Abstract: The invention relates to reshaped human monoclonal antibodies directed against isotypic determinants of immunoglobulin E (IgE), direct equivalents and derivatives of said antibodies. The molecules of the invention are useful for diagnostics, prophylaxis and treatment of allergy.

Abstract: The invention relates to reshaped human monoclonal antibodies directed against isotypic determinants of immunoglobulin E (IgE), direct equivalents and derivatives of said antibodies. The molecules of the invention are useful for diagnostics, prophylaxis and treatment of allergy.

Abstract: The invention relates to reshaped human monoclonal antibodies directed against isotypic determinants of immunoglobulin E (IgE), direct equivalents and derivatives of said antibodies. The molecules of the invention are useful for diagnostics, prophylaxis and treatment of allergy.

Abstract: Disclosed are conjugates including a substantially nonimmunogenic polymer backbone or microbead and binding molecules, such as Fv, Fab, or F(ab').sub.2 fragments of monoclonal antibodies or whole antibodies that are bound through their Fc carbohydrate moieties or have their Fc portion modified so that they cannot effect ADCC or complement-mediated cytolysis, and that are specific for a T cell surface antigen, such as CD3, TCR, CD4, CD8, or CD28 on T cells. The polymer or microbead is preferably made of cross-linked dextran, ficoll, latex, or agarose, and is preferably of 0.1 to 10 .mu.m in size, so that it can be suspended in fluids for in vivo applications. These conjugates can be used as adjuvants to enhance the antibody response against an administered immunogen.

Abstract: The invention relates to a method of using a peptide which has the sequence of epitopes which are present on B cell-bound but not secreted IgA. This induces production of the antibody itself. These extracellular peptide segments form, entirely or in part, antigenic epitopes unique to membrane-bound but not secreted IgA.

Abstract: Monoclonal antibodies are revealed which bind to the gp 120 protein on the envelope of HIV-1. These antibodies neutralize HIV-1. They inhibit the infection of T cells, and also inhibit syncytium formation. Further, the antibodies are group-specific and neutralize different strains and isolates of HIV-1. These antibodies have a variety of uses, including the treatment and prevention of AIDS and ARC. The antibodies are used in immunotoxins which are specifically toxic to HIV-1 infected T cells.

Abstract: Disclosed are immunogens and peptides based on the binding site of gC1q-R for HIV-1 gp120, and immunogens and peptides based on the binding site of HIV-1 gp120 for gC1q-R. The sequence of the gC1q-R binding site for gp120 is shown in SEQ ID NO.: 2. The sequence of the HIV-1 gp120 binding site for gC1q-R is shown in SEQ ID NO.: 3. Also disclosed are antibodies and binding molecules to all such immunogens and peptides, and inducing the endogenous production of such antibodies.

Abstract: Disclosed are immunogens and peptides based on the binding site of gC1q-R for HIV-1 gp120, and immunogens and peptides based on the binding site of HIV-1 gp120 for gC1q-R. The sequence of the gC1q-R binding site for gp120 is shown in SEQ D NO.: 2. The sequence of the HIV-1 gp120 binding site for gC1q-R is shown in SEQ ID NO.: 3. Also disclosed are antibodies and binding molecules to all such immunogens and peptides, and inducing the endogenous production of such antibodies.

Abstract: Disclosed is a hybrid recombinant protein consisting of human interferon, preferably interferon-.alpha. (IFN.alpha.), and human immunoglobulin Fc fragment, preferably .gamma.4 chain, joined by a peptide linker comprising the sequence Gly Gly Ser Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser (SEQ ID NO:1).

Abstract: Disclosed are immunogens and peptides based on the binding site of gC1q-R for HIV-1 gp120, and immunogens and peptides based on the binding site of HIV-1 gp120 for gC1q-R. The sequence of the gC1q-R binding site for gp120 is shown in SEQ ID NO.: 2. The sequence of the HIV-1 gp120 binding site for gC1q-R is shown in SEQ ID NO.: 3. Also disclosed are antibodies and binding molecules to all such immunogens and peptides, and inducing the endogenous production of such antibodies.

Abstract: The invention relates to unique extracellular peptide segments present on B cell-bound but not secreted IgA. These extracellular peptide segments form, entirely or in part, antigenic epitopes unique to membrane-bound but not secreted IgA, and thereby provide a unique epitope on the IgA-bearing B cells to which membrane-bound IgA is attached. These peptide segments can be used as immunogens to generate antibodies which specifically target membrane-bound IgA and IgA-bearing B cells.

Abstract: Disclosed are pharmaceutical preparations containing human monoclonal IgA antibodies specific for major allergenic proteins found in ragweed, house dust mites, and cat and dog dander. Also disclosed are constructs comprising physiological compatible polymer backbones or microbeads and a plurality of covalently conjugated allergen-specific binding molecules. Such binding molecules are IgG or IgA, or their F(ab').sub.2, Fab, or Fv fragments, specific to the major allergenic proteins mentioned above. Also disclosed are methods for treating a patient with allergic rhinitis, asthma, or conjunctivitis by applying a pharmaceutical preparation containing the antibodies specific for the allergenic molecules, to which the patient is sensitized, to the patient's affected mucosal tissues, such as the nasal linings, the respiratory tract, or the eyes.

Abstract: Disclosed are immunogens and peptides based on the binding site of gC1q-R for HIV-1 gp120 and immunogens and peptides based on the binding site of HIV-1 gp120 for gC1q-R. The sequence of the gC1q-R binding site for gp120 is shown in SEQ ID NO.: 2. The sequence of the HIV-1 gp120 binding site for gC1q-R is shown in SEQ ID NO.: 3. Also disclosed are antibodies and binding molecules to all such immunogens and peptides, and inducing the endogenous production of such antibodies.

Abstract: Unique antigenic epitopes of IgE (designated ige.bl) which are present on IgE-bearing B lymphocytes but not basophils are described. Monoclonal antibodies which bind to the epitopes are useful to treat IgE-mediated allergy. The monoclonal antibodies, either alone or as cytotoxin-conjugated immunotoxins, can be used to reduce or deplete IgE-producing B cells in allergy sufferers. The antibodies may also have the additional therapeutical effects of clearing IgE from circulation by forming immune complexes. Monoclonal antibodies against the paratope of the antibody can be used to actively immunize allergy sufferers to attain the same results of administering the monoclonal antibody.

Abstract: The invention relates to methods of treating allergic reactions and of reducing circulating IgE using antibodies which bind to secreted IgE and membrane-bound IgE on the surface of IgE-producing B cells but not to IgE on basophils or mast cells.

Abstract: Antigenic epitopes associated with the extracellular segment of the domain which anchors dog immunoglobulin-.epsilon. to the B cell membrane are disclosed. The epitopes are present on dog IgE-bearing B cells but not basophils or the secreted, soluble form of dog IgE. The peptides representing the epitopes associated with the anchor domain of dog IgE can be used to generate antibodies against these regions.

Abstract: The invention relates to epitopes which are present on B cell-bound but not secreted IgA, peptide segments which represent such epitopes, and DNA coding for these peptides. These extracellular peptide segments form, entirely or in part, antigenic epitopes unique to membrane-bound but not secreted IgA.

Abstract: Antibodies that bind soluble IgE but not IgE on the surface of B lymphocytes or basophils are described. The antibodies do not induce histamine release by basophils or mast cells.

Abstract: Chimeric antibodies which bind to unique antigenic epitopes of IgE (designated ige.b1) which are present on IgE-bearing B lymphocytes but not basophils are described.

Abstract: Methods of producing monoclonal antibodies that bind to unique antigenic epitopes of IgE (designated ige.bl) which are present on IgE-bearing B cells but not basophils are described. The monoclonal antibodies block binding of IgE to mast cells and basophils in vitro.