXCR2. The invention also relates to nucleic acids, vectors and host cells capable of expressing the polypeptides of the invention, pharmaceutical compositions comprising the polypeptides and uses of said polypeptides and compositions for treatment of diseases involving aberrant functioning of CXCR2.

Provided is a method for producing a heavy chain variable domain of a heavy-chain antibody (VHH) with a high yield. The method for producing a VHH includes culturing a Bacillus bacterium into which a gene that encodes variable domain of heavy chain of heavy-chain antibody is introduced and which is deficient in an extracellular protease.

Antibody-based binding agents derived from human and camelid immunoglobulins are described, as well as strains of yeast engineered to secrete the binding agents, and methods of treating and preventing Clostridium difficile infections using the engineered strains of yeast. These binding agents recognize and bind with specificity to Clostridium difficile toxin A and/or toxin B and in some cases exhibit toxin neutralizing activity. The binding agents include camelid V.sub.HH peptide monomers, linked groups of V.sub.HH peptide monomers, V.sub.HH peptide monomers joined to antibody Fc domains, and V.sub.HH peptide monomers joined to IgG antibodies.

A tetravalent, homodimer-type bispecific antibody molecule that simultaneously targets immune effector cell antigen CD3 and human epidermal growth factor receptor 2 (Her2); the bispecific antibody molecule comprises, from in sequence from N-terminus to C-terminus, a first single-chain Fv capable of specifically binding to Her2, a second single-chain Fv capable of specifically binding to CD3, and an Fc fragment; the first and second single-chain Fv are connected by means of a connection peptide, and the second single-chain Fv is connected to the Fc directly fragment or is connected by means of a connection peptide; the Fc fragment does not have effector functions such as CDC, ADCC and ADCP. The bispecific antibody may significantly inhibit or kill tumor cells, and has controlled toxic side effects that may be caused by excessive activation of effector cells. The maximum safe starting dose in preclinical toxicology evaluation tests is significantly higher than other doses having the same target, and no systemic immunotoxicity occurs, suggesting that the drug administration safety window for the bispecific antibody is wide; in addition, said bispecific antibody is a homodimer that does not experience the problem of heavy chain and light chain mismatching; the steps of purification are simple and efficient, expression is high, and the physicochemical and in vivo stability of the antibody are significantly improved.

This disclosure provides a monoclonal population of highly sialylated multimeric binding molecules where the population includes IgM antibodies, IgM-like antibodies, or other IgM-derived binding molecules, where the population of binding molecules has a higher level of sialic acid content than is found in normal serum IgM. Also provided are methods of producing such monoclonal populations of highly sialylated multimeric binding molecules.

The invention relates to a protein complex comprising at least two polypeptide chains A (PCA) and B (PCB), wherein PCA comprises a heterodimerization domain A (HDA) and PCB comprises a heterodimerization domain B (HDB), wherein HDA and HDB bind to each other and wherein one heterodimerization domain comprises or consists of two N-terminal β-strands (N-β) of an immunoglobulin (Ig) domain and the other heterodimerization domain comprises or consists of two C-terminal β-strands (C-β) of an Ig domain. The invention further relates to polynucleotides encoding one or more polypeptides of the protein complex, expression vectors comprising the polynucleotides and a cell comprising the polynucleotides or the expression vectors.

Described herein are methods to affect binding by a multivalent binding molecule to a FZD receptor and a Wnt co-receptor on a cell wherein binding by the multivalent binding molecule to both FZD receptor and co-receptor on the cell activates a Wnt signaling pathway. Also described herein are multivalent binding molecules comprising a FZD receptor binding domain and a Wnt co-receptor biding domain on either end of an Fc domain that activate a Wnt signaling pathway and methods for their use.