Abstract: A recombinant first antigen, coupled with a foreign protein (such as immunoglobulin Fc from different species), can be used as a vaccine to induce active auto-immunity specifically through a T cell-dependent antibody response. The induced autoantibodies can recognize self-antigen in vivo and trigger immune responses to reduce or eliminate a target autologous antigen. Since there is evidence that the pathogenesis of some diseases, such as cancer, allergy, arthritis, atherosclerosis, graft rejection, or other inflammatory diseases, are caused by increased levels of certain autologous proteins, the instant compositions and methods provide a method of inducing autoantibodies to down-regulate the levels of a target autologous antigen or cells expressing the antigen to ameliorate diseases or disorders.

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: The invention relates to antibodies which immunologically bind epitopes present on B cell-bound but not secreted IgA. This is accomplished by targeting extracellular epitopes on the membrane anchoring peptide of the .alpha. chain which form, entirely or in part, antigenic epitopes unique to membrane-bound but not secreted IgA.

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. Three different isoforms of the C-terminal segment of the human .epsilon. chain resulting from alternative mRNA splicings in the membrane exon region are disclosed, one of which is secreted and not membrane-bound.

Abstract: Disclosed are immunofluorescence staining methods which increase the likelihood that antibodies expressed by a single B cell selected and sorted by fluorescence activated cell sorting are specific for the antigen of interest, and which also allow selection of B cells expressing antibodies of high affinity for the antigen of interest. The selection for B cells expressing antibodies to specific antigens is increased by labeling B cells with at least two antigen probes, where each antigen probe includes the antigen of interest and is labeled with a different fluorochrome. The positive selection is preferably combined with a negative selection step, in which autofluorescent cells and sticky cells are excluded out. The specificity of sorting of the desired B cells can be further enhanced by staining those antigen-specific B cells which produce the immunoglobulin isotype (typically IgG), with targeting molecules reactive with a B cell marker, such as .gamma.

Abstract: The invention relates to a method of stimulating IgA production through administering 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: Membrane anchoring peptides are attached to the C terminal end of the heavy chain of the various immunoglobulin isotypes (IgM, IgD, IgA, IgE, or IgG). The membrane anchoring peptides span the cell membrane lipid bilayer of B cells thereby affixing the associated immunoglobulin to the cell membrane surface. The extracellular segments of these peptides are unique for different isotypes. Epitopes unique to the B cells which produce each isotype are formed, in whole or in part, by these extracellular segments. These membrane-bound immunoglobulin isotype-specific ("migis") extracellular epitopes are not present on the secreted, soluble form of the immunoglobulins, which are not bound to the cell surface by the membrane anchoring peptides. The antibodies of the invention (and other related products) specifically bind to the extracellular migis epitopes of human .mu. chain, human .delta. chain, or human .gamma. chain.

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: Membrane anchoring peptides which are part of the heavy chain of an associated immunoglobulin (IgM, IgD, IgA, IgE, or IgG), span the cell membrane lipid bilayer of B cells thereby affixing the associated immunoglobulin to the cell membrane surface. The extracellular segments of these peptides are unique for different isotypes, but tend to be very similar among different subclasses of a particular isotype. The extracellular segments form in whole or in part an epitope unique to the B cells which produce each isotype. These membrane-bound immunoglobulin isotype-specific ("migis") extracellular epitopes are not present on the secreted, soluble form of the immunoglobulins, which are not bound to the cell surface by the membrane anchoring peptides. The antibodies of the invention (and other related products) bind the extracellular migis epitopes.

Abstract: The invention includes human .epsilon. chain transmembrane anchor peptide resulting from mRNA splicing other than the C.epsilon.4 exon, the .epsilon.m1 exon, and the .epsilon.m2 exon. Two new peptides in particular have been specifically identified. These novel peptides are not present in the conventional secreted (and circulating) IgE. These peptides provide antigenic sites for antibody binding. Thus, the invention further includes antibodies to such peptide segments, as well as such antibodies conjugated to cytotoxic agents, and their use in extracorporeal or in vivo therapy.

Abstract: Disclosed are monoclonal antibodies and related products which bind to the second variable region of HIV-1 gp120 and synthetic peptides and anti-idiotypic antibodies which induce endogenous production of antibodies with these same properties.

Abstract: Disclosed are immunofluorescence staining methods which increase the likelihood that antibodies expressed by a single B cell selected and sorted by fluorescence activated cell sorting are specific for the antigen of interest, and which also allow selection of B cells expressing antibodies of high affinity for the antigen of interest. The antigen-specific single B cells are to be used in a procedure which amplifies and selects their V.sub.H and V.sub.L sequences. The selection for B cells expressing antibodies to specific antigens is increased by labeling B cells with at least two antigen probes, where each antigen probe includes the antigen of interest and the difference between the two probes is that each is labeled with a different fluorochrome. The positive selection achieved using antigen probes with two different colors is preferably combined with a negative selection step, in which autofluorescent cells and sticky cells exhibiting fluorescence for the third irrelevant surface marker are excluded out.

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 or downregulate IgE-bearing lymphocytes, thus blocking IgE-mediated allergic reactions. Three different isoforms of the C-terminal segment of the human .epsilon. chain resulting from alternative mRNA splicings in the membrane exon region are disclosed, one of which is secreted and not membrane-bound.

Abstract: A method for producing antibodies specific for antigenic associated with the extracellular segment of the domain which anchors immunoglobulins to the B cell membrane is disclosed. The epitopes recognized by the antibodies of the invention are present on IgE-bearing B cells but not basophils or in the secreted, soluble form of IgE.

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. DNA constructs encoding chimeric antibodies, with murine variable regions and human constant regions, which bind to this epitope, can be produced and expressed in transfected mycloma cells.

Abstract: Disclosed are immunofluorescence staining methods which increase the likelihood that antibodies expressed by a single B cell selected and sorted by fluorescence activated cell sorting are specific for the antigen of interest, and which also allow selection of B cells expressing antibodies of high affinity for the antigen of interest. The selection for B cells expressing antibodies to specific antigens is increased by labeling B cells with at least two antigen probes, where each antigen probe includes the antigen of interest and the difference between the two probes is that each is labeled with a different fluorochrome. The specificity of sorting of the desired B cells can be further enhanced by staining those antigen-specific B cells which produce the immunoglobulin isotype (typically IgG), with targeting molecules reactive with B cell markers, such as .gamma. chain and CD19, that are conjugated with different fluorochromes.

Abstract: An antibody matrix immunoassay device for determination of number and proportion of subpopulations of leukocytes is described. The device can be used to evaluate and monitor the immune status of an individual and to diagnose and monitor the progression of AIDS.