Multivalent D-peptidic compounds that specifically bind to a target protein are provided. The multivalent D-peptidic compounds can include two or more distinct variant D-peptidic domains connected via linking components. The D-peptidic compounds can include multiple distinct domains that specifically bind to different binding sites on a target protein to provide for high affinity binding to, and potent activity against, the target protein. D-peptidic variant GA and Z domain polypeptides are also provided, which polypeptides have specificity-determining motifs (SDM) for specific binding to a target protein, such as VEGF-A or PD-1. In some embodiments where the target protein is homodimeric (e.g., VEGF-A, PD-1), the D-peptidic compounds may be similarly dimeric, and include a dimer of multivalent (e.g., bivalent) D-peptidic compounds. Methods for using the compounds are provided, including methods for treating a disease or condition associated with a target protein in a subject.

The present invention provides a fusion polypeptide that induces a humoral immune response and a cellular immune response to a virus, containing antigens or fragments thereof of the following (a) and (b), and having an oligomerization activity: (a) an antigen of the virus or a fragment thereof containing a B cell epitope conserved among subtypes of the virus; and (b) an antigen of the virus or a fragment thereof containing a T cell epitope conserved among subtypes of the virus (wherein the antigen(s) or the fragment(s) thereof of (a) and/or (b) have an oligomerization activity, or the fusion polypeptide further contains (c) a polypeptide having an oligomerization activity in addition to the antigens or the fragments thereof (a) and (b)).

The invention provides improved staphylococcal antigens. Immunogenic compositions are also provided. The invention may find use in the prevention and treatment of staphylococcal infections.

The invention provides improved staphylococcal antigens. Immunogenic compositions are also provided. The invention may find use in the prevention and treatment of staphylococcal infections.

Described herein are variants of alpha-hemolysin having at least one amino acid substitution at H35G, E111N, M113A, and/or K147N in the mature, wild-type alpha-hemolysin amino acid sequence. In certain examples, the variant may have a substitution at E111S, M113S, T145S, K147S, or L135I in the mature alpha-hemolysin amino acid sequence. The α-hemolysin variants may also include a substitution at H144A and/or a series of glycine residues spanning residues 127 to 131 of the mature, wild-type alpha hemolysin. Also provided are nanopore assemblies including the alpha-hemolysin variants, the assembly having an increased nanopore lifetime. Further, provided are variants that, in addition to providing increased lifetime, provide a decreased time-to-thread. Hence, the variants provided herein both increase nanopore lifetime and improve efficiency and accuracy of DNA sequencing reactions using nanopores comprising the variants.

Non-natural albumin binding domains, polynucleotides encoding thereof and methods of making and using these domains and polynucleotides are useful in controlling the half-life of therapeutic molecules for patients.

Non-natural albumin binding domains, polynucleotides encoding thereof and methods of making and using these domains and polynucleotides are useful in controlling the half-life of therapeutic molecules for patients.

A composition-of-matter comprising a crystallized form of a large ribosomal (50S) subunit of a pathogenic bacterium, and the atomic coordinates of the three-dimensional structure thereof are provided herein, as well as methods for crystallizing the same, and using the atomic coordinates of the same to design de novo ligands with high specificity thereto.

A composition-of-matter comprising a crystallized form of a large ribosomal (50S) subunit of a pathogenic bacterium, and the atomic coordinates of the three-dimensional structure thereof are provided herein, as well as methods for crystallizing the same, and using the atomic coordinates of the same to design de novo ligands with high specificity thereto.

The present invention concerns a method of storing a separation matrix comprising multimers of immunoglobulin-binding alkali-stabilized Protein A domains covalently coupled to a porous support. The method comprises the steps of: a) providing a storage liquid comprising at least 50% by volume of an aqueous alkali metal hydroxide solution; b) permeating the separation matrix with the storage liquid; and c) storing the storage liquid-permeated separation matrix for a storage time of at least days. The alkali-stabilized Protein A domains comprise mutants of a parental Fc-binding domain of Staphylococcus Protein A (SpA), as defined by, or having at least 80% such as at least 90%, 95% or 98% identity to, SEQ ID NO 51 or SEQ ID NO 52, wherein the amino acid residues at positions 13 and 44 of SEQ ID NO 51 or 52 are asparagines and wherein at least the asparagine residue at position 3 of SEQ ID NO 51 or 52 has been mutated to an amino acid selected from the group consisting of glutamic acid, lysine, tyrosine, threonine, phenylalanine, leucine, isoleucine, tryptophan, methionine, valine, alanine, histidine and arginine.