Articoli di riviste: "Anti-idiotypic antibodies"

1

Nagpal, S., K. N. Shanthi, R. Kori, H. Schroder, D. D. Metcalfe e P. V. Subba Rao. "Induction of allergen-specific IgE and IgG responses by anti-idiotypic antibodies." Journal of Immunology 142, n. 10 (15 maggio 1989): 3411–15. http://dx.doi.org/10.4049/jimmunol.142.10.3411.

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Abstract In order to explore idiotypic, anti-idiotypic, and anti-anti-idiotypic responses to allergens, BALB/c mice were immunized with affinity-purified human idiotypic antibodies directed against a highly purified shrimp allergen. This resulted in the production of anti-idiotypic antibodies which were quantitated by using rabbit idiotypic antibodies raised against the same purified allergen. The mouse anti-idiotypic antibodies recognized shrimp-specific human idiotypic antibodies of the IgE isotype from 18 of 20 individuals, and IgG antibodies from 14 of 20 shrimp-sensitive patients. Immunization of BALB/c mice with affinity-purified, allergen-specific anti-idiotypic antibodies induced anti-allergen IgE and IgG responses in the absence of the allergen. This paper thus presents evidence that anti-idiotypic antibodies raised against allergen-specific idiotypic antibodies may substitute for the original allergen in the induction of allergen-specific idiotypic antibodies. The demonstration of shared idiotopes on IgG and IgE antibodies in the sera of shrimp-sensitive patients supports the use of allergen-specific anti-idiotypic antibodies as surrogate allergens.

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Ng, David S. S., e Gary E. Isom. "Anti-morphine anti-idiotypic antibodies". Biochemical Pharmacology 34, n. 16 (agosto 1985): 2853–58. http://dx.doi.org/10.1016/0006-2952(85)90006-1.

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3

Mermelstein, Norman, e Grant Morahan. "Assays to detect monoclonal anti-idiotypic anti-idiotypic antibodies". Journal of Immunological Methods 101, n. 1 (giugno 1987): 147. http://dx.doi.org/10.1016/0022-1759(87)90228-6.

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4

Lin, C., M. Musch, P. Meo, J. Zebrowitz, E. Chang e T. R. Kleyman. "Anti-idiotypic antibodies to delineate epitope specificity of anti-amiloride antibodies". American Journal of Physiology-Cell Physiology 267, n. 3 (1 settembre 1994): C821—C826. http://dx.doi.org/10.1152/ajpcell.1994.267.3.c821.

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Amiloride and related compounds have found widespread use as cation transport inhibitors. We have previously raised a series of polyclonal anti-amiloride antibodies using different amiloride-protein conjugates as immunogens, where amiloride was coupled to protein either through its guanidino moiety or through its 5-aminopyrazinyl moiety. The anti-amiloride antibodies recognized distinct sites on amiloride, and the site of attachment of amiloride to carrier protein was a critical factor in determining which part of the amiloride molecule was recognized by the anti-amiloride antibody. The specificity of binding of amiloride analogues to these polyclonal anti-amiloride antibodies mimicked the specificity of binding of amiloride analogues to selected isoforms of the epithelial Na+ channel or the Na+/H+ exchanger, suggesting that antigen binding site of these antibodies might be similar in structure to amiloride binding sites on selected Na+ transport proteins. We previously generated monoclonal anti-idiotypic antibodies RA2.4 and RA6.3 by an auto-anti-idiotypic approach, using amiloride coupled to albumin through the guanidinium moiety (amiloride-A1). We have now raised a series of monoclonal anti-idiotypic antibodies, T6, T26, T40, and T181, using amiloride coupled to keyhole limpet hemocyanin through the 5-aminopyrazinyl moiety (amiloride-A5) as an immunogen with the same auto-anti-idiotypic approach. These monoclonal anti-idiotypic antibodies recognized both polyclonal anti-amiloride-A1 and anti-amiloride-A5 antibodies, suggesting that idiotype-anti-idiotype interaction was not epitope restricted.(ABSTRACT TRUNCATED AT 250 WORDS)

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Juge-Aubry, CE, Hong Liang, Jochen Lang, John W. Barlow e Albert G. Burger. "Synthesis and characterization of anti-idiotypic anti-T4 antibodies". European Journal of Endocrinology 130, n. 1 (gennaio 1994): 107–12. http://dx.doi.org/10.1530/eje.0.1300107.

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Juge-Aubry CE, Liang H, Lang J, Barlow JW, Burger AG. Synthesis and characterization of anti-idiotypic anti-thyroxine antibodies. Eur J Endocrinol 1994;130:107–12. ISSN 0804–4643 We injected rabbits with purified monoclonal murine immunoglobulin (IgG1) or polyclonal anti-thyroxine antibodies (anti-T4) and polyclonal anti-triiodothyroacetic acid (anti-Triac) antibodies to stimulate the production of anti-idiotypic antibodies. Purified immunoglobulins from all five rabbits immunized with monoclonal primary antibodies were able to inhibit the interaction between [125I]T4 and the primary antibody. The preimmune sera were inactive. This effect was not due to endogenous T4 contamination or contamination with the injected primary antibody. Half-maximal inhibition of binding of primary antibody with anti-idiotype was between 1.6 and 30 μg of total immunoglobulins. Addition of normal mouse IgG1 did not alter the inhibitory effect of the anti-idiotypic antibody. suggesting that this effect is specific. These anti-idiotypic antibodies reacted differently with different polyclonal antibodies, reflecting the heterogeneous nature of polyclonal antibody populations. Polyclonal antibodies were less effective in stimulating anti-idiotypic antibody production. One polyclonal anti-T4 and one anti-Triac antibody produced weak anti-idiotypic antibody that had to be used at a concentration of > 600 μg of total immunoglobulins to be inhibitory. Both inhibited the binding of T4 to the monoclonal anti-T4 antibody. However, they were ineffective in inhibiting the function of their own antigen, the polyclonal anti-T4 or anti-Triac antibody. We tested the most potent anti-idiotypic antibodies for their ability to compete with T4 for other T4-binding proteins. Specific inhibition of T4 binding to thyroid-binding globulin was observed with half-maximal effect at approximately 450 μg of total IgG. The antibody was negative when tested against Transthyretin, rat liver deiodinase type I, triiodothyronine cell uptake and liver cytoplasmic triiodothyronine binding. In conclusion, the technique described herein allows production of anti-idiotypic anti-T4, which can be useful in the characterization of the range of iodothyronine-binding sites involved in thyroid hormone action. AG Burger, Unité de la Thyroïde, Hôpital Cantonal Universitaire, 1211 Genève 4, Switzerland

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6

Monroe, John G., e Mark I. Greene. "Anti-Idiotypic Antibodies and Disease". Immunological Investigations 15, n. 3 (gennaio 1986): 263–86. http://dx.doi.org/10.3109/08820138609026688.

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7

Couraud, P. O. "Anti-angiotensin II anti-idiotypic antibodies bind to angiotensin II receptor." Journal of Immunology 138, n. 4 (15 febbraio 1987): 1164–68. http://dx.doi.org/10.4049/jimmunol.138.4.1164.

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Abstract An anti-idiotypic serum from a rabbit immunized with one anti-angiotensin II (AII) monoclonal antibody (A25) was shown to identify a cross-reactive idiotope (CRI) shared by six anti-AII monoclonal antibodies, in addition to a binding site-associated private idiotope. This anti-idiotypic reagent bound to rat liver membranes bearing AII receptors; binding was abolished after pretreatment of the membranes with AII. In immunoblotting experiments with rat liver membranes, as well as with rat pituitary homogenates, a 63,000 +/- 2,000 dalton protein was revealed that co-migrated with the AII receptor. After purification by affinity chromatography on an immobilized CRI+-antibody (A41), anti-CRI antibodies could immunoprecipitate the hormone binding activity from detergent-treated rat liver membranes and still recognize the 63,000 dalton protein. In contrast, anti-idiotypic antibodies specific for the private idiotope failed to interact with the AII receptor. Similar results were obtained with a second anti-idiotypic serum produced by immunization with another CRI+ anti-AII monoclonal antibody (A22). The sharing of the CRI determinant between the AII receptor and anti-AII antibodies might account for the reactivity of anti-idiotypic antibodies towards the AII receptor.

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8

de Saint Basile, G., A. Durandy, G. Somme e C. Griscelli. "Idiotypy of human anti-Candida albicans antibodies: recurrence, presence of a cross-reactive autoanti-idiotypic-like activity, and role in the induction of specific in vitro antibody response." Journal of Immunology 138, n. 2 (15 gennaio 1987): 417–22. http://dx.doi.org/10.4049/jimmunol.138.2.417.

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Abstract Rabbit anti-idiotypic antibodies (L12) were raised against human anti-mannan of Candida albicans (CA) antibodies isolated from the serum of a normal donor. The absorbed anti-idiotypic antiserum bound to donor anti-CA mannan antibodies but not to control immunoglobulins. Binding was inhibited by CA mannan but not by other polysaccharide antigens. L12 was shown to cross-react with anti-CA mannan-isolated antibodies or with anti-CA antibody-containing sera from individuals unrelated to the donor. IgG fraction isolated from the donor serum was repeatedly absorbed on CA mannan Sepharose to remove anti-mannan antibodies. This IgG fraction (named autoanti-idiotypic fraction) blocked, in a dose-dependent fashion, the binding of rabbit anti-idiotype to donor anti-CA mannan antibodies. Moreover, this CP-depleted IgG fraction cross-reacted with public idiotypic determinants of unrelated anti-CA mannan antibodies. Finally, L12 induced sensitized lymphocytes to produce anti-CA mannan antibodies in vitro in the absence of antigen.

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Pasquali, J. L., T. Martin, A. M. Knapp, H. Levallois e A. Farradji. "Monoclonal rheumatoid factor-secreting cells in a patient with mixed cryoglobulinemia. Homogeneity and stability of the idiotypic production and in vitro idiotypic suppression." Journal of Immunology 143, n. 6 (15 settembre 1989): 1826–31. http://dx.doi.org/10.4049/jimmunol.143.6.1826.

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Abstract The potential therapeutic value of anti-idiotypic antibodies during B cell proliferations largely depends on the stability of the target Ig idiotopes. We investigated this stability in a clinical condition of so called nonmalignant monoclonal B cell proliferation, mixed cryoglobulinemia. The idiotypic profile of a single IgM kappa monoclonal auto-antibody with anti-IgG activity (rheumatoid factor (RF] which originated from a patient suffering from a nonmalignant mixed cryoglobulinemia was followed over a period of 3 yr. As judged from the reactivity of a panel of five different mouse monoclonal anti-idiotypic antibodies mapping the RF variable regions, there was no idiotypic change in the serum IgM RF. At a cellular level, in vitro stimulation of the patient's PBL gives rise to IgM kappa auto-antibodies that were shown to bear the same idiotypic determinants as the serum IgM kappa. We then investigated the effects of the anti-idiotypic antibodies on the in vitro IgM kappa production. When stimulated with PWM and in the presence of anti-idiotypic antibodies (10 micrograms/ml), the patient's PBL produced less IgM RF (18 to 62% inhibition). The same inhibition of IgM RF production was observed after EBV infection of the patient's PBL (from 19 to 90% inhibition). In both cases, the remaining IgM RF production was idiotypically indistinguishable from the serum IgM RF. The implications of the idiotypic stability and of the results of in vitro idiotypic manipulation could be important in view of both the understanding of nonmalignant cryoglobulinemia and of the possible therapeutic use of anti-idiotypic antibodies in diseases.

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Volkova, YE N., S. G. Morozov, YE V. Mitichkina, A. A. Grigoriyeva e I. V. Yelistratova. "Role of disorders related to idiotypic and anti-idiotypic interactions in slowing down the achievement of negative serologic reactions in patients with early onset forms of syphilis after specific therapy". Vestnik dermatologii i venerologii 90, n. 1 (24 febbraio 2014): 37–44. http://dx.doi.org/10.25208/0042-4609-2014-90-1-37-44.

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Goal. To study the humoral immunity state in patients with the slowed down achievement of negative serologic reactions after the treatment of early onset forms of syphilis by means of examining the blood serum level of idiotypic and anti-idiotypic antibodies to cardiolipin and p17 Treponema Pallidum antigenic protein. Materials and methods. The study involved 324 patients (39.5% male and 60.5% female) with the slowed down achievement of negative serologic reactions. Primary (idiotypic) antibodies to cardiolipin and p17 protein were obtained using immunochromatographic assays with the help of the Bio Logik LP system. Purified antibodies were concentrated using the ultrafiltration technique with the aid of the XM-100А membrane. To obtain the rabbit antiserum to p17 Treponema Pallidum protein, chinchilla rabbits were immunized using the commercial recombinant p17 protein. To determine anti-cardiolipin idiotypic antibodies in the blood serum, the ELISa method optimized for detecting anti-cardiolipin antibodies was applied. To determine anti-cardiolipin anti-idiotypic antibodies as well as idiotypic and anti-idiotypic antibodies to p17 Treponema Pallidum protein, the standard ELISA method was applied. The following antigens were used to process the pads: F(ab)2 fragments of anti-cardiolipin antibodies (5 μg/mL), recombinant р17 T. pallidum protein (5 μg/mL) and F(ab)2 fragments of antibodies to р17 T. pallidum protein (10 μg/mL). The level of antibodies was assessed based on the absorbancy and expressed in conventional activity units using the K coefficient being the absorbancy of the serum under examination to the mean absorbancy of control serums ratio. The K value exceeding 1.5 conventional units indicated the increased level of antibodies. Results. Patients with the slowed down achievement of negative serologic reactions demonstrated a selective increase in the level of anti-idiotypic antibodies (AIAB) relative to T. pallidum antigens, cardiolipin and p17 protein, vs. first-order antibodies, which points at abnormal mutual regulation between idiotypic antibodies (IAB) and AIAB; the discovered phenomenon lays the immunochemical basis for the formation of a self-sustaining “vicious circle” contributing to the induction of high levels of antibodies to treponema antigens even when the pathogen was destroyed.

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Dwyer, D. S., M. Vakil e J. F. Kearney. "Idiotypic network connectivity and a possible cause of myasthenia gravis." Journal of Experimental Medicine 164, n. 4 (1 ottobre 1986): 1310–18. http://dx.doi.org/10.1084/jem.164.4.1310.

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Extensive idiotypic connectivity has been discovered between the antibodies composing the immune responses against the acetylcholine receptor (AChR) and alpha-1,3-dextran. The idiotypic connections form an elaborate network linking these disparate antigen systems, and there is an hierarchical organization of the antibodies in this network. The key anti-Ids that interconnect these two responses are more crossreactive, lower-affinity antibodies. Interestingly, 15% of patients with MG, which is caused by autoantibodies against the AChR, have serum antibodies against DEX. Control sera are negative for anti-DEX antibodies. Certain anti-DEX antibodies also bind to anti-AChR antibodies via idiotypic interactions. These findings suggest a model for the initiation of autoimmunity in MG. Antibodies made in response to DEX epitopes on the surface of certain bacteria would elicit the production of anti-Ids. However, some of these anti-Ids would also be autoantibodies against the AChR. Thus, is some circumstances, autoimmunity may develop as a consequence of the normal operation of regulatory idiotypic networks.

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Dang, H., M. Fischbach e N. Talal. "Anti-idiotypic antiserum to monoclonal anti-Sm inhibits the autoantigen-induced proliferative response." Journal of Immunology 134, n. 6 (1 giugno 1985): 3825–30. http://dx.doi.org/10.4049/jimmunol.134.6.3825.

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Abstract Anti-idiotypic sera were produced in BALB/c mice against three established monoclonal anti-Sm antibodies. Inhibition assays showed that the anti-idiotypic antibodies recognized determinants that were present on all three monoclonal antibodies but not on normal mouse IgG from unimmunized BALB/c mice or myeloma proteins. Normal (+/+) and autoimmune (lpr/lpr) MRL/MpJ or C3H/HeJ mice were immunized with Sm in complete Freund's adjuvant. Immune T cells from the draining lymph nodes proliferated in response to the addition of Sm in vitro. Anti-idiotypic serum added to these cultures inhibited the proliferative response by 50 to 70%, whereas normal BALB/c serum had no effect. This inhibition of proliferation was antigen specific, because the anti-idiotypic serum did not inhibit the T cell proliferative response to an irrelevant antigen, TNP-KLH, or ovalbumin. Kinetic studies showed that the anti-idiotypic serum inhibited an early event in antigen-induced proliferative response, because the addition of serum late in culture did not cause any significant reduction in proliferation. The reduced proliferative response was due to direct action of the anti-idiotypic serum on the Lyt-1+, 2- T cell population.

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13

LIANG, SHAOHONG, PETER RIEBER, MARIE PREWETT, GERD RIETHMÜLLER, CHARLES PLETCHER, JAMES HOXIE, HILARY KOPROWSKI e DOROTHEE HERLYN. "Anti-idiotypic Antibodies Against Anti-CD4 Antibodies MT151 and OKT4A". Viral Immunology 4, n. 2 (gennaio 1991): 83–90. http://dx.doi.org/10.1089/vim.1991.4.83.

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Phillips, T. M. "High-performance immunoaffinity chromatographic detection of immunoregulatory anti-idiotypic antibodies in cancer patients receiving immunotherapy." Clinical Chemistry 34, n. 9 (1 settembre 1988): 1689–92. http://dx.doi.org/10.1093/clinchem/34.9.1689.

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Abstract Anti-idiotypic antibodies are regulatory antibodies responsible for the shutdown of active immune responses against growing tumor cells. In an attempt to study these antibodies, a technique for isolating specific anti-idiotypic antibodies by immunoaffinity chromatography was devised. Human anti-tumor antibodies were isolated by affinity absorption to fixed autologous tumor cells. These antibodies were biotinylated, immobilized on streptavidin-coated beads, and used as a ligand to isolate reactive anti-idiotypes from the plasma of patients during periods when immune reactivity against their tumors could not be detected. The isolated anti-idiotypes demonstrated the ability to react with the original antibodies and to inhibit their binding to autologous tumor cells. Thus functional anti-idiotypic antibodies can be isolated by immunoaffinity chromatography with the original idiotype as the ligand. This technique can be used to monitor regulatory antibodies in cancer patients receiving immunotherapy.

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SHAKIB, F. "Controlling allergy with anti-idiotypic antibodies". Clinical Experimental Allergy 25, n. 10 (ottobre 1995): 908–9. http://dx.doi.org/10.1111/j.1365-2222.1995.tb00389.x.

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Polonelli, L., S. Conti, M. Gerloni, W. Magliani, M. Castagnola, G. Morace e C. Chezzi. "‘Antibiobodies’: antibiotic-like anti-idiotypic antibodies". Medical Mycology 29, n. 4 (gennaio 1991): 235–42. http://dx.doi.org/10.1080/02681219180000351.

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Rico, M. J. "ANTI-IDIOTYPIC ANTIBODIES AS VACCINE CANDIDATES". Pediatric Infectious Disease Journal 8, n. 12 (dicembre 1989): 898. http://dx.doi.org/10.1097/00006454-198912000-00027.

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WHYTE, ANTHONY, e MING-WEI WANG. "Anti-Idiotypic Antibodies in Reproductive Immunology". American Journal of Reproductive Immunology 21, n. 2 (ottobre 1989): 54–56. http://dx.doi.org/10.1111/j.1600-0897.1989.tb01001.x.

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Nath, A., B. Slagle e J. S. Wolinsky. "Anti-idiotypic antibodies to rubella virus". Archives of Virology 107, n. 1-2 (marzo 1989): 159–67. http://dx.doi.org/10.1007/bf01313888.

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Cheung, Nai-Kong V., Adela Canete, Irene Y. Cheung, Jian-Nan Ye e Chongyuan Liu. "Disialoganglioside GD2 anti-idiotypic monoclonal antibodies". International Journal of Cancer 54, n. 3 (28 maggio 1993): 499–505. http://dx.doi.org/10.1002/ijc.2910540324.

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Rico, M. Joyce. "Anti-idiotypic Antibodies as Vaccine Candidates". Archives of Dermatology 125, n. 2 (1 febbraio 1989): 271. http://dx.doi.org/10.1001/archderm.1989.01670140123024.

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Umeda, M., I. Diego, E. D. Ball e D. M. Marcus. "Idiotypic determinants of monoclonal antibodies that bind to 3-fucosyllactosamine." Journal of Immunology 136, n. 7 (1 aprile 1986): 2562–67. http://dx.doi.org/10.4049/jimmunol.136.7.2562.

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Abstract Many monoclonal antibodies that react with the lacto-N-fucopentaose III (LNF III) antigenic determinant, Gal beta 1-4(Fuc alpha 1-3)GlcNAc beta 1-3Gal beta 1-4Glc, have been described recently. The terminal trisaccharide of this determinant, fucosyllactosamine, is present on glycolipids and glycoproteins and on the surface of granulocytes, monocytes, and other cells. To study the structural and genetic diversity of these antibodies, syngeneic anti-idiotypic monoclonal antibodies were produced in BALB/c mice against PMN 6, a monoclonal antibody directed against this sequence. Anti-idiotypic antibodies 6B1 and 6C4 reacted with 50% of a panel of 20 anti-LNF III monoclonal antibodies, whereas 6A3 reacted strongly only with PMN 6. This indicates that the determinants recognized by 6C4 and 6B1 represent major cross-reactive idiotopes of this family of antibodies. The binding of idiotypic antibodies to a glycolipid bearing this antigenic determinant was completely inhibited by the three anti-idiotypic antibodies, 6A3, 6B1, and 6C4. The idiotopes could be demonstrated on the heavy chain of the monoclonal antibodies by an antibody transfer technique when mild reducing conditions were employed, but a high concentration of reducing agent destroyed the idiotypic determinants. This suggests that the anti-idiotypic antibodies recognize conformational structures expressed on the heavy chain molecules. The binding of 18 monoclonal antibodies to two glycolipid antigens and to a fucosyllactosamine-bovine serum albumin conjugate was compared. Antibodies that possessed the 6C4 cross-reactive idiotope bound to fucosyllactosamine-bovine serum albumin more weakly than idiotype-negative antibodies (p = 0.001). This suggests that the 6C4-positive antibodies might represent germline structures.

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Park, Yoon-Sun. "Characterization of Anti-anti-idiotypic Antibodies (Ab3) Induced by Immunization of Anti-idiotypic Antibodies (Ab2) Mimicking Disialoganglioside GD2". Immune Network 3, n. 2 (2003): 118. http://dx.doi.org/10.4110/in.2003.3.2.118.

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Müller, S., H. T. Wang, S. V. Kaveri, S. Chattopadhyay e H. Köhler. "Generation and specificity of monoclonal anti-idiotypic antibodies against human HIV-specific antibodies. I. Cross-reacting idiotopes are expressed in subpopulations of HIV-infected individuals." Journal of Immunology 147, n. 3 (1 agosto 1991): 933–41. http://dx.doi.org/10.4049/jimmunol.147.3.933.

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Abstract In this study we have generated monoclonal anti-idiotypic antibodies against human monoclonal and polyclonal anti-HIV antibodies in seropositive sera. A human anti-gp41 mAb (H2, IgM kappa) was used to immunize BALB/c mice and to prepare hybridoma anti-antibodies that react with H2 and not with normal human IgM. Similar monoclonal anti-antibodies were made in BALB/c mice immunized with Ig fraction prepared from a pool of HIV-seropositive sera. Both kinds of anti-idiotypic antibodies reacted with antibodies in pools of seropositive sera and with individual seropositive sera but not with normal human Ig or seronegative sera. The Id-positive Ig from single donors were isolated on two different anti-Id immunoabsorbents and shown to bind to p24 and gp120, respectively. The detection and isolation of idiotypically cross-reactive human anti-HIV antibodies from seropositive donors demonstrated, for the first time, the existence of shared Id expressed by antibodies against HIV Ag. The utility of cross-reacting anti-idiotypic antibodies as tools to dissect the network regulation of the anti-viral immunity in AIDS is discussed.

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Uchigata, Y., B. S. Prabhakar, K. F. Salata, F. Ginsberg-Fellner e A. L. Notkins. "Human monoclonal multiple-organ-reactive autoantibodies distinguished by mouse monoclonal anti-idiotypic antibodies: expression of idiotopes in humans with and without autoimmune diseases." Journal of Immunology 138, n. 12 (15 giugno 1987): 4218–21. http://dx.doi.org/10.4049/jimmunol.138.12.4218.

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Abstract Previously we reported on the production and characteristics of a number of human monoclonal autoantibodies. All of these autoantibodies were of the IgM class and reacted with antigens in multiple organs. In this study we generated IgG murine monoclonal anti-idiotypic antibodies against five human monoclonal autoantibodies, (i.e., MOR-h2, MOR-h3, MOR-h4, CG1, and CG2). These anti-idiotypic antibodies reacted strongly with the corresponding human monoclonal autoantibody, but minimally or not at all with other human monoclonal autoantibodies. By using these anti-idiotypic antibodies as probes, we screened sera obtained from normal individuals and patients with insulin-dependent diabetes mellitus, Hashimoto's thyroiditis, and systemic lupus erythematosus for the expression of idiotopes. Our study showed that the idiotopes recognized by three of the anti-idiotypic antibodies, i.e., anti-CG1, anti-CG2, and anti-MOR-h2, were not expressed, but the idiotopes recognized by two of the anti-idiotypic antibodies, i.e., anti-MOR-h3 and anti-MOR-h4, were expressed in normal individuals. In patients with autoimmune disorders, there was no increase in the expression of the CG1, CG2, and MOR-h2 idiotopes, but 45 and 23% of the patients with systemic lupus erythematosus showed a significant increase in the expression of the MOR-h3 and MOR-h4 idiotopes respectively. These findings show that there is widespread expression in the B cell repertoire of certain autoantibody-associated idiotopes.

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Osheroff, P. L., T. R. Chiang e D. Manousos. "Interferon-like activity in an anti-interferon anti-idiotypic hybridoma antibody." Journal of Immunology 135, n. 1 (1 luglio 1985): 306–13. http://dx.doi.org/10.4049/jimmunol.135.1.306.

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Abstract We describe here an anti-idiotypic hybridoma antibody directed against affinity-purified rabbit idiotypic antibodies (Rb-Id) to a homogeneous protein, the recombinant human leukocyte A interferon (rIFN-alpha A). The supernatant of the hybridoma, designated 3-1B, was able to inhibit the neutralization of rIFN-alpha A activity by the idiotypic antibodies. An in vivo passage of uncloned 3-1B cells yielded hybridoma cells (presumably a subclone), designated 3B1, the supernatant of which exhibited interferon-like antiviral activity with both bovine kidney (MDBK) cells and human amnion (WISH) cells. This activity could be absorbed by polymer-bound goat anti-mouse immunoglobulin serum and by Rb-Id coupled to Affi-Gel 10, and could be partially eluted from the latter at pH 2.5. The anti-idiotypic hybridoma antibody was able to compete with 125I-rIFN-alpha A for binding to the Rb-Id and also to interferon receptor-bearing MDBK cells. The clinical significance of an interferon-like anti-idiotypic antibody is discussed.

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Jiang, Wei, Henriette Macmillan, Anne-Marie Madec e Elizabeth D. Mellins. "Purification and characterization of GAD65-specific monoclonal autoantibodies". F1000Research 4 (29 maggio 2015): 135. http://dx.doi.org/10.12688/f1000research.6467.1.

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Autoantibodies against antigens expressed by insulin-producing β cells are circulating in both healthy individuals and patients at risk of developing Type 1 diabetes. Recent studies suggest that another set of antibodies (anti-idiotypic antibodies) exists in this antibody/antigen interacting network to regulate auto-reactive responses. Anti-idiotypic antibodies may block the antigen-binding site of autoantibodies or inhibit autoantibody expression and secretion. The equilibrium between autoantibodies and anti-idiotypic antibodies plays a critical role in mediating or preventing autoimmunity. Herein, using GAD65/anti-GAD65 autoantibodies as a model system, we aimed at establishing reliable approaches for purification of highly pure autoantibodies for the downstream investigation of molecular mechanisms underlying such a network.

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Chamat, S., J. Hoebeke, L. Emorine, J. G. Guillet e A. D. Strosberg. "The immune response towards beta-adrenergic ligands and their receptors. VI. Idiotypy of monoclonal anti-alprenolol antibodies." Journal of Immunology 136, n. 10 (15 maggio 1986): 3805–11. http://dx.doi.org/10.4049/jimmunol.136.10.3805.

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Abstract Four murine monoclonal antibodies specific for alprenolol, a synthetic beta-adrenergic ligand, with different binding properties towards alprenolol and other beta-adrenergic antagonists and agonists (as described in a previous report) were used to induce anti-idiotypic responses in rabbits and mice. Three of the rabbit anti-idiotypes inhibited, and one increased the binding of tritiated dihydroalprenolol to the Ab1 against which they were induced. The syngeneic mouse anti-idiotypes all had an inhibitory effect on the ligand binding to their corresponding Ab1. Cross-reactivity tests of the xenogeneic and syngeneic anti-idiotypes were positive only for two monoclonal anti-alprenolol antibodies. Cross-reaction could be shown neither on a panel of 15 other monoclonals, nor on polyclonal anti-alprenolol antibodies of the BALB/c and the C57BL/10 mice. These results suggest that the immune response against alprenolol results in antibodies with mostly private idiotypic determinants. Moreover, the properties of the anti-idiotypic response against the same monoclonal antibody seem to be different according to the species used for anti-idiotypic induction.

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29

Linthicum, D. S., M. B. Bolger, P. H. Kussie, G. M. Albright, T. A. Linton, S. Combs e D. Marchetti. "Analysis of idiotypic and anti-idiotypic antibodies as models of receptor and ligand." Clinical Chemistry 34, n. 9 (1 settembre 1988): 1676–80. http://dx.doi.org/10.1093/clinchem/34.9.1676.

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Abstract Antibodies to small bioactive ligands and peptides may mimic the binding characteristics of the natural receptor; in turn, the anti-idiotypic antibodies generated against the binding sites of such anti-ligand antibodies may mimic some aspects of small bioactive ligands and peptides. Among the several levels of investigation of such antibody-receptor networks are (a) the quantitative structure-activity relationships of ligand binding to antibody as compared with natural receptor; (b) the molecular modeling of antibody-receptor binding sites and the genomic basis for such structures; and (c) the characteristics of the molecular mimicry exhibited by "mimetopes" on anti-idiotypic antibodies. To illustrate the analysis encountered at each of these levels, we discuss here antibody and anti-idiotypic systems that are directed to small neuroactive ligands and their receptors.

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30

Sharon, J. "Structural characterization of idiotopes by using antibody variants generated by site-directed mutagenesis." Journal of Immunology 144, n. 12 (15 giugno 1990): 4863–69. http://dx.doi.org/10.4049/jimmunol.144.12.4863.

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Abstract Four anti-idiotopic mAB, 107, MB, AI, and AD8, react with mouse hybridoma protein 36-65 specific for the hapten p-azophenylarsonate. The four antiidiotypic antibodies do not react with hybridoma protein 36-71, a somatically mutated variant of 36-65 whose H and L chain V region sequence differs at 19 amino acid positions. To determine which regions of 36-65 are important for the interaction with each of the four anti-idiotypic antibodies, variants of 36-65 containing one or more of the 36-71 substitutions were generated by oligonucleotide-directed mutagenesis of the rearranged 36-65 H chain V region gene, followed by expression of mutant proteins containing either the 36-65 or the 36-71 L chain in transfected hybridoma cells. Idiotypic characterization of the mutant proteins showed that reactivity correlates with the 36-65 H chain, but some contributions from the 36-65 L chain come into play. In the 36-65 H chain V region, idiotopes were mapped to the first and third complementarity-determining regions for anti-idiotypic antibodies 107, MB, and AI, and to all three complementarity-determining regions for anti-idiotypic antibody AD8. The binding of all four anti-idiotypic antibodies to hybridoma protein 36-65 was hapten inhibitable. However, a comparison between the effect of individual 36-71 substitutions on idiotope expression and their effect on Ag-binding affinity suggests that none of the four anti-idiotypic antibodies bodies mimics the structure of Ag.

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31

Jeske, D., E. C. Milner, O. Leo, M. Moser, J. Marvel, J. Urbain e J. D. Capra. "Molecular mapping of idiotopes of anti-arsonate antibodies." Journal of Immunology 136, n. 7 (1 aprile 1986): 2568–74. http://dx.doi.org/10.4049/jimmunol.136.7.2568.

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Abstract (sommario):

Abstract As part of understanding molecular function in structural terms, we have been attempting to map the idiotypic topography of specific anti-arsonate (Ars) antibodies. A panel of anti-Ars hybridomas of which the complete primary sequences are known were used. These molecules show a varied reactivity profile with a panel of monoclonal anti-idiotypic antibodies. By judicious chain recombination experiments and chemical modifications that altered this reactivity profile, we were able to identify particular amino acid residues or discreet regions of anti-Ars antibodies as having crucial roles in the expression of idiotypic determinants. Idiotopes were mapped to the heavy chain second hypervariable region and D segment, and to the light chain first and third hypervariable regions.

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32

Devyaltovskaya, M. G. "Links of pathogenesis of pre- and perinatal damage of the children’s brain". Proceedings of the National Academy of Sciences of Belarus, Medical series 16, n. 1 (12 marzo 2019): 88–92. http://dx.doi.org/10.29235/1814-6023-2019-16-1-88-92.

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Abstract (sommario):

A correlation analysis was made of the relationships between the structural changes in the brain and the content of idiotypic, anti-idiotypic antibodies to the soluble calcium-binding protein of the nervous tissue S100 in the serum of 318 children of the frst year of life with consequences of pre- and perinatal brain damage. We established the conjugation between the structural pathology of the brain, represented by cystic-atrophic changes, calcifcations, glia in the brain substance, periventricular leukomalacia, periventricular cysts, expansion of the ventricular system, congenital malformations of the brain, and the content of idiotypic, anti-idiotypic antibodies to the S100 protein in the serum blood of children 3, 6, 9, 12 months old. The concentration of idiotypic and anti-idiotypic antibodies to the protein of the nervous tissue S100 in the serum reﬂects the severity of destructive processes in the brain substance. Autoimmune processes are one of the mechanisms that lead to the structural damage to the brain in children with adverse pre- and perinatal factors.

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33

Davidson, A., A. Smith, J. Katz, J. L. Preud'Homme, A. Solomon e B. Diamond. "A cross-reactive idiotype on anti-DNA antibodies defines a H chain determinant present almost exclusively on IgG antibodies." Journal of Immunology 143, n. 1 (1 luglio 1989): 174–80. http://dx.doi.org/10.4049/jimmunol.143.1.174.

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Abstract (sommario):

Abstract We have previously reported two anti-idiotypic antibodies, 3I and 8.12, that recognize L chain determinants on anti-DNA antibodies. We have generated a new anti-idiotypic antibody, F4, that recognizes a H chain determinant on cationic anti-DNA antibodies. F4 reactivity is present in high titer in serum of approximately 60% of SLE patients and on 84 of 706 myeloma proteins. It is preferentially associated with 3I reactive L chains. Furthermore, antibodies bearing both the F4 and 3I idiotypic determinants preferentially bind DNA. Amino acid sequencing of H chains isolated from four F4-reactive myeloma proteins suggests that they derive from two currently identified VH gene families. F4 reactivity is restricted almost exclusively to Ig of the IgG isotype suggesting that F4 may recognize either a somatically mutated hypervariable region or a variable region used late in the immune response. F4, therefore, represents a new idiotypic family preferentially associated with auto-Ag specificity and having features of an Ag-driven immune response.

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34

Diakun, K. R., e K. L. Matta. "Synthetic antigens as immunogens: Part III. Specificity analysis of an anti-anti-idiotypic antibody to a carbohydrate tumor-associated antigen." Journal of Immunology 142, n. 6 (15 marzo 1989): 2037–40. http://dx.doi.org/10.4049/jimmunol.142.6.2037.

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Abstract These investigations are centered on the development of anti-idiotypic and anti-anti-idiotypic antibodies to a structurally defined carbohydrate Ag, 3-O-alpha-L-fucopyranosyl-beta-D-galactopyranoside (Fuc alpha 1----3Gal). Biologic association of this disaccharide Ag structure had previously been found with tissues from areas of benign and malignant disease of the colon and breast. The exquisite specificity of binding of the original Ab1, with the antibody-Ag reaction requiring both fucose and galactose and the alpha-anomeric 1----3 linkage, was repeated with the anti-anti-idiotypic antibodies. This information indicates that although antigenic mimicry of anti-idiotypic for Ag is accomplished using amino acids in place of sugars, the specificity pattern can be precisely reproduced.

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35

Legrain, P., e G. Buttin. "The VK gene expressed by BALB/c ABPC48 cross-reactive idiotypes induced by anti-idiotypic immunization is identical to that of BALB/c anti-oxazolone and A/J anti-arsonate antibodies." Journal of Immunology 134, n. 5 (1 maggio 1985): 3468–73. http://dx.doi.org/10.4049/jimmunol.134.5.3468.

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Abstract (sommario):

Abstract Anti-idiotypic immunization triggers the production of antibodies that are structurally related to the idiotype. We have shown that the heavy chain variable regions of antibodies produced after anti-ABPC48 (A48) anti-idiotypic immunization of BALB/c mice are homologous to that of A48, except for the third hypervariable region. We present here partial light chain sequences of A48 and of antibodies induced by anti-idiotypic immunization. Nearly perfect homology is found, suggesting that these chains are the products of genes derived from a unique VK germ-line gene. These observations indicate that the H and L hypervariable regions contribute to define the structure of A48 idiotopes. Remarkably, the VK sequence we identify is the same as that described for anti-arsonate and anti-oxazolone antibodies. We discuss the relative importance of particular amino acids for idiotype expression and antigen-binding activity.

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36

Phillips, S. M., E. G. Fox, N. G. Fathelbab e D. Walker. "Epitopic and paratopically directed anti-idiotypic factors in the regulation of resistance to murine schistosomiasis mansoni." Journal of Immunology 137, n. 7 (1 ottobre 1986): 2339–47. http://dx.doi.org/10.4049/jimmunol.137.7.2339.

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Abstract (sommario):

Abstract In this study we investigated aspects of targets and regulatory mechanisms of immunologically mediated resistance to schistosomiasis. The interactions of antigen, monoclonal antibodies (MAb), and anti-idiotypic antibodies were studied by using competitive inhibition ELISA, radioimmunoprecipitation, and direct-binding ELISA techniques. MAb, either protective or nonprotective against challenge with Schistosoma mansoni, recognize either discrete or shared epitopes. MAb that recognize the same specific epitope may or may not express the ability to adoptively transfer resistance to syngeneic recipients. These results suggest that the functional as well as the epitopic specificity must be considered in an evaluation of protective mechanisms. The antibodies also can be characterized by both unique and cross-reacting idiotypic determinants. In addition, a relationship between antigen and anti-idiotypic antibody activity has been demonstrated. The immunologic analogy between antigenic epitopes and anti-idiotypic antibodies has been demonstrated by the ability of these two moieties to reciprocally inhibit the recognition of paratope-associated idiotypes, expressed by the protective MAb. This anti-idiotypic activity can be demonstrated in serum of infected animals. In this study we have identified two specific epitopes related to protection, and we illustrate here the steric relationship between antigen and anti-idiotypic antibody. The presence of idiotypically directed regulatory pathways within actively infected animals suggests that the immune response can be differentially regulated at the clonal level.

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37

Gifford, L. A., T. Chernov-Rogan, J. P. Harvey, C. H. Koo, D. W. Goldman e E. J. Goetzl. "Recognition of human polymorphonuclear leukocyte receptors for leukotriene B4 by rabbit anti-idiotypic antibodies to a mouse monoclonal antileukotriene B4." Journal of Immunology 138, n. 4 (15 febbraio 1987): 1184–89. http://dx.doi.org/10.4049/jimmunol.138.4.1184.

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Abstract (sommario):

Abstract Rabbit anti-idiotypic IgG antibodies to the combining site of a mouse monoclonal IgG2b antibody to leukotriene B4 (LTB4) cross-reacted with human polymorphonuclear (PMN) leukocyte receptors for LTB4. Anti-idiotypic IgG and Fab both inhibited the binding of [3H]LTB4, but not [3H]N-formylmethionyl-leucylphenylalanine (fMLP), to PMN leukocytes with similar concentration-effect relationships, whereas neither nonimmune rabbit IgG nor Fab had any inhibitory activity. At a concentration of anti-idiotypic IgG that inhibited by 50% the binding of [3H] LTB4 to PMN leukocytes, the antibodies preferentially recognized high affinity receptors. Anti-idiotypic IgG and Fab inhibited PMN leukocyte chemotactic responses to LTB4, but not fMLP, with concentration-effect relationships resembling those characteristic of the inhibition of binding of [3H] LTB4, without altering the LTB4-induced release of beta-glucuronidase. Chemotaxis and increases in the cytoplasmic concentration of calcium equal in magnitude to those elicited by optimal concentrations of LTB4 were attained at respective concentrations of anti-idiotypic IgG equal to and 1/25 the level required for inhibition of binding of [3H]LTB4 by approximately 50%. Thus, the anti-idiotypic antibodies bound to PMN leukocyte receptors for LTB4 with a specificity, preference for high affinity sites, and capacity to alter PMN leukocyte functions that were similar to LTB4.

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38

Forsyth, R. B., e G. W. Hoffmann. "A study of auto-anti-idiotypes to BSA." Journal of Immunology 145, n. 1 (1 luglio 1990): 215–23. http://dx.doi.org/10.4049/jimmunol.145.1.215.

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Abstract (sommario):

Abstract In order to study the idiotypic relationships between the antibody populations produced in different species during normal immune responses to ordinary protein Ag, we raised immune sera in mice and chickens by using three protein Ag: BSA, keyhole limpet hemocyanin, and diphtheria toxoid. An avidin-biotin ELISA was used to measure idiotypic binding between antibody populations from these sera. We found that the chicken sera contained auto-anti-idiotypes (AAI) against Ag-specific antibodies that were present in the same serum and that co-purified with those antibodies on Ag-Sepharose columns. These AAI were present in secondary response chicken anti-BSA serum at levels comparable with those of the anti-BSA antibody. The chicken AAI also react specifically with Id in mouse anti-BSA serum. The mouse anti-BSA serum completely inhibits the binding between the chicken Id and AAI. This similarity between the Id of whole populations of antibodies produced in two distantly related species, in the absence of any manipulation with idiotypic or anti-idiotypic reagents, suggests that the AAI detected in this way are internal image antibodies. It indicates there is positive selection for such AAI to be internal images.

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39

Abbott, W. M., e P. G. Strange. "Attempts to obtain anti(D2 dopamine receptor) antibodies via the anti-idiotypic route". Biochemical Journal 238, n. 3 (15 settembre 1986): 817–23. http://dx.doi.org/10.1042/bj2380817.

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Abstract (sommario):

Five stable hybridomas have been obtained that secrete monoclonal antibodies against the D2-dopamine receptor-selective drug spiperone. Each monoclonal antibody has been characterized in terms of its ability to bind a range of dopamine-receptor-selective ligands. One monoclonal antibody has been purified by Protein A affinity chromatography and used to immunize mice. Anti-idiotypic antisera and one hybridoma secreting an anti-idiotypic monoclonal antibody were obtained and shown to inhibit [3H]spiperone binding to the anti-spiperone antibody used for immunization. Neither the antisera nor the anti-idiotypic monoclonal antibody, however, inhibited binding of [3H]spiperone to D2-dopamine receptors.

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40

Kawasaki, H., K. Zupko, B. Diamond, M. Minami e M. E. Dorf. "Antibody inhibition of suppressor cell induction." Journal of Immunology 138, n. 7 (1 aprile 1987): 2063–68. http://dx.doi.org/10.4049/jimmunol.138.7.2063.

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Abstract The IJ genetic restrictions of suppressor T (Ts) cells are controlled by H-2-related determinants that are expressed on antigen-presenting cells. This has led to the hypothesis that Ts cells carry receptors for a self H-2-related ligand that is expressed on specialized antigen-presenting cells. We refer to this H-2-related ligand as the IJ interacting molecule. This report evaluates the ability of rabbit antibodies directed against idiotypes on monoclonal anti-IJ antibodies (the latter are presumably reactive with the Ts cell receptor) to bind IJ interacting molecule and to inhibit antigen presentation to Ts cells. Such anti-idiotypic reagents were prepared against T cell-reactive monoclonal anti-IJk and anti-IJd antibodies. The F(ab')2 fragments of these anti-idiotypic reagents blocked Ts cell induction. The inhibition was haplotype specific and mapped to the IJ region. The anti-idiotypic antibodies blocked the generation of Ts1, Ts2, and Ts3 cells. The cellular target of the blocking activity mediated by these anti-idiotypic antibodies is a macrophage. This was shown by using a cloned macrophage hybridoma line for both Ts induction and absorption of antibody activity. The combined data support the concept that macrophages express IJ interacting determinants that are responsible for Ts cell induction.

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41

Haasemann, M., J. Buschko, A. Faussner, A. A. Roscher, J. Hoebeke, R. M. Burch e W. Müller-Esterl. "Anti-idiotypic antibodies bearing the internal image of a bradykinin epitope. Production, characterization, and interaction with the kinin receptor." Journal of Immunology 147, n. 11 (1 dicembre 1991): 3882–92. http://dx.doi.org/10.4049/jimmunol.147.11.3882.

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Abstract mAb against bradykinin, the prototypic member of the kinin family of vasodilator peptides, were generated by somatic cell fusion. The antibodies were isotyped as IgG1, kappa-type, and their target epitopes mapped with bradykinin, lysyl-bradykinin (kallidin), kinin receptor antagonists, and fragments thereof, revealing three distinct sets of mAb, i.e., mAb against bradykinin (MBK)1, MBK2, and MBK3. Comparison of the immunologic binding affinities and the known pharmacologic binding specificities of bradykinin derivatives disclosed a striking similarity in the binding profiles of mAb MBK3 and the B2 type of the kinin receptor. Anti-idiotypic antibodies against MBK1, MBK2, and MBK3 were raised in rabbit and sheep. Inhibition and competition experiments on the level of the Ag (ligand), the idiotype, and the anti-idiotype demonstrated the mutual specificity of the network system components. Anti-idiotypic antibodies against MBK3 recognized a particular idiotope that was conformation-dependent and associated with the Ag binding site of the antibody. Binding of anti-idiotypic antibodies to the B2 receptor expressed by human foreskin fibroblasts and guinea pig ileum demonstrated that the anti-idiotypes cross-react with the corresponding receptor across species. Specific stimulation of the inositol phosphate pathway in human fibroblasts and of the PG pathway in mouse fibroblasts, respectively, and inhibition of the latter effect by the B2 kinin receptor antagonist NPC 567 indicated that the anti-idiotypes bear the internal image of a bradykinin epitope. Furthermore, antibodies of the third generation (anti-anti-idiotypic antibodies) recognized the authentic Ag, i.e., bradykinin. Hence, the anti-idiotypic approach provides powerful tools to probe for the hitherto poorly characterized B2 kinin receptor.

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42

POLONELLI, L., R. LORENZINI, F. BERNARDIS, M. GERLONI, S. CONTI, G. MORACE, W. MAGLIANI e C. CHEZZI. "Idiotypic Vaccination: Immunoprotection Mediated by Anti-idiotypic Antibodies with Antibiotic Activity". Scandinavian Journal of Immunology 37, n. 1 (gennaio 1993): 105–10. http://dx.doi.org/10.1111/j.1365-3083.1993.tb01671.x.

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43

Poggianella, Monica, Robert Bernedo, Sandra Oloketuyi e Ario de Marco. "Nanobodies Selectively Binding to the Idiotype of a Dengue Virus Neutralizing Antibody Do Not Necessarily Mimic the Viral Epitope". Biomolecules 13, n. 3 (17 marzo 2023): 551. http://dx.doi.org/10.3390/biom13030551.

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Abstract (sommario):

Vaccination against dengue virus is challenged by the fact that a generic immune response can induce antibody-dependent-enhancement (ADE) in secondary infections. Only some antibodies targeting a quaternary epitope formed by the dimerization of the virus protein E possess sufficient neutralizing capacity. Therefore, the immunization with anti-idiotypic antibodies of neutralizing antibodies might represent a safe vaccination strategy. Starting from a large pre-immune library, we succeeded in isolating a wide set of anti-idiotypic nanobodies characterized by selective and strong binding to the paratope of the neutralizing antibody 1C10. However, the mice immunized with such constructs did not produce effective antibodies, despite at least some of them eliciting an immune response selective for the nanobody variable regions. The results suggest that complex conformational epitopes might be difficult to be recreated by anti-idiotypic structures. The selection process of the anti-idiotypic candidates might be optimized by applying epitope mapping and modeling approaches aimed at identifying the key residues that is necessary to bind to trigger selective immune response.

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44

Iribe, H., H. Kabashima e T. Koga. "Antibody response against a possible arthritogenic epitope on human type II collagen induced by anti-idiotypic antibody." Journal of Immunology 142, n. 5 (1 marzo 1989): 1487–94. http://dx.doi.org/10.4049/jimmunol.142.5.1487.

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Abstract We reported the presence of three distinct epitopes commonly present on murine and human type II collagen (CII), observed using mAb. To investigate the possible involvement of these epitopes in collagen-induced arthritis, we raised rabbit anti-idiotypic antibodies that may bear the internal image of these epitopes. Anti-idiotypic antibodies developed against three anti-CII mAb designated as 1-5, 2-14, and 2-15 were demonstrated to recognize idiotype expressed on Ag-binding site (paratope) of their related mAb. Anti-CII antibody response specific for a given epitope could be induced in DBA/1J mice upon immunization with anti-idiotypic antibodies coupled to keyhole limpet hemocyanin. Anti-idiotypic antibody to 1-5 antibody in particular could stimulate all DBA/1J mice for production of anti-CII antibody possessing Ag specificity and idiotype similar to those of 1-5 antibody. Although the mice immunized with anti-1-5 antibody alone did not develop arthritis, they did show a much more enhanced antibody response against a given epitope than did control mice non-treated with anti-idiotypic antibody upon the subsequent immunization with human CII. Some of the mice immunized with anti-1-5 antibody and challenged with human CII developed arthritis, whereas the control mice did not. These findings strongly suggest that a common epitope recognized by 1-5 antibody might be involved in the induction of arthritis.

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45

Sumida, T., e M. Taniguchi. "Novel mechanisms of specific suppression of anti-hapten antibody response mediated by monoclonal anti-carrier antibody." Journal of Immunology 134, n. 6 (1 giugno 1985): 3675–81. http://dx.doi.org/10.4049/jimmunol.134.6.3675.

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Abstract (sommario):

Abstract The cellular mechanisms of the antibody-induced suppression of immune responses were analyzed in the keyhole limpet hemocyanin (KLH) system. Some of the monoclonal anti-KLH antibodies, like KLH-specific suppressor T cell factor (KLH-TsF), were demonstrated to suppress the anti-2,4-dinitrophenyl IgG but not IgM plaque-forming cell responses in a KLH-specific and H-2-restricted manner. The anti-KLH antibodies with suppressive activity reacted with, and in turn, stimulated the suppressor hybridoma (34S-281) with the anti-idiotypic receptor complementary to the idiotypic KLH-TsF of the inducer type. Moreover, because the suppressive activity of the anti-KLH antibody was completely abolished by the treatment of responding spleen cells with anti-Lyt-2 and complement, it was apparent that the suppressive antibody activated suppressor T cell pathways. The isotype or affinity of antibodies is not related to the suppressive activity, because suppressive and nonsuppressive antibodies possess a similar affinity belonging to the same Ig isotypes. It also has been demonstrated that the Fc portion is not the functional site, because the F(ab')2 fragment still has the activity. The antibody specificity is found to be important for determining whether the antibody is suppressive or not. In fact, anti-KLH 26, but not other antibodies without activity, recognizes the particular KLH epitope seen by KLH-TsF, and exclusively interacts with the anti-idiotypic suppressor T cells. Thus, the anti-idiotypic suppressor T cell receives signals both from the suppressive anti-KLH antibody and from KLH-TsF, and transmits the antibody-induced suppressor signals to the effector-suppressor pathway. The size of the repertoire of anti-idiotypic suppressor T cells involved in the suppression seems to be very limited, because only four out of 120 monoclonal anti-KLH antibodies were found to have suppressor activity. The possible mechanisms of the cell interaction mediated by the suppressive antibody are discussed.

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46

Verma, N. K., R. Sodhi e Y. S. Rajput. "Anti-idiotypic Antibodies against Bovine Growth Hormone". Asian-Australasian Journal of Animal Sciences 16, n. 5 (1 gennaio 2003): 732–37. http://dx.doi.org/10.5713/ajas.2003.732.

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47

Polonelli, L., e G. Morace. "Yeast killer toxin-like anti-idiotypic antibodies." Journal of Clinical Microbiology 26, n. 3 (1988): 602–4. http://dx.doi.org/10.1128/jcm.26.3.602-604.1988.

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48

Ferrone, Soldano. "Anti-idiotypic monoclonal antibodies as therapeutic vaccines". Melanoma Research 6, n. 2 (aprile 1996): 179. http://dx.doi.org/10.1097/00008390-199604000-00014.

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49

Gramsch, C., R. Schulz, S. Kosin e A. Herz. "Monoclonal anti-idiotypic antibodies to opioid receptors." Journal of Biological Chemistry 263, n. 12 (aprile 1988): 5853–59. http://dx.doi.org/10.1016/s0021-9258(18)60644-1.

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50

Haasemann, M., J. Buschko, A. Faussner, A. A. Roscher, J. Hoebeke, R. Burch e W. Müller-Esterl. "Anti-Idiotypic Antibodies Against the Kinin Receptor". Journal of Cardiovascular Pharmacology 20, Supplement 9 (1992): S47—S54. http://dx.doi.org/10.1097/00005344-199200209-00010.

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