Academic literature on the topic 'Anti-idiotypic antibodies'
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Journal articles on the topic "Anti-idiotypic antibodies"
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Nagpal, S., K. N. Shanthi, R. Kori, H. Schroder, D. D. Metcalfe, and P. V. Subba Rao. "Induction of allergen-specific IgE and IgG responses by anti-idiotypic antibodies." Journal of Immunology 142, no. 10 (May 15, 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., and Gary E. Isom. "Anti-morphine anti-idiotypic antibodies." Biochemical Pharmacology 34, no. 16 (August 1985): 2853–58. http://dx.doi.org/10.1016/0006-2952(85)90006-1.
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Mermelstein, Norman, and Grant Morahan. "Assays to detect monoclonal anti-idiotypic anti-idiotypic antibodies." Journal of Immunological Methods 101, no. 1 (June 1987): 147. http://dx.doi.org/10.1016/0022-1759(87)90228-6.
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Lin, C., M. Musch, P. Meo, J. Zebrowitz, E. Chang, and T. R. Kleyman. "Anti-idiotypic antibodies to delineate epitope specificity of anti-amiloride antibodies." American Journal of Physiology-Cell Physiology 267, no. 3 (September 1, 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, and Albert G. Burger. "Synthesis and characterization of anti-idiotypic anti-T4 antibodies." European Journal of Endocrinology 130, no. 1 (January 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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Monroe, John G., and Mark I. Greene. "Anti-Idiotypic Antibodies and Disease." Immunological Investigations 15, no. 3 (January 1986): 263–86. http://dx.doi.org/10.3109/08820138609026688.
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Couraud, P. O. "Anti-angiotensin II anti-idiotypic antibodies bind to angiotensin II receptor." Journal of Immunology 138, no. 4 (February 15, 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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de Saint Basile, G., A. Durandy, G. Somme, and 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, no. 2 (January 15, 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, and 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, no. 6 (September 15, 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, and 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, no. 1 (February 24, 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.
Dissertations / Theses on the topic "Anti-idiotypic antibodies"
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Barden, Timothy John. "The synthesis of novel O-alkyl analogues of the energy-repartitioning [beta]-agonist clenbuterol and their physiological and immunological characterisations." Thesis, [Campbelltown, N.S.W. : The Author], 1995. http://handle.uws.edu.au:8081/1959.7/29572.
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It was proposed that some O-alkyl analogues of the beta-adrenergic agonist clenbuterol would be effective structural and functional congeners of clenbuterol which may then be used for the production of clenbuterol-specific idiotypic antibodies. These antibodies could possibly then be used to generate anti-idiotypic antibodies that mimic the energy-repartitioning effects of clenbuterol. Therefore, the aim of this work was to synthesise and characterise these compounds, evaluate their physiological effects, characterise the specificity of antibodies produced in response to protein conjugates of two of the novel compounds, and then use this data to determine the utility of these compounds for the generation of anti-idiotype antibodies which mimic clenbuterol. The target compounds were synthesised in five steps from 3,5-dichloro-4-hydroxyacetophenone in overall yields of 5-28%. A synthetic scheme similar to that which has led to clenbuterol was used to form the phenylethanolamine backbone, with modifications to include the O-alkyl moiety via a modified Williamson ether synthesis, and elimination of a synthetic chlorination step. Overall, 15 new compounds were synthesised, which were characterised and their structure confirmed from proton and carbon-13 NMR, IR and mass spectral data. The two haptenic analogues were then conjugated to carrier proteins using carbodiimide-based chemistries. In conclusion, the results indicated that the O-alkyl analogues, although structurally similar, were ineffective functional mimics of clenbuterol. Therefore, the anti-clenbuterol antobodies produced from the novel O-alkyl analogues would appear to be unsuitable for production of anti-idiotypic antibodies that mimic the energy-repartitioning effects of clenbuterol since the antibodies were unable to distinguish between the compound which demonstrated energy-repartitioning effects (clenbuterol) and those that did not (O-alkyl clenbuterol analogues).
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Barden, Timothy John. "The synthesis of novel O-alkyl analogues of the energy-repartitioning [beta]-agonist clenbuterol and their physiological and immunological characterisations /." [Campbelltown, N.S.W. : The Author], 1995. http://library.uws.edu.au/adt-NUWS/public/adt-NUWS20030723.132446/index.html.
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Erlandsson, Ann. "Interaction studies of idiotypic and antiidiotypic antibodies at experimental tumor targeting /." Umeå : Klinisk mikrobiologi, 2005. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-583.
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Shanti, K. N. "Identification of Tropomyosin as the Major Cross-Reacting Crustacean Allergen." Thesis, Indian Institute of Science, 1994. https://etd.iisc.ac.in/handle/2005/103.
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Seafood including crustaceans, on ingestion, are known to provoke gastrointestinal as well as systemic allergic reactions. Crustaceans are aquatic arthropods with a chitinous exoskeleton and include shrimp, lobster, prawn and crab. Earlier studies in our laboratory have led to the identification and characterization of three allergens from shrimp, designated as Sa-I, Sa-I1 and Sa-III. The former two were shown to be heat stable proteins with a mol. wt. of 8.4 and 34 kDa respectively, while Sa-III was identified as tRNA Arg and TRNATyr ). Sa-II was found to be the major allergen contributing to more than 50% of the allergenic activity.
There are several reports on the existence of cross-reactivity among atopic allergens, in particular food allergens. It is well known that individuals with shrimp allergy often complain of adverse reactions following the ingestion of other re1ated crustaceans. Recognition of crustacea as a group causing adverse reactions in sensitive individuals has a basis in the close phylogenetic relationship of shrimp, lobster, crab and prawn. Thus, one could expect appreciable similarity in the IgE binding epitopes of the offending allergens from related crustaceans. The present study was, therefore, aimed towards the identification of the major cross-reacting crustacean allergen and localization of its IgE binding epitopes. Cross-reactivity among a1lergens from shrimp, prawn, crab and lobster was evaluated by immunochemical methods. Antigenic cross-reactivity was established by immunodiffusion using shrimp-specific rabbit IgG. Competitive ELlSA inhibition experiments using sera of shrimp sensitive patients revealed a high degree of allergenic cross-reactivity between different crustaceans. SDSPAGE and immunoblot analysis using the sera of shrimp sensitive patients have identified a 34 kDa protein as the cross-reacting crustacean allergen. Using shrimp as a model system and Sa-II as a representative crustacean allergen, further studies were carried out to get an insight into the structural and molecular basis of allergenic cross-reactivity. The strategies adopted were, (1) to raise allergen specific anti-idiotypic antibodies and explore the possibility of using these anti-idiotypic antibodies as surrogate allergens for diagnosis of crustacea allergy and (2) to identify the IgE binding epitopes on the major shrimp allergen Sa-II, which may be shared by the 34 kDa allergen from the related crustaceans.
In order to explore idiotypic, anti-idiotypic and anti-anti-idiotypic responses to Sa-II, Balb/c mice were immunized with affinity purified human idiotypic antibodies directed against the purified allergen. This resulted in the production of anti-idiotypic antibodies which were quantitated using rabbit idiotypic antibodies raised against the same 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. The induction of anti-anti-idiotypic antibodies functionally identical to allergen-specific idiotypic antibodies confirmed that the anti-idiotypic antibodies generated, are indeed a mirror image of the allergen. The present study thus provides 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. These anti-anti-idiotypic antibodies not only recognized Sa-II, but also the 34 kDa allergen from prawn, lobster and crab.
Cross-reactivity studies using polyclonal sera of shrimp sensitive patients and Sa-II anti-anti-idiotypic antibodies have attributed the allergenic cross-reactivity observed among the related crustaceans to the presence of highly conserved IgE binding epitopes on the 34 kDa crossreacting allergen from shrimp, crab, lobster and prawn. In order to identify the igE binding epitopes on Sa-11, it was subjected to limited tryptic digestion and the peptides were separated by reverse phase HPLC. Amino acid sequence analysis of these peptides and several other peptides generated by Asp N and Lys C treatment revealed an 861 homology with the muscle protein tropomyosin from the fruit fly Drosophila melanogaster, suggesting that the major shrimp allergen is tropomyosin. To establish that Sa-II is indeed tropomyosin, the latter was isolated from shrimp and its physicochemical and immunochemical properties were compared with those of Sa-II. Both tropomyosin and Sa-II had the same molecular mass and focused in the isoelectric pH range of 4.8-5.4. In the presence of 6 M urea, the mobility of both Sa-I1 and shrimp tropomyosin shifted to give an apparent molecular mass of 50 kDa, which is a characteristic property of tropomyosins. Shrimp tropomyosin bound to specific IgE antibodies in the sera of shrimp sensitive patients as assessed by competitive ELISA inhibition and immunoblot analysis. Tropomyosin, similar to Sa-I1 was subjected to limited tryptic digestion and the tryptic maps of both Sa-II and tropomyosin as obtained by reverse phase HPLC were found to be super imposable. Dot blot immunoassay and competitive ELISA inhibition assay using the sera of shrimp sensitive patients identified two peptides, 6 and 9 that exhibited allergenic activity. Both the peptides were purified to homogeneity and sequenced. Peptide 6 is a nonapeptide corresponding to the amino adds 153-161 and peptide 9 has 17 amino acids corresponding to the aminoacid residues 50-66. The peptides individually blocked upto 50% the binding of allergen-specific IgE to hropomyosin. Sa-II specific mouse anti-anti-idiotypic antibodies recognized not only tropomyosin, but also the two allergenic peptides, thus confirming that these peptides represent the major IgE binding epitopes. The IgG binding activity was found to be associated with peptides 6 and 9 as assessed by dot blot immunoassay using the sera of shrimp sensitive patients. Thus, it was found that both IgG and IgE binding epitopes on shrimp tropomyosin are identical. Tropomyosins from both phylogenetically related and unrelated species were assessed for allergenic activity using the sera of shrimp sensitive patients. It was found that allergenic activity was associated with tropomyosins from related crustaceans and from Drosophila melanogaster which shares 86% homology with shrimp tropornyosin. However, tropomyosins from totally unrelated species like yeast, chicken, bovine, rat, rabbit and human did not exhibit allergenic activity. A comparison of the amino acid sequence of shrimp tropomyosin in the region of IgE binding epitopes with the corresponding regions of bopomyosins from different species confirmed lack of allergenic cross-reactivity. The allergenic peptides 6 and 9 were able to inhibit the binding of tropomyosins from related crustaceans to shrimp tropomyosin-specific IgE antibodies to the same extent, confirming the presence of highly conserved IgE binding epitopes. It has been established for the first time that the major crustacean allergen is the heat stable muscle protein, tropomyosin, and extensive cross-reactivity between different members of crustacea is due to the presence of highly conserved IgE binding epitopes on tropomyosins from these sources. Thus, from the present study, information with respect to the amino acid sequence of tropomyosin and localization of its 1gE binding epitopes, could be used to design synthetic peptides corresponding to the B cell and T cell epitopes which would find application in the diagnosis and desensitization of individuals allergic to crustacea.
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Shanti, K. N. "Identification of Tropomyosin as the Major Cross-Reacting Crustacean Allergen." Thesis, Indian Institute of Science, 1994. http://hdl.handle.net/2005/103.
Full textAbstract:
Seafood including crustaceans, on ingestion, are known to provoke gastrointestinal as well as systemic allergic reactions. Crustaceans are aquatic arthropods with a chitinous exoskeleton and include shrimp, lobster, prawn and crab. Earlier studies in our laboratory have led to the identification and characterization of three allergens from shrimp, designated as Sa-I, Sa-I1 and Sa-III. The former two were shown to be heat stable proteins with a mol. wt. of 8.4 and 34 kDa respectively, while Sa-III was identified as tRNA Arg and TRNATyr ). Sa-II was found to be the major allergen contributing to more than 50% of the allergenic activity.
There are several reports on the existence of cross-reactivity among atopic allergens, in particular food allergens. It is well known that individuals with shrimp allergy often complain of adverse reactions following the ingestion of other re1ated crustaceans. Recognition of crustacea as a group causing adverse reactions in sensitive individuals has a basis in the close phylogenetic relationship of shrimp, lobster, crab and prawn. Thus, one could expect appreciable similarity in the IgE binding epitopes of the offending allergens from related crustaceans. The present study was, therefore, aimed towards the identification of the major cross-reacting crustacean allergen and localization of its IgE binding epitopes. Cross-reactivity among a1lergens from shrimp, prawn, crab and lobster was evaluated by immunochemical methods. Antigenic cross-reactivity was established by immunodiffusion using shrimp-specific rabbit IgG. Competitive ELlSA inhibition experiments using sera of shrimp sensitive patients revealed a high degree of allergenic cross-reactivity between different crustaceans. SDSPAGE and immunoblot analysis using the sera of shrimp sensitive patients have identified a 34 kDa protein as the cross-reacting crustacean allergen. Using shrimp as a model system and Sa-II as a representative crustacean allergen, further studies were carried out to get an insight into the structural and molecular basis of allergenic cross-reactivity. The strategies adopted were, (1) to raise allergen specific anti-idiotypic antibodies and explore the possibility of using these anti-idiotypic antibodies as surrogate allergens for diagnosis of crustacea allergy and (2) to identify the IgE binding epitopes on the major shrimp allergen Sa-II, which may be shared by the 34 kDa allergen from the related crustaceans.
In order to explore idiotypic, anti-idiotypic and anti-anti-idiotypic responses to Sa-II, Balb/c mice were immunized with affinity purified human idiotypic antibodies directed against the purified allergen. This resulted in the production of anti-idiotypic antibodies which were quantitated using rabbit idiotypic antibodies raised against the same 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. The induction of anti-anti-idiotypic antibodies functionally identical to allergen-specific idiotypic antibodies confirmed that the anti-idiotypic antibodies generated, are indeed a mirror image of the allergen. The present study thus provides 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. These anti-anti-idiotypic antibodies not only recognized Sa-II, but also the 34 kDa allergen from prawn, lobster and crab.
Cross-reactivity studies using polyclonal sera of shrimp sensitive patients and Sa-II anti-anti-idiotypic antibodies have attributed the allergenic cross-reactivity observed among the related crustaceans to the presence of highly conserved IgE binding epitopes on the 34 kDa crossreacting allergen from shrimp, crab, lobster and prawn. In order to identify the igE binding epitopes on Sa-11, it was subjected to limited tryptic digestion and the peptides were separated by reverse phase HPLC. Amino acid sequence analysis of these peptides and several other peptides generated by Asp N and Lys C treatment revealed an 861 homology with the muscle protein tropomyosin from the fruit fly Drosophila melanogaster, suggesting that the major shrimp allergen is tropomyosin. To establish that Sa-II is indeed tropomyosin, the latter was isolated from shrimp and its physicochemical and immunochemical properties were compared with those of Sa-II. Both tropomyosin and Sa-II had the same molecular mass and focused in the isoelectric pH range of 4.8-5.4. In the presence of 6 M urea, the mobility of both Sa-I1 and shrimp tropomyosin shifted to give an apparent molecular mass of 50 kDa, which is a characteristic property of tropomyosins. Shrimp tropomyosin bound to specific IgE antibodies in the sera of shrimp sensitive patients as assessed by competitive ELISA inhibition and immunoblot analysis. Tropomyosin, similar to Sa-I1 was subjected to limited tryptic digestion and the tryptic maps of both Sa-II and tropomyosin as obtained by reverse phase HPLC were found to be super imposable. Dot blot immunoassay and competitive ELISA inhibition assay using the sera of shrimp sensitive patients identified two peptides, 6 and 9 that exhibited allergenic activity. Both the peptides were purified to homogeneity and sequenced. Peptide 6 is a nonapeptide corresponding to the amino adds 153-161 and peptide 9 has 17 amino acids corresponding to the aminoacid residues 50-66. The peptides individually blocked upto 50% the binding of allergen-specific IgE to hropomyosin. Sa-II specific mouse anti-anti-idiotypic antibodies recognized not only tropomyosin, but also the two allergenic peptides, thus confirming that these peptides represent the major IgE binding epitopes. The IgG binding activity was found to be associated with peptides 6 and 9 as assessed by dot blot immunoassay using the sera of shrimp sensitive patients. Thus, it was found that both IgG and IgE binding epitopes on shrimp tropomyosin are identical. Tropomyosins from both phylogenetically related and unrelated species were assessed for allergenic activity using the sera of shrimp sensitive patients. It was found that allergenic activity was associated with tropomyosins from related crustaceans and from Drosophila melanogaster which shares 86% homology with shrimp tropornyosin. However, tropomyosins from totally unrelated species like yeast, chicken, bovine, rat, rabbit and human did not exhibit allergenic activity. A comparison of the amino acid sequence of shrimp tropomyosin in the region of IgE binding epitopes with the corresponding regions of bopomyosins from different species confirmed lack of allergenic cross-reactivity. The allergenic peptides 6 and 9 were able to inhibit the binding of tropomyosins from related crustaceans to shrimp tropomyosin-specific IgE antibodies to the same extent, confirming the presence of highly conserved IgE binding epitopes. It has been established for the first time that the major crustacean allergen is the heat stable muscle protein, tropomyosin, and extensive cross-reactivity between different members of crustacea is due to the presence of highly conserved IgE binding epitopes on tropomyosins from these sources. Thus, from the present study, information with respect to the amino acid sequence of tropomyosin and localization of its 1gE binding epitopes, could be used to design synthetic peptides corresponding to the B cell and T cell epitopes which would find application in the diagnosis and desensitization of individuals allergic to crustacea.
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Jaradat, Ziad Waheed. "Production and characterization of anti-idiotypic antibodies for the control of Escherichia coli infections in mammals." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp02/NQ45002.pdf.
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Golisch, Thea Leandra [Verfasser], Christoph [Gutachter] Königs, and Erhard [Gutachter] Seifried. "Exploration of anti-idiotypic antibodies for elimination of fVIII inhibitors in Hemophilia A patients / Thea Leandra Golisch ; Gutachter: Christoph Königs, Erhard Seifried." Frankfurt am Main : Universitätsbibliothek Johann Christian Senckenberg, 2020. http://d-nb.info/1208033077/34.
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Rahal, Amal. "Anti-idiotypic induction therapy for the treatment of chronic inflammatory disorders. Therapeutic evaluation of two anti-SLE A monoclonal antibodies in an animal model for acute inflammation." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape9/PQDD_0017/MQ47086.pdf.
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Gangadhar, Vidya. "Role Of Idiotypic Anti-Idiotypic Network In The Sustenance Of Immunological Memory." Thesis, 2007. https://etd.iisc.ac.in/handle/2005/516.
Full textAbstract:
Living amidst a milieu of pathogenic organisms, vertebrates are in constant threat of contracting one or the other disease. As a mechanism of protection against such ‘invasions’, the vertebrate immune system has evolved to serve two main functions. One, to generate a specific immune response against the invading pathogen (in the from of specific antibodies and cell mediated immune responses). And two, to ‘remember’ the pathogen after the first exposure and mount a heightened and quicker immune response upon subsequent encounters. This phenomenon is called immunological memory, or anamnestic response and is achieved by the generation of memory B and T cells. The generation of specific Immunological memory is indeed the most important requirement/purpose of prophylactic vaccination
Though different mechanisms are known to operate to maintain memory B and T cells, some aspects are still debatable. The ‘relay hypothesis’ (Nayak etal., Immunology.102(4)(2001); Nayak R etal., Microbes. Infect.(2005)), addresses some of those key issues. It describes that antigen specific memory B cells can be maintained by the interaction of membrane bound idiotypic (Id, Ab1) and anti-idiotypic (α-Id, Ab2) antibodies on B cells. Anti-Ids binding to idiotopes on Abs (Ab1) are known to be potential regulators of immunity in a variety of diseases, such as autoimmunity, cancer as well as viral, bacterial or parasitic infections. The relay hypothesis outlines the mechanism of persistence of memory cells in the absence of persisting antigen. This is achieved through the ‘internal image’ of the antigen on the Ab2 variable region, which serves as surrogate antigen thus helping in maintenance of immunological memory even in the absence of persisting antigen. It also explains that all antigens, protein or nonprotein can be converted to the common “coinage” of internal image peptides, otherwise called peptido-mimics. Peptido-mimics that have similar binding properties to MHC as the antigenic epitope, will ensure that the antigen specific memory T cells are also maintained. Hence T cell activation could also occur in the absence of nominal antigen, a potentially important process in T-B cooperation and immune regulation.
Scope and objectives of this work:
To demonstrate the presence of idiotypic and cognate anti-idiotypic antibody for the given antigen
To examine the likelihood of the three dimensional structural similarity between antigen and Ab2 variable region
To demonstrate the presence of peptido-mimics of the antigenic epitope in the Ab2 variable region; and if those peptido-mimics have structural and functional
similarity with antigenic peptides when bound to MHC-I
To examine the (immunological) memory associated phenotype of thediotypic anti-idiotypic B cells.
The antigen of choice for the current study is Heamagglutinin-Neuraminidase (HN) protein of peste des petits ruminants virus (PPRV). Idiotypic (Id, Ab1), antiidiotypic (α-Id, Ab2) hybridoma against a deletion mutant of PPRV HN were generated and characterized. These hybridoma served as surrogate B cells for the study of Id α-Id B cell interactions. Anti-anti-idiotypic (Ab3) lymphocytes were also generated by immunizing syngenic BALB/c mice with Ab2 hybridoma. Results not only indicated the interplay of idiotypic and anti-idiotypic B and T cells in this cascade but also the mimicry of the antigen by Ab2. Ab2 Mab could recognize idiotopes of anti-PPRV HN Ab1 raised in diff species of animals, thus demonstrating that Ab2 was indeed an antigen mimic that interacts with Ab1 paratope irrespective of which species the Ab1 originates from. Ab2 Mab also mimicked the antigen (Hemagglutinin-neuraminidase) in functional assays by bringing about hemagglutination. Similarly, Polyclonal Ab3 which reacts with Ab2 Mab and with antigen, inhibits hemagglutination, just as Ab1 does, albeit to a lesser extent. This suggests Ab3 has functional similarity with Ab1.
It is imperative that T cells be involved in this network of B cells for the maintenance of antigen specific immunological memory. This is because B cells require T cell help in the form of cytokines for proliferation and Cytotoxic T Lymphocytes (CTLs) are needed to control the specific population of Id and anti-Id B cells to maintain homeostasis.
The Ab2 hybridoma as well as soluble Ab2 stimulated the proliferation of antigen specific T cells. Similarly, Ab3 splenocytes were stimulated to proliferate by the Ab2 as well as the antigen. Peptides generated from monoclonal Ab2 heavy and light chain variable regions (VH and VL) showed structural and functional similarity to the antigenic peptides in terms of p-MHC binding. These peptides stimulated the proliferation of antigen and Ab2 specific T cells, and also triggered 4-5 times higher CTL targeted cell lysis of peptide pulsed RMAS-Kd cells, as compared to a control peptide. VH, VL and antigenic peptides stabilized MHC-I on the cell surface of the TAP deficient, RMAS-Kd cell line for upto six hrs as compared to the ‘empty’ MHC-I, which remained on the surface only for one hr.
The presence of peptido-mimics in the Ab2 variable region, which have structural similarity with antigenic peptide (when bound to MHC I), was also established using insilico software tools. Antigenic peptides and VH and VL peptides were modeled onto MHC-I crystal structures using the molecular modeling software InsightII and the minimization program, CNS. Putative MHC-I binding peptides from these sequences were generated using the p-MHC-I binding prediction algorithm, BIMAS. By replacing these peptides in the respective crystal structure of MHC I and superimposing the two structures, we have tried to establish that through structural similarity in binding to MHC-I, peptidomimics have a role in the maintenance of antigen-specific CTL memory. Consequently CTL memory specific to antigenic epitope can be preserved even in the absence of antigen by its peptidomimic.
Following long-term immunizations, as expected of a secondary immune response, the serum Ab1 titre was found to be higher than the titer during primary response. It was also noted that though the number of Ab1 and Ab2 cell number was comparable in the total splenocyte population, Ab1 titre in the serum was higher than Ab2, immaterial of Ag/Ab2 booster. The same trend was noticed in prolifertion assay and CTL assays when the splenocytes were stimulated by Ag/Ab2 pulsed bone-marrow derived dendritic cells (BMDCs) as APCs. That is, irrespective of immunization and boost with Ag/Ab2, Ag pulsed BMDCs stimulated the proliferation and CTL lysis of long term immunized splenocytes to a greater extent than Ab2 pulsed BMDCs.
Memory markers present on B and T cell surface might help maintain their close interactions in the idiotypic network. CD27/CD70 (CD27L) might play a role in maintaining these cells in a memory state. The Id α-Id B cells in addition to being triggered through the membrane bound Id, α-Id antibodies, can also be activated through CD27/CD70 to differentiate into plasma cells upon activation by antigen. Id and α-Id B cells were demonstrated to possess the CD27 memory marker on their surface in addition to the membrane bound IgM. Antigen specific IgM and CD27 double positive cells were detected in the range of 1-3% in the total splenocyte population.
In conclusion: PPRV HN immunization triggered the generation of Ab1, Ab2, Ab3 (Id, α-Id, α-α-Id) cascade through the interaction of membrane bound immunoglobulin of the corresponding B cells. Ab2 was demonstrated to be a significant structural and functional mimic of the antigen. Peptidomimics of the antigenic epitope, present in the Ab2 variable region, can serve the purpose of maintaining antigen specific T cell memory response.
These findings re-confirm the importance of anti-id antibodies in the regulation of immune responses. Ever since the concept of antigen mimicry by anti-Id antibody has been confirmed by several laboratories, the utility of anti-Ids as surrogate antigens for the purpose of prophylactic vaccination has received great attention. The results of the current work are especially significant for the purpose of development of vaccines for diseases related to antigens that are very cumbersome to purify (for ex., in case of several cancers) or when it is too dangerous to immunize with the antigen itself (for ex., in case of some pathogenic organisms). The results also signify that immaterial of the nature of the antigen, their respective petidomimics can establish and maintain immunological memory.
10
Gangadhar, Vidya. "Role Of Idiotypic Anti-Idiotypic Network In The Sustenance Of Immunological Memory." Thesis, 2007. http://hdl.handle.net/2005/516.
Full textAbstract:
Living amidst a milieu of pathogenic organisms, vertebrates are in constant threat of contracting one or the other disease. As a mechanism of protection against such ‘invasions’, the vertebrate immune system has evolved to serve two main functions. One, to generate a specific immune response against the invading pathogen (in the from of specific antibodies and cell mediated immune responses). And two, to ‘remember’ the pathogen after the first exposure and mount a heightened and quicker immune response upon subsequent encounters. This phenomenon is called immunological memory, or anamnestic response and is achieved by the generation of memory B and T cells. The generation of specific Immunological memory is indeed the most important requirement/purpose of prophylactic vaccination
Though different mechanisms are known to operate to maintain memory B and T cells, some aspects are still debatable. The ‘relay hypothesis’ (Nayak etal., Immunology.102(4)(2001); Nayak R etal., Microbes. Infect.(2005)), addresses some of those key issues. It describes that antigen specific memory B cells can be maintained by the interaction of membrane bound idiotypic (Id, Ab1) and anti-idiotypic (α-Id, Ab2) antibodies on B cells. Anti-Ids binding to idiotopes on Abs (Ab1) are known to be potential regulators of immunity in a variety of diseases, such as autoimmunity, cancer as well as viral, bacterial or parasitic infections. The relay hypothesis outlines the mechanism of persistence of memory cells in the absence of persisting antigen. This is achieved through the ‘internal image’ of the antigen on the Ab2 variable region, which serves as surrogate antigen thus helping in maintenance of immunological memory even in the absence of persisting antigen. It also explains that all antigens, protein or nonprotein can be converted to the common “coinage” of internal image peptides, otherwise called peptido-mimics. Peptido-mimics that have similar binding properties to MHC as the antigenic epitope, will ensure that the antigen specific memory T cells are also maintained. Hence T cell activation could also occur in the absence of nominal antigen, a potentially important process in T-B cooperation and immune regulation.
Scope and objectives of this work:
To demonstrate the presence of idiotypic and cognate anti-idiotypic antibody for the given antigen
To examine the likelihood of the three dimensional structural similarity between antigen and Ab2 variable region
To demonstrate the presence of peptido-mimics of the antigenic epitope in the Ab2 variable region; and if those peptido-mimics have structural and functional
similarity with antigenic peptides when bound to MHC-I
To examine the (immunological) memory associated phenotype of thediotypic anti-idiotypic B cells.
The antigen of choice for the current study is Heamagglutinin-Neuraminidase (HN) protein of peste des petits ruminants virus (PPRV). Idiotypic (Id, Ab1), antiidiotypic (α-Id, Ab2) hybridoma against a deletion mutant of PPRV HN were generated and characterized. These hybridoma served as surrogate B cells for the study of Id α-Id B cell interactions. Anti-anti-idiotypic (Ab3) lymphocytes were also generated by immunizing syngenic BALB/c mice with Ab2 hybridoma. Results not only indicated the interplay of idiotypic and anti-idiotypic B and T cells in this cascade but also the mimicry of the antigen by Ab2. Ab2 Mab could recognize idiotopes of anti-PPRV HN Ab1 raised in diff species of animals, thus demonstrating that Ab2 was indeed an antigen mimic that interacts with Ab1 paratope irrespective of which species the Ab1 originates from. Ab2 Mab also mimicked the antigen (Hemagglutinin-neuraminidase) in functional assays by bringing about hemagglutination. Similarly, Polyclonal Ab3 which reacts with Ab2 Mab and with antigen, inhibits hemagglutination, just as Ab1 does, albeit to a lesser extent. This suggests Ab3 has functional similarity with Ab1.
It is imperative that T cells be involved in this network of B cells for the maintenance of antigen specific immunological memory. This is because B cells require T cell help in the form of cytokines for proliferation and Cytotoxic T Lymphocytes (CTLs) are needed to control the specific population of Id and anti-Id B cells to maintain homeostasis.
The Ab2 hybridoma as well as soluble Ab2 stimulated the proliferation of antigen specific T cells. Similarly, Ab3 splenocytes were stimulated to proliferate by the Ab2 as well as the antigen. Peptides generated from monoclonal Ab2 heavy and light chain variable regions (VH and VL) showed structural and functional similarity to the antigenic peptides in terms of p-MHC binding. These peptides stimulated the proliferation of antigen and Ab2 specific T cells, and also triggered 4-5 times higher CTL targeted cell lysis of peptide pulsed RMAS-Kd cells, as compared to a control peptide. VH, VL and antigenic peptides stabilized MHC-I on the cell surface of the TAP deficient, RMAS-Kd cell line for upto six hrs as compared to the ‘empty’ MHC-I, which remained on the surface only for one hr.
The presence of peptido-mimics in the Ab2 variable region, which have structural similarity with antigenic peptide (when bound to MHC I), was also established using insilico software tools. Antigenic peptides and VH and VL peptides were modeled onto MHC-I crystal structures using the molecular modeling software InsightII and the minimization program, CNS. Putative MHC-I binding peptides from these sequences were generated using the p-MHC-I binding prediction algorithm, BIMAS. By replacing these peptides in the respective crystal structure of MHC I and superimposing the two structures, we have tried to establish that through structural similarity in binding to MHC-I, peptidomimics have a role in the maintenance of antigen-specific CTL memory. Consequently CTL memory specific to antigenic epitope can be preserved even in the absence of antigen by its peptidomimic.
Following long-term immunizations, as expected of a secondary immune response, the serum Ab1 titre was found to be higher than the titer during primary response. It was also noted that though the number of Ab1 and Ab2 cell number was comparable in the total splenocyte population, Ab1 titre in the serum was higher than Ab2, immaterial of Ag/Ab2 booster. The same trend was noticed in prolifertion assay and CTL assays when the splenocytes were stimulated by Ag/Ab2 pulsed bone-marrow derived dendritic cells (BMDCs) as APCs. That is, irrespective of immunization and boost with Ag/Ab2, Ag pulsed BMDCs stimulated the proliferation and CTL lysis of long term immunized splenocytes to a greater extent than Ab2 pulsed BMDCs.
Memory markers present on B and T cell surface might help maintain their close interactions in the idiotypic network. CD27/CD70 (CD27L) might play a role in maintaining these cells in a memory state. The Id α-Id B cells in addition to being triggered through the membrane bound Id, α-Id antibodies, can also be activated through CD27/CD70 to differentiate into plasma cells upon activation by antigen. Id and α-Id B cells were demonstrated to possess the CD27 memory marker on their surface in addition to the membrane bound IgM. Antigen specific IgM and CD27 double positive cells were detected in the range of 1-3% in the total splenocyte population.
In conclusion: PPRV HN immunization triggered the generation of Ab1, Ab2, Ab3 (Id, α-Id, α-α-Id) cascade through the interaction of membrane bound immunoglobulin of the corresponding B cells. Ab2 was demonstrated to be a significant structural and functional mimic of the antigen. Peptidomimics of the antigenic epitope, present in the Ab2 variable region, can serve the purpose of maintaining antigen specific T cell memory response.
These findings re-confirm the importance of anti-id antibodies in the regulation of immune responses. Ever since the concept of antigen mimicry by anti-Id antibody has been confirmed by several laboratories, the utility of anti-Ids as surrogate antigens for the purpose of prophylactic vaccination has received great attention. The results of the current work are especially significant for the purpose of development of vaccines for diseases related to antigens that are very cumbersome to purify (for ex., in case of several cancers) or when it is too dangerous to immunize with the antigen itself (for ex., in case of some pathogenic organisms). The results also signify that immaterial of the nature of the antigen, their respective petidomimics can establish and maintain immunological memory.
Books on the topic "Anti-idiotypic antibodies"
1
Pierre-André, Cazenave, ed. Anti-idiotypic vaccines. New York: Springer-Verlag, 1991.
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2
1939-, Cerny Jan, and Hiernaux Jacques R. J, eds. Idiotypic network and diseases. Washington, D.C: American Society for Microbiology, 1990.
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3
A, Bona Constantin, ed. Biological applications of anti-idiotypes. Boca Raton, Fla: CRC Press, 1988.
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4
Scott, Linthicum D., Farid Nadir R, and International Congress of Immunology (6th : 1986 : Toronto, Ont.), eds. Anti-idiotypes, receptors, and molecular mimicry. New York: Springer-Verlag, 1988.
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5
Praputpittaya, Kriangsak. Anti-idiotypic antibodies and their role in the immune response to M. leprae and M. tuberculosis. Birmingham: University of Birmingham, 1986.
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6
Mayforth, Ruth D. Designing antibodies. San Diego: Academic Press, Inc., 1993.
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7
Albert, Osterhaus, and UytdeHaag Fons, eds. Idiotype networks in biology and medicine: Proceedings of the Congress on Idiotype Networks in Medicine and Biology, 17-20 April 1989, held in Gennep, the Netherlands. Amsterdam: Excerpta Medica, 1990.
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8
Congress on Idiotype Networks in Biology and Medicine (1989 Gennep, Netherlands). Idiotype networks in biology and medicine: Proceedings of the Congress on Idiotype Networks in Biology and Medicine, 17-20 April 1989, held in Gennep, the Netherlands. Edited by Osterhaus Albert, UytdeHaag Fons, and Commission of the European Communities. Directorate-General for Science, Research, and Development. Amsterdam: Excerpta Medica, 1990.
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9
Yehuda, Shoenfeld, Kennedy Ronald C, and Ferrone Soldano 1940-, eds. Idiotypes in medicine: Autoimmunity, infection, and cancer. Amsterdam: Elsevier, 1997.
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10
Kennedy, Ronald C. Anti-Idiotypic Antibodies As Vaccines. Crc Pr I Llc, 1993.
Find full textBook chapters on the topic "Anti-idiotypic antibodies"
1
López-Requena, Alejandro, Oscar R. Burrone, and Rolando Pérez. "Anti-Idiotypic Antibodies." In Handbook of Therapeutic Antibodies, 407–34. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2014. http://dx.doi.org/10.1002/9783527682423.ch16.
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2
Avalle, B., A. Friboulet, and D. Thomas. "Catalysis by Anti-Idiotypic Antibodies." In Catalytic Antibodies, 80–88. Basel: KARGER, 2000. http://dx.doi.org/10.1159/000058798.
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3
Nicholson, Steve. "Measurement of HAMA and Anti-Idiotypic Antibodies." In Diagnostic and Therapeutic Antibodies, 381–90. Totowa, NJ: Humana Press, 2000. http://dx.doi.org/10.1385/1-59259-076-4:381.
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4
Gurish, Michael F., Tamar Ben-Porat, and Alfred Nisonoff. "Induction of Antibodies to Pseudorabies Virus by Immunization with Anti-Idiotypic Antibodies." In Antibodies, 81–89. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1873-6_8.
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Erlanger, B. F., W. L. Cleveland, N. H. Wasserman, H. H. Ku, B. L. Hill, R. Sarangarajan, R. Rajagopalan, et al. "Antibodies to Acetylcholine, Adenosine and Glucocorticoid Receptors by an Auto-Anti-Idiotypic Route." In Antibodies, 119–34. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1873-6_11.
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6
Chatterjee, M., K. A. Foon, and H. Kohler. "Anti-idiotypic Monoclonal Antibodies: Novel Approach to Immunotherapy." In The Pharmacology of Monoclonal Antibodies, 387–401. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78432-3_16.
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7
Couraud, Jean-Yves. "Anti-idiotypic Antibodies and Substance P Receptors." In Anti-Idiotypes, Receptors, and Molecular Mimicry, 45–59. New York, NY: Springer New York, 1988. http://dx.doi.org/10.1007/978-1-4612-3734-1_6.
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8
Warren, Ronald Q., and Ronald C. Kennedy. "Anti-Idiotypic Antibodies as Potential Viral Vaccines." In Progress in Vaccinology, 73–91. New York, NY: Springer New York, 1991. http://dx.doi.org/10.1007/978-1-4612-2992-6_7.
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Haasemann, M., J. Buschko, A. Faussner, A. A. Roscher, J. Hoebeke, R. Burch, and W. Müller-Esterl. "Anti-Idiotypic Antibodies Against the Kinin Receptor." In Recent Progress on Kinins, 497–512. Basel: Birkhäuser Basel, 1992. http://dx.doi.org/10.1007/978-3-0348-7321-5_62.
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Mariani, S. M., E. A. Armandola, and S. Ferrone. "Anti-idiotypic Antibodies in the HLA System." In The HLA System in Clinical Transplantation, 317–24. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-77506-2_24.
Full textConference papers on the topic "Anti-idiotypic antibodies"
1
Nugent, Diane. "IDENTIFICATION OF ANTIPLATELET ANTIBODY IDIOTYPlSS ASSOCIATED WITH GLYCOPROTEIN Ib SPECIFICITY, PRESENT IN ITP PLASMA AND PRODUCED BY HUMAN HYBRIDOMAS FROM ITP SPLEEN CELL FUSIONS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644758.
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Platelet membrane glycoproteins (GP) express anumber of antigenic determinants important in theetiology of autoimmune thrombocytopenia. Sensitization to GPIb, although not the most frequent cause of ITP, leads to a particularly severe form ofthe disease. We have identified a number of casesof ITP in which GPIb bears the relevant immunogen. Using GPIb-specific autoantibodies isolated from the plasma of one such patient, we have produced a number of rabbit polyclonal and murine monoclonal anti-idiotypic antibodies. These antibodies recognize an idiotype expressed on the IgM antibody of this patient as well as IgG or IgM antibodies from several other patients with ITP, all of which can be shown to bind specifically to GPIb. Statistical analysis of a series of plasmas from normal individuals and thrombocytopenic patients demonstrated that there is a very strong correlation between the presence of the idiotype and GPIb reactivity, (p < 0.00001). These anti-idiotypic antibodies are useful for the detection and characterization of GPIb-specific antibodies in the sera of patients with a clinically severe form of ITP. The classification of patients bearing this idiotype in their plasma may be useful in predicting disease outcome, thus identifying a group of ITP patients in whom more aggressive therapeutic regimens may be indicated. The use of these reagents and the development of human B lymphoblastoid cell lines producing monoclonal anti-GPIb antibodies will serve to elucidate the clonal origin and cellular regulation of autoantibody production in this disease
2
Heeb, S. R., M. Schaller, and J. A. Kremer. "Anti-ADAMTS13 Autoantibody-specific Anti-idiotypic Antibodies Restore ADAMTS13 Activity in Immune-mediated Thrombotic Thrombocytopenic Purpura (iTTP) Patients." In 63rd Annual Meeting of the Society of Thrombosis and Haemostasis Research. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-1680104.
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Heeb, S. R., M. Schaller, and J. A. Kremer. "Anti-ADAMTS13 Autoantibody-specific Anti-idiotypic Antibodies Restore ADAMTS13 Activity in Immune-mediated Thrombotic Thrombocytopenic Purpura (iTTP) Patients." In 63rd Annual Meeting of the Society of Thrombosis and Haemostasis Research. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-1680203.
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Yarygina, E. I., M. C. Kalmikova, R. F. Ivannikova, and N. V. Pimenov. "Biological technologies of polyclonal anti-idiotypic antibodies that mimic the «internal image» of Turkey herpes virus antigens." In PROCEEDINGS OF THE II INTERNATIONAL CONFERENCE ON ADVANCES IN MATERIALS, SYSTEMS AND TECHNOLOGIES: (CAMSTech-II 2021). AIP Publishing, 2022. http://dx.doi.org/10.1063/5.0092608.
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