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: Murine monoclonal antibodies and related products such as antibody fragments, immunotoxins, human and humanized antibodies are disclosed, all of which bind to the gp120 protein on the envelope of HIV-1. These antibodies and related products neutralize HIV-1. They inhibit the infection of T cells, and also inhibit syncytium formation. Further, the antibodies are preferably group-specific and neutralize various strains and isolates of HIV-1. These antibodies have a variety of uses, including the treatment of AIDS and ARC, the prevention of HIV-1 infection, as well as a diagnostic application, in that they can be used for assaying of unknown fluid samples for HIV-1.

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 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: 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: 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.

Abstract: Anti-idiotypic monoclonal antibodies that recognize the paratope of monoclonal antibodies specific for unique antigenic epitopes of IgE (designated ige.bl) which are present on membrane-bound IgE-expressed by bearing B cells but not on IgE bound to Fc.epsilon.R on basophils are described.

Abstract: Antigenic epitopes associated with the extracellular segment of the domain which anchors immunoglobulins to the B cell membrane are disclosed. For IgE, the epitopes are present on IgE-bearing B cells but not basophils or the secreted, soluble form of IgE. The epitope can be exploited for therapy and diagnosis. For example, antibodies or immunotoxins specific for the epitopes associated with the anchor domain of IgE can be used to selectively destroy IgE-bearing lymphocytes, thus blocking IgE-mediated allergic reactions.

Abstract: Molecular conjugates which facilitate the attachment of macromolecular drugs onto cellular surfaces and their entry into cells are described. The molecular conjugates comprise a macromolecular drug linked to an "inactivated" membrane blending agent which inserts into the cellular plasma membrane. The membrane blending agent is inactivated by cleavable linkage to a blocking agent which, until released from the conjugate under appropriate conditions, blocks and ability of the membrane blending agent to insert into the cellular membrane. Upon release of the blocking agent, the membrane blending agent is "activated" and the conjugate can be inserted into a cellular plasma membrane. The membrane blending agents can be peptides such as fusogenic or ion channel forming peptides or long chain fatty acids. The blocking agents can be bulky or charged moieties which mask and prevent insertion of the membrane blending agent.

Abstract: Antigenic epitopes associated with the extracellular segment of the domain which anchors immunoglobulins to the B cell membrane are disclosed. For IgE, the epitopes are present on IgE-bearing B cells but not basophils or the secreted, soluble form of IgE. The epitope can be exploited for diagnosis.

Abstract: Antigenic epitopes associated with the extracellular segment of the domain which anchors immunoglobulins to the B cell membrane are disclosed. For IgA, the epitopes are present on IgA-bearing B cells but not the secreted, soluble form of IgA. The epitopes can be exploited for therapy and prophylaxis. For example, antibodies specific for the epitopes associated with the anchor and peptide encompassing the epitope domain of IgA can be used to increase secretory IgA production for the purposes of treating patients with infectious diseases and IgE-mediated allergic diseases.

Abstract: Antigenic epitopes associated with the extracellular segment of the domain which anchors immunoglobulins to the B cell membrane are disclosed. For IgA, the epitopes are present on IgA-bearing B cells but not the secreted, soluble form of IgA. The epitope can be exploited for therapy and prophylacsis. For example, antibodies specific for the epitopes associated with the anchor and peptide encompassing the epitope domain of IgA can be used to increase secretory IgA production for the purposes of treating patients susceptible with infectious diseases and IgE-mediated allergic diseases.

Abstract: A method of preparing simultaneously monoclonal antibodies specific for different cell-free products of activated human T lymphocytes is disclosed. Human T cells are activated in a medium supplemented with mouse serum rather than conventional calf serum. A supernatant prepared from the activated T cells is used to immunize mice. The dominant immunogens in the supernatant are the cell-free products of human T lymphocytes. The yield of hybrid cells which produce products reactive with cell-free products of human T lymphocytes is enhanced by injecting the immunized mice with a supernatant from mitogen-activated murine splenocytes. In addition, a novel radioimmunoadsorbent assay for screening hybrids to detect production of monoclonal antibodies reactive with cell-free products of human T lymphocytes is disclosed.

Abstract: This invention relates to a novel immunoassay device and method for the determination of antigenic substances. The device essentially comprises a pattern or array of minute antibody-coated spots on the surface of a support. The array of antibody-coated spots is preferably in the form of a rectangular matrix. Each antibody-coated spot is made up of antibodies of a different and distinct specificity. A large number of different antibody-coated spots can be assembled on a very small portion of the surface of the support. The spots serve as tiny, specific immunoadsorbents of cells. The expression of particular surface antigen by cells may be detected by determining to which antibody-coated spot the cells bind.