Jacqueline Sharon

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The structure of the antigen-binding fragment (Fab) of an anti-p-azophenylarsonate monoclonal antibody, 36-71, bearing a major cross-reactive idiotype of A/J mice has been refined to an R factor of 24.8% at a resolution of 1.85 A. The previously solved partial structure of this Fab at a resolution of 2.9 A (Rose et al., 1990) was used as an initial model(More)
Two murine monoclonal antibodies (BE1 and BE2), produced by using leukemic helper T cells from a patient with cutaneous T-cell lymphoma (CTCL) as immunogens, reacted selectively with CTCL lymphocytes and some transformed cultured lymphocytes, as determined by radioimmunoassay (RIA) and indirect immunofluorescence (IIF). BE1 reacted significantly (P less(More)
Examination of the gel electrophoresis patterns of 14C-biosynthetically labeled immunoglobulin from C57BL/6 X BALB/c IgA hybridomas reveals that each of the monoclonal cell populations produces two different forms of IgA: molecules with heavy chains (H) and light chains (L) joined by disulfide bonds, as well as molecules with H and L being noncovalently(More)
We describe the expression and consistent production of a first target-specific recombinant human polyclonal antibody. An anti-Rhesus D recombinant polyclonal antibody, Sym001, comprised of 25 unique human IgG1 antibodies, was produced by the novel Sympress expression technology. This strategy is based on site-specific integration of antibody genes in CHO(More)
Libraries of Ab fragments have been produced by others from light and heavy chain cDNAs derived from populations of B lymphocytes and expressed in bacteria. However, such libraries have not been transferred to eukaryotic expression vectors to generate polyclonal libraries of intact glycosylated Abs that can mediate effector functions. We present a method(More)
Tularemia is caused by the Gram-negative facultative intracellular bacterium Francisella tularensis, which has been classified as a category A select agent-a likely bioweapon. The high virulence of F. tularensis and the threat of engineered antibiotic resistant variants warrant the development of new therapies to combat this disease. We have characterized(More)
An anti-idiotope monoclonal antibody (MAb), called CA1 (Ab2), was produced in mice against MAb 2C7, which recognizes a widely in vivo-expressed gonococcal lipooligosaccharide (LOS) epitope. Mice immunized with MAb CA1 initially had a 2.5-fold increase in IgG (12-fold after a booster) but no increase in IgM anti-LOS (Ab1') antibody. Control mice immunized(More)
GK1.5 is a rat mAb that recognizes the mouse CD4 Ag. It has been shown to deplete CD4+ cells in vivo and to be immunosuppressive. To evaluate the effect of the C region of this antibody in achieving cell depletion, chimeric antibodies, each having the rat GK1.5 V regions and one of the four mouse IgG C region isotypes, were compared with the native rat(More)
Tularemia is a severe infectious disease in humans caused by the Gram-negative bacterium Francisella tularensis (Ft). Because of its low infectious dose, high mortality rate, and the threat of its large-scale dissemination in weaponized form, development of vaccines and immunotherapeutics against Ft is essential. Ft lipopolysaccharide (LPS), which contains(More)
Binding constants of monomers of seven BALB/c IgM, four BALB/c IgA, and one C57BL/6 IgA anti-alpha (1 leads to 6) dextran hybridoma antibodies with dextran B512 and with isomaltoheptaose were determined by affinity electrophoresis. Bindings constants to dextran range from 1.52 X 10(5) to 4.43 X 10(5) ml/g for the five IgA monomers and from 1.70 X 10(3) to(More)