The present invention relates to a polypeptide comprising a silk polypeptide and an antigen. Further, the present invention relates to an article comprising the polypeptide. Furthermore, the present invention relates to a pharmaceutical composition comprising the article. In addition, the present invention relates to the article or pharmaceutical composition for use as a pharmaceutical, for inducing an immune response and/or for use in a prophylactic and/or therapeutic treatment of a disease.

Provided in the present invention is a PDL-1 molecule. The affinity of the PDL-1 molecule to the PD-1 molecule is at least two times the affinity of the wild-type PDL-1 molecule to the PD-1 molecule. Meanwhile, the PDL-1 molecule of the present invention can effectively improve the killing efficiency of lymphocytes. In addition, the present invention also provides nucleic acids encoding the PDL-1 molecule of the present invention, and a complex of the PDL-1 molecules of the present invention. The PDL-1 molecule of the present invention may be used alone or in combination with other molecules.

Non-naturally occurring polypeptides are disclosed that include (a) 3-3 secondary structure elements, wherein each secondary structure element is either an α-helix (H domain) of between 10-20 amino acid residues in length or a β-strand (E domain) of between 3-10 amino acid residues in length; and (b) 2-4 linkers of between 2 to 6 amino acid residues in length connecting adjacent secondary structure elements; wherein the polypeptide is between 25-50 amino acid residues in length; and wherein the polypeptide includes no cysteine residues.

Provided are processes and materials for solving biological or structural information about proteins or other organic molecules. The processes capitalize on a rigid multimeric nanocage formed from self-assembling substructure proteins. The processes and materials allow for recognition and tight, optionally covalent, bonding of any protein molecule with a tag complementary to a capture sequence on the nanocage. The processes and materials may be used to obtain biological or structural information by cryo-electron microscopy and overcome prior limitations of target protein size or salt concentration.

Provided are processes and materials for solving biological or structural information about proteins or other organic molecules. The processes capitalize on a rigid multimeric nanocage formed from self-assembling substructure proteins. The processes and materials allow for recognition and tight, optionally covalent, bonding of any protein molecule with a tag complementary to a capture sequence on the nanocage. The processes and materials may be used to obtain biological or structural information by cryo-electron microscopy and overcome prior limitations of target protein size or salt concentration.

Provided are: an economically superior protein crystallization method capable of efficiently finding conditions for crystallization by using a small amount of protein; and a crystallization device used for the method. According to the present invention, a transparent sealed container 1 is filled with a solution of protein, a part of the transparent sealed container 1 being formed of a semipermeable membrane 2 with a molecular weight cut-off that inhibits passage of the protein while allowing passage of a precipitant, and then, a precipitant solution with changed concentration and/or pH of the precipitant is continuously supplied to the semipermeable membrane 2, to crystallize the protein with the precipitant that infiltrates from the semipermeable membrane 2 into the sealed container 1.

The present invention relates to enveloped RNA viruses. The invention in particular relates to the generation of superior antigens for mounting an immune response by first identifying then mutating the immunosuppressive domains in fusion proteins of enveloped RNA viruses resulting in decreased immunosuppressive properties of viral envelope proteins from the viruses.

The present invention relates to enveloped RNA viruses. The invention in particular relates to the generation of superior antigens for mounting an immune response by first identifying then mutating the immunosuppressive domains in fusion proteins of enveloped RNA viruses resulting in decreased immunosuppressive properties of viral envelope proteins from the viruses.

The invention relates to a healthcare product comprising (i) a component selected from the group of heat shock proteins from alfalfa and heat shock protein hydrolysates from alfalfa, the product further comprising imiquimod ##STR00001##
or a pharmaceutically acceptable salt or derivative thereof. Further, the invention relates to a healthcare product for use in the prophylactic or therapeutic treatment of a skin disorder. Further, the invention relates to HSP for use for use in preventing the occurrence of a negative-side effect of a treatment with imiquimod, or alleviating such side effect.

Provided herein are heteromultimer constructs with reduced or silenced effector function. In an embodiment is provided a heteromultimer construct comprising an IgG Fc construct having a first and a second Fc polypeptide, each Fc polypeptide comprising a modified lower hinge region wherein: the modified lower hinge region of said first Fc polypeptide comprises at least one amino acid modification, the modified lower hinge region of said second Fc polypeptide comprises at least one amino acid modification which is different from at least one amino acid modification of said first Fc polypeptide, and the IgG Fc construct displays reduced binding to all Fcγ receptors and to C1q protein as compared to a corresponding parent IgG Fc construct. Also provided are methods of producing such heteromultimer constructs, and methods of reducing ADCC for an antibody construct by reducing effector function.