Abstract: The present disclosure is directed to IgE EMPD peptide immunogen constructs and formulations thereof for the treatment of IgE-mediated allergic diseases. The IgE EMPD peptide immunogen constructs have a B cell epitope peptide of more than 20 amino acids, preferably cyclic, linked through an optional spacer to heterologous T helper cell (Th) epitopes derived from pathogen proteins. These peptide immunogen constructs and formulations thereof can stimulate the generation of highly specific antibodies in vaccinated hosts that are directed against the IgE EMPD peptide and are crossreactive with membrane-bound IgE on B lymphocytes committed to IgE secretion. The antibodies induced by the peptide immunogen constructs and formulations thereof in vaccinated hosts can induce apoptosis of IgE-expressing B cells and mediate Antibody Dependent Cellular Cytototoxity (ADCC), resulting in reduction of antigen-specific IgE and total IgE levels in vaccinated hosts to effectively treat IgE-mediated allergic pathology.

Abstract: The present disclosure is directed to individual peptide immunogen constructs targeting portions of the Interleukin-6 (IL-6) protein, compositions containing the constructs, antibodies elicited by the constructs, and methods for making and using the constructs and compositions thereof. The disclosed IL-6 peptide immunogen constructs contain a B cell epitope from IL-6 linked to a heterologous T helper cell (Th) epitope directly or through an optional heterologous spacer. The IL-6 peptide immunogen constructs stimulate the generation of highly specific antibodies directed to the IL-6 receptor (IL-6R) binding site for the prevention and/or treatment of diseases impacted by IL-6 dysregulation.

Abstract: A novel humanized anti-IgE antibody is disclosed. The antibody is capable of binding to free IgE, membrane-bound IgE on B lymphocytes, IgE bound by CD23, but not to IgE bound by high-affinity IgE.Fc receptor on mast cells. The present invention relates to the treatment of IgE-mediated diseases, including allergic asthma, allergic rhinitis, atopic dermatitis, food allergy, chronic spontaneous (idiopathic) urticaria, chronic rhinosinusitis, systemic mastocytosis, cutaneous mastocytosis, allergic bronchopulmonary aspergillosis, recurrent idiopathic angioedema, and eosinophil-associated gastrointestinal disorder by administering the anti-IgE antibody of the present invention.

Abstract: A novel humanized anti-IgE antibody is disclosed. The antibody is capable of binding to free IgE, membrane-bound IgE on B lymphocytes, IgE bound by CD23, but not to IgE bound by high-affinity IgE.Fc receptor on mast cells. The present invention relates to the treatment of IgE-mediated diseases, including allergic asthma, allergic rhinitis, atopic dermatitis, food allergy, chronic spontaneous (idiopathic) urticaria, chronic rhinosinusitis, systemic mastocytosis, cutaneous mastocytosis, allergic bronchopulmonary aspergillosis, recurrent idiopathic angioedema, and eosinophil-associated gastrointestinal disorder by administering the anti-IgE antibody of the present invention.

Abstract: Antibodies binding to junction regions between the CH4 and C?mX domains of membrane-bound IgE and uses thereof in treating IgE-mediated diseases such as allergic diseases.

Abstract: Antibodies binding to junction regions between the CH4 and C?mX domains of membrane-bound IgE and uses thereof in treating IgE-mediated diseases such as allergic diseases.

Abstract: The invention pertains to methods of using C?mX peptides (e.g., GLAGGSAQSQRAPDRVL; SEQ ID NO:2) that can bind effectively induce immune responses to membrane-bound IgE (mIgE) expressed on the surface of human B lymphocytes.

Abstract: The invention pertains to the generation and utility of antibodies that can bind effectively to C?mX domain on membrane-bound IgE (mIgE) expressed on the surface of human B lymphocytes. The C?mX domain of 52 amino acid residues, located between the CH4 domain and the C-terminal membrane-anchor peptide on human membrane-bound epsilon chain, had been suggested as an antigenic site for immunological targeting of B cells expressing mIgE. Previous reported monoclonal antibodies, including a20, which bind to RADWPGPP (SEQ ID NO:1) peptide at the C-terminal of C?mX, have now been found to bind poorly to mIgE on human B cells. We have discovered that only monoclonal antibodies specific for certain segments, such as GLAGGSAQSQRAPDRVL (SEQ ID NO:2) and HSGQQQGLPRAAGGSVPHPR (SEQ ID NO:3), of C?mX can bind effectively to mIgE on human B cells and hence have the utility for targeting those B cells for the treatment of diseases mediated by IgE.

Abstract: The invention pertains to the generation and utility of antibodies that can bind effectively to C?mX domain on membrane-bound IgE (mIgE) expressed on the surface of human B lymphocytes. The C?mX domain of 52 amino acid residues, located between the CH4 domain and the C-terminal membrane-anchor peptide on human membrane-bound epsilon chain, had been suggested as an antigenic site for immunological targeting of B cells expressing mIgE. Previous reported monoclonal antibodies, including a20, which bind to RADWPGPP (SEQ ID NO:1) peptide at the C-terminal of C?mX, have now been found to bind poorly to mIgE on human B cells. We have discovered that only monoclonal antibodies specific for certain segments, such as GLAGGSAQSQRAPDRVL (SEQ ID NO:2) and HSGQQQGLPRAAGGSVPHPR (SEQ ID NO:3), of C?mX can bind effectively to mIgE on human B cells and hence have the utility for targeting those B cells for the treatment of diseases mediated by IgE.

Abstract: The invention pertains to the generation and utility of antibodies that can bind effectively to C?mX domain on membrane-bound IgE (mIgE) expressed on the surface of human B lymphocytes. The C?mX domain of 52 amino acid residues, located between the CH4 domain and the C-terminal membrane-anchor peptide on human membrane-bound epsilon chain, had been suggested as an antigenic site for immunological targeting of B cells expressing mIgE. Previous reported monoclonal antibodies, including a20, which bind to RADWPGPP (SEQ ID NO:1) peptide at the C-terminal of C?mX, have now been found to bind poorly to mIgE on human B cells. We have discovered that only monoclonal antibodies specific for certain segments, such as GLAGGSAQSQRAPDRVL (SEQ ID NO:2) and HSGQQQGLPRAAGGSVPHPR (SEQ ID NO:3), of C?mX can bind effectively to mIgE on human B cells and hence have the utility for targeting those B cells for the treatment of diseases mediated by IgE.

Abstract: The invention pertains to the generation and utility of antibodies that can bind effectively to C?mX domain on membrane-bound IgE (mIgE) expressed on the surface of human B lymphocytes. The C?mX domain of 52 amino acid residues, located between the CH4 domain and the C-terminal membrane-anchor peptide on human membrane-bound epsilon chain, had been suggested as an antigenic site for immunological targeting of B cells expressing mIgE. Previous reported monoclonal antibodies, including a20, which bind to RADWPGPP peptide at the C-terminal of C?mX, have now been found to bind poorly to mIgE on human B cells. We have discovered that only monoclonal antibodies specific for certain segments, such as GLAGGSAQSQRAPDRVL and HSGQQQGLPRAAGGSVPHPR, of C?mX can bind effectively to mIgE on human B cells and hence have the utility for targeting those B cells for the treatment of diseases mediated by IgE.