The invention is directed to HIV-1 neutralizing antibodies and methods for their uses.

Described herein are modified integrin α and/or β headpiece polypeptides, and crystallizable integrin polypeptide dimers comprising a modified integrin α and/or β headpiece polypeptide and a disulfide bond linking the two integrin headpiece polypeptide subunits. Methods for using the modified integrin α and/or β headpiece polypeptides and the integrin polypeptide dimers are also provided herein. For example, methods for characterizing integrin-ligand interaction and identifying integrin ligands are also provided herein. In some embodiments, the identified integrin ligands can be used as inhibitors of integrins.

Provided herein are tetravalent antigen binding complexes having agonist activity for a cell surface receptor. In some embodiments, the complexes comprise binding specificities for multiple epitopes of the same cell surface receptor. Further provided herein are nucleic acids, vectors, host cells, pharmaceutical compositions, and methods of production related thereto.

The present disclosure provides binding proteins, such as antibodies, that bind to a GDNF Family Receptor Alpha Like (GFRAL) protein, including human GFRAL protein, and methods of their use.

The present disclosure provides antibodies that specifically bind to TIGIT. The antibodies have the capacity for substantial activation of T cells and natural killer cells by inhibiting binding of TIGIT to CD155. The antibodies can be used for treatment of cancer and infectious disease, among other applications.

Antibody molecules that specifically bind to TIM-3 are disclosed. The anti-TIM-3 antibody molecules can be used to treat, prevent and/or diagnose immune, cancerous, or infectious conditions and/or disorders.

The present invention relates to broadly neutralizing anti-HIV-1 antibodies and isolated antigens. Also disclosed are related methods and compositions.

The present invention is based, in part, on the discovery of the human-specific regulatory control of cGAS and the structure of the active human cGAS-DNA complex, as well as compositions comprising the modified hcGAS polypeptide, hcGAS-DNA complex, hcGAS-DNA-ATP complex, and methods of screening for modulators of the structure, expression, and/or activity of such polypeptides and complexes.

The invention provides methods for producing crystalline an anti-PD-1 monoclonal antibody (mAb), wherein the mAb is pembrolizumab or a pembrolizumab variant, comprising (1) mixing a solution comprising (a) the mAb, (b) polyethylene glycol (PEG), and (c) an additive selected from the group consisting of: caffeine, theophylline, 2′ deoxyguanosine-5′-monophosphate, a bioactive gibberellin, and a pharmaceutically acceptable salt of said bioactive gibberellin, to form a crystallization solution, (2) incubating the crystallization solution for a period of time sufficient for crystal formation; and (3) optionally harvesting the crystalline anti-PD-1 mAb from the solution. In specific embodiments, the PEG is PEG 3350 and the additive is caffeine. The invention also relates to the novel anti-human PD-1 mAb crystals produced by the methods described herein. Characterization of re-dissolved crystalline suspensions using several biochemical methods showed the bio-physical properties of the re-dissolved mAb crystals were consistent with the intact antibody starting sample. The crystals and methods of the invention are amenable to multiple pharmaceutical applications such as purification, storage, formulation, and drug delivery.

Provided herein are multispecific antigen-binding polypeptide constructs comprising at least two different heterodimers, each comprising a heavy chain and a light chain. At least one heterodimer comprises a Fab region comprising a lambda light chain and at least one heterodimer comprises a Fab region comprising a kappa light chain. One or more of the immunoglobulin heavy and light chains that form the antigen-binding polypeptide construct comprise amino acid modifications that promote correct pairing between the heavy and light chains to form the desired multispecific antigen-binding polypeptide construct. The amino acid modifications may be in the C.sub.H1 and/or C.sub.L domains, in the V.sub.H and/or V.sub.L domains, or a combination thereof.