V L Woods

National Institute of Allergy and Infectious Diseases, Maryland, United States

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Publications (8)48.18 Total impact

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    ABSTRACT: Allotypes of membrane IgD of 27 strains of mice were determined with a series of anti-delta reagents, each capable of binding to the IgD of BALB/c spleen cells. One of these reagents is a newly defined allospecific rabbit anti-mouse-delta a. Typing with these reagents reveals the strain distribution of the previously described IgD.36 (Ig5.1) and IgD.43 (Ig5.4) specificities and demonstrates the existence of a new specificity, IgD.45 (Ig5.5). The results confirm the previous subdivision of the Igh-Ce haplotype into Igh-Ce, to which A mice are assigned, and Igh-Cn, to which NZB and NZW mice are assigned. In addition, it is shown that the Igh-Cd haplotype must also be subdivided. AKR mice, which express the a allele at the Igh-5(delta) locus, are designated as possessing the Igh-Cd haplotype while AL/N and C.AL20 mice, which have the e allele at the Igh-5(delta) locus, are assigned a new Igh-C haplotype designation, o.
    No preview · Article · Jan 1981 · The Journal of Immunology
  • V L Woods · I Scher · R Lieberman · W E Paul
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    ABSTRACT: Allotypic determinants expressed on membrane IgD of 27 strains of mice representing each of the major Igh-C haplotypes of inbred mice were examined with reagents specific for the IgD of mice of the b, e, and o Igh-C haplotypes. The distribution of two specificities, IgD.44 (Ig5.2) and IgD.37 (Ig5.3), recognized by two monoclonal anti-delta reagents was determined. In addition, a new specificity, IgD.46, expressed on mice of the o Igh-C type, but not of the b or a types, was detected by a BALB/c anti-AL/N spleen cell antiserum. The results also confirmed the description of the new Igh-C haplotype o, by demonstrating that the mice of this group express the IgD.37 determinant. This determinant is also expressed by mice of the b and e types, but not by mice of the d haplotype, from which the o haplotype was subdivided.
    No preview · Article · Jan 1981 · The Journal of Immunology
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    ABSTRACT: Four cell lines derived from spontaneous BALB/c lymphoma tumors were analyzed with regard to the type of their membrane immunoglobulins (Ig). Using lactoperoxidase iodination of membrane proteins combined with immunoprecipitation and electrophoresis on polyacrylamide gel, three of these cell lines (X16c, L10A and K46) were found to express the monomeric form of IgM and IgD as well as half molecules. One cell line (M12) lacked both IgM and IgD. The apparent mol. wt of the lymphoma micro chain was about 80 000 and exceeded the mol. wt. of 75 000 determined for micro chains secreted by myeloma cells. The mol. wt. of the delta heavy chain was found to be 66 000. Immunofluorescence showed that the L10A and X16c lines expressed lambda light chains on their cell surface. Another Ig-bearing cell line (K46) expressed both lambda and kappa chains. Thus, three out of the four B lymphomas examined expressed both IgM and IgD with light chains of the Lambda type. These results, together with our previous findings which demonstrate the presence of Ia and Fc receptors on the same cells, indicate that spontaneous B lymphomas in BALB/c mice are the malignant counterpart of mature B lymphocytes.
    No preview · Article · Jan 1981 · European Journal of Immunology
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    ABSTRACT: Heterologous anti-delta-chain antibodies have an adjuvant effect on specific in vivo humoral immune responses to simultaneously, or subsequently, injected antigens in the rat and rhesus monkey. We have used a hybridoma-secreted antibody that binds murine delta-chain of the allotype (4.22aM delta a) to study this phenomenon in the mouse and to investigate the mechanism of this effect. Injection of 4.22aM delta a into BALB/c mice removes almost all surface IgD (sIgD) from splenic B lymphocites. sIgD does not reappear until the serum level of 4.22aM delta a decreased 5-7 d after injection. 4.22aM delta a fails to induce detectable proliferation or to raise total serum Ig levels substantially above control values. However, 4.22aM dalta a injected 24 h before antigen elicits an approximately twofold enhancement of serum IgM and a 3- to 10-fold enhancement of serum IgG anti-trintriphenyl (TNP) antibodies in response to immunization with optimal doses of TNP-Ficoll or TNP-sheep red blood cells (TNP-SRBC). 4.22aM delta a injected 1 wk before or 3 d after TNP-SRBC, however, has no effect on IgG anti-TNP levels. The adjuvant effect of anti-delta-chain antibody was markedly decreased when suboptimal antigen doses were used. Furthermore, even in the case of TNP-Ficoll, a relatively T-independent antigen, the ability of 4.22aM dalta a to enhance the anti-TNP antibody response was T cell dependent. Our data suggest that the binding of anti-delta-chain antibody to cell sIgD may partially activate B lymphocytes and make them more capable of differentiating into antibody-secreting cells when stimulated by antigen-specific T cell help.
    Preview · Article · Oct 1980 · Journal of Experimental Medicine

  • No preview · Article · Feb 1980 · Immunological Reviews
  • S W Kessler · V L Woods · F D Finkelman · I Scher
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    ABSTRACT: The general structure, surface orientation, and location of allotypic determinants of mouse lymphocyte IgD have been deduced by enzymatic and immunochemical dissection of this molecule on the cell membrane. After limited trypsin digestion of IgD of the a (and cross-reacting c) and b allotypes, IgD was no longer detectable on cell surfaces by immunofluorescent staining with an antiserum against light chain determinants, an allotype specific heteroantiserum against IgDa, and a hybridoma antibody specific for the IgDb allotype. Immunoprecipitations performed with these reagents and m.w. analyses by polyacrylamide gel electrophoresis in sodium dodecyl sulfate, after lactoperoxidase-catalyzed cell radioiodination and trypsin digestion, indicated that the respective cleavage fragments were contained in the incubation medium and corresponded to the Fab portion of IgD. On the other hand, trypsin digestion reduced, but did not eliminate immunofluorescent staining with a heteroantiserum that bound IgD determinants common to all allotypes, and straining with two other hybridoma antibodies specific for the a and b allotypes of IgD was only minimally affected. Immunoprecipitations with these reagents indicated that the respective antigenic fragments, corresponding to the Fc portion of IgD, were retained on the cell membrane. Therefore, mouse lymphocyte IgD contains distinct allotypic determinants on both the Fab and Fc portions. Furthermore, it was determined that both fragments bore carbohydrate moieties by lentil lectin chromatography, and that cleavage took place NH2-terminal to a disulfide bond joining the two heavy chains in the Fc region. These findings point to a high degree of structural homology between mouse membrane IgD and human IgD myeloma proteins.
    No preview · Article · Jan 1980 · The Journal of Immunology
  • F D Finkelman · V L Woods · A Berning · I Scher
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    ABSTRACT: Although the mouse would provide an excellent experimental model for the study of serum IgD function, previous investigations have failed to detect serum IgD in this species. We have developed an immunofluorescence inhibition assay that has allowed us to identify and quantitate mouse serum IgD. Mouse sera or serum fractions were assayed for their abilities to inhibit staining of mouse spleen cells with an allotype-specific fluorescein isothiocyanate-labeled rabbit antibody against mouse cell-surface IgD (FITC-RaMδa), as analyzed with a fluorescence-activated cell sorter. FITC-RaMδa stains surface IgD+ spleen cells of mouse strains that have surface(s) sIgD of the a allotype, such as BALB/c, but not strains that have surface IgD of the b allotype, such as C57BL/6 or C.B20, which have the C57BL/6 CH genome on a BALB/c background. The staining of BALB/c lymphocytes by FITC-RaMδa was inhibited by BALB/c serum, but not by C57BL/6 or C.B20 serum. The staining was also not inhibited by BALB/c sera that had been adsorbed with rabbit anti-mouse Ig or a mouse hybridoma protein anti-mouse δ, or by BALB/c IgG, IgM, or IgA plasmacytoma proteins. These data strongly suggest that mice have IgD in their serum. Mouse serum IgD is probably secreted rather than shed from B cells, since amounts of serum IgD and splenic IgD in the same mice did not correlate with each other and serum IgD and shed sIgD had different density profiles.
    No preview · Article · Oct 1979 · The Journal of Immunology
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    ABSTRACT: Staphylococcal protein A and several different immunoglobulins have been radiolabeled to high specific activities (>106 cpm/μg) by reductive methylation with tritiated (3H) sodium borohydride. The proteins retain excellent functional and antigenic properties. The utility of these reagents in a variety of assays for cell surface antigens is illustrated. The results indicate that this radiolabeling procedure may become the method of choice for many cell surface and solution immunoassays.
    No preview · Article · Feb 1979 · Journal of Immunological Methods