Antibodies (especially humanized antibodies) against the hepatitis B surface antigen (HBsAg), a nucleic acid molecule encoding same, a method for preparing same, and a pharmaceutical composition containing same. The anti-HBsAg antibodies have a higher binding affinity to HBsAg at a neutral pH than at an acidic pH, thereby significantly enhancing virus clearance efficiency and prolonging virus inhibition time. The antibodies and pharmaceutical composition may be used to prevent and/or treat HBV infections or diseases related to HBV infection (such as hepatitis B) for use in neutralizing the virulence of HBV in the body of a subject (such as a human) to reduce a serum level of HBV DNA and/or HBsAg in the body of the subject, or to activate a humoral immune response of a subject (such as a person infected with chronic HBV or a patient who has chronic hepatitis B) against HBV.

The present application relates to a variant Fc region comprising at least one modification relative to a wild-type human Fc region, where the modification selected from the group consisting of 434S, 252Y/428L, 252Y/434S, and 428L/434S, and the numbering is according to the EU index.

A specific conformational epitope of a hepatitis B surface antigen and a hepatitis B neutralizing antibody binding thereto are disclosed. The epitope has a specific conformational structure. In addition, the conformational epitope does not contain the ‘a’ determinant that may generate an escape mutation upon administration of conventional vaccines or HBIg. Thus, an antibody capable of binding to the epitope is highly unlikely to allow the emergence of a vaccine escape mutation, which is caused by conventional vaccines, and as such, can retain a sustained effect. Therefore, such an antibody or a vaccine composition can find effective applications in the prevention and treatment of HBV, having great economic value.

The present invention relates to a method of producing recombinant binding proteins with binding specificity for a peptide-MHC (pMHC) complex. The invention also relates to recombinant binding proteins comprising one, two or more designed repeat domain(s), preferably designed ankyrin repeat domain(s), with binding specificity for a pMHC complex, and to such binding proteins which further comprise a binding agent having binding specificity for a protein expressed on the surface of an immune cell, preferably a T-cell. In addition, the invention relates to nucleic acids encoding such binding proteins or repeat domains, pharmaceutical compositions comprising such binding proteins or nucleic acids, and the use of such binding proteins, nucleic acids or pharmaceutical compositions in methods for treating or diagnosing diseases, including cancer, infectious diseases and autoimmune diseases.

Disclosed is a method for producing an antibody reagent for detecting a test substance in a sample by an immune complex transfer method. The method comprises the steps of: bringing an antibody solution comprising a labeled antibody capable of binding to the test substance into contact with a solid phase used in the immune complex transfer method; and separating the solid phase and the antibody solution to prepare the antibody reagent from the antibody solution.

Disclosed is a method for controlling affinity of an antibody for an antigen, comprising substituting at least 3 amino acid residues of framework region 3 (FR3) defined by the Chothia method with charged amino acid residues, in an antibody whose electrical characteristic of complementarity determining region (CDR) based on the amino acid sequence of the CDR is neutral or negatively charged.

The present invention relates to designed ankyrin repeat domains with altered surface residues, as well as to proteins comprising such a designed ankyrin repeat domain, nucleic acids encoding such domains or proteins, methods of preparing such proteins, pharmaceutical compositions comprising such proteins or nucleic acids, and the use of such proteins, nucleic acids or pharmaceutical compositions in the treatment of diseases.

Disclosed are the methods of curing HBV infection and providing complete protection against HBV infection in a simplified HBV immunization schedule. The mechanistic basis for curing HBV infection is founded on the understanding that hepatitis B virus infection is established and prolonged by new rounds of infection with continuously produced viruses, which are not fully neutralized because of insufficient endogenous neutralizing antibodies. The methods of curing HBV infection including chronic HBV infection are aimed to block new rounds of HBV infection. The guidelines for establishing treatment regimens for curing HBV infection, include production or administration of sufficient level of HBV neutralizing antibodies in treated patients. Among the many different possibilities contemplated, the sufficient level of HBV neutralizing antibodies is expressed and maintained by the single injection of the HBV therapeutics that comprises non-replicating viruses or vectors encoding HBV neutralizing antibodies or by multi-injection of exogenous HBV neutralizing antibodies.

The present application relates to a variant Fc region comprising at least one modification relative to a wild-type human Fc region, where the modification selected from the group consisting of 434S, 252Y/428L, 252Y/434S, and 428L/434S, and the numbering is according to the EU index.

The present invention provides modified glucagon-like peptide 1 (GLP1) polypeptides, fusion proteins comprising modified GLP1 polypeptides, and methods of use thereof. In various embodiments of the invention, the fusion proteins are GLP1 receptor agonists that comprise a modified GLP1 fused to a stabilizing domain. In some embodiments, the fusion proteins comprising modified GLP1 are useful for treating or ameliorating a symptom or indication of a disorder such as obesity and diabetes.