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Artykuły w czasopismach na temat „EPITOPING”

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Data publikacji: 11 września 2023

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1

Kotani, Tomio, Masako Maeda, Kazumi Umeki i Sachiya Ohtaki. "Epitopic difference among rat thyroglobulins". Immunology Letters 9, nr 2-3 (styczeń 1985): 167–72. http://dx.doi.org/10.1016/0165-2478(85)90029-x.

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2

Leclerc, C., M. P. Schutze, E. Deriaud i G. Przewlocki. "The in vivo elimination of CD4+ T cells prevents the induction but not the expression of carrier-induced epitopic suppression." Journal of Immunology 145, nr 5 (1.09.1990): 1343–49. http://dx.doi.org/10.4049/jimmunol.145.5.1343.

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Abstract Injection of mice with an immunogenic dose of carrier (keyhole limpet hemocyanin (KLH)) followed by immunization with hapten-carrier conjugate (TNP-KLH) selectively suppresses anti-hapten antibody response. In this study, the cellular basis of this epitopic suppression and also of the suppression induced by a high dose of carrier were analyzed by in vivo depletion of CD4+ or CD8+ T cell subsets by using mAb. The mAb treatments were performed either at the time of carrier priming or at the time of hapten-carrier immunization. The elimination of CD8+ T cells has not modified the anti-carrier antibody response, whether this treatment was performed at the time of KLH-priming or during TNP-KLH immunization. Moreover, the in vivo treatment with the anti-CD8 mAb did not modify the carrier-induced epitopic suppression induced either by a low immunogenic dose of KLH or by a high dose of this Ag. The elimination of CD4+ T cells at the time of KLH immunization has prevented the induction of a memory response to KLH, clearly establishing that CD4+ T cells are essential in memory B cell development to T-dependent Ag. Moreover, this treatment has totally abrogated the epitopic suppression induced either by low or high dosages of KLH. In contrast, the in vivo elimination of CD4+ T cells after carrier immunization did not abolish the secondary anti-carrier antibody response and did not prevent the expression of epitopic suppression. These data indicate that primed CD4+ T cells are required neither for memory B cell expression nor for the expression of suppression. Finally, once induced, the suppression can be evidenced after in vivo depletion of both primed CD4+ and CD8+ T cells. These data support the view that epitopic suppression is induced through the expansion of carrier-specific B cells and resulted from intramolecular antigenic competition between hapten and carrier epitopes.

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3

Schutze, M. P., E. Deriaud, G. Przewlocki i C. LeClerc. "Carrier-induced epitopic suppression is initiated through clonal dominance." Journal of Immunology 142, nr 8 (15.04.1989): 2635–40. http://dx.doi.org/10.4049/jimmunol.142.8.2635.

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Abstract Injection of mice with an immunogenic dose of carrier followed by immunization with hapten-carrier conjugate selectively suppresses anti-hapten antibody response. Previous studies have proposed that this epitopic suppression is related to the induction of carrier-specific Ts cells which in turn could inhibit selectively anti-hapten response. In the present study, we propose that the epitopic suppression is in fact due to clonal dominance. Immunization with a carrier such as tetanus toxoid induces a clonal expansion of carrier-specific B cells, thus decreasing the probability of hapten-specific B cells to react with the Ag. Increasing the density of the TNP-hapten on the conjugate has totally prevented the induction of the epitopic suppression. Moreover, using low hapten-carrier concentrations to challenge carrier-primed mice has enhanced the induction of the suppression. Finally, priming hapten-specific B cells before carrier/hapten-carrier immunization has also abrogated the suppression. The results of these experiments support the view that epitopic suppression is induced through the expansion of the clones specific for the carrier epitopes and resulted from intra-molecular antigenic competition between hapten and carrier epitopes. Based on these findings a regulatory role is proposed for B cells, where through their capacity to process and present antigen, they would exercise a strong influence on the selection of immune responses.

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4

Mendz, G. L., W. J. Moore, S. Easterbrook-Smith i D. S. Linthicum. "Proton-n.m.r. study of interaction of myelin basic protein with a monoclonal antibody". Biochemical Journal 228, nr 1 (15.05.1985): 61–68. http://dx.doi.org/10.1042/bj2280061.

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Proton n.m.r. at 400 MHz has been applied to study the interactions of bovine or porcine myelin basic protein (b- or p-MBP) with a monoclonal antibody to human (h-) MBP. The antibody, an IgG immunoglobulin that contains a sequential epitopic region, cross-reacts with b-MBP but not with p-MBP, the presumed epitope being identical in h- and b-MBP. N.m.r. spectra were recorded from the Fab fragment of the antibody and for mixtures of Fab and MBP at various molar ratios. The n.m.r. spectrum of MBP in the mixture consists mostly of well resolved peaks against a broad background due to the Fab. With b-MBP, but not p-MBP, specific interactions are observed at the residue tyrosine-135, which is part of the epitopic sequence. Other interactions occur between the Fab and both b- and p-MBP at residues distant from the epitopic region. Standard radioassay techniques were employed to calculate the binding constants of both basic proteins with the immunoglobulin. The binding constant, Kb, for IgG to column-immobilized b-MBP at 298K is (0.95 +/- 0.07) X 10(7) dm3/mol. The value of Kb decreases with the ionic strength of the medium, suggesting a coulombic interaction between antigen and antibody. N.m.r. spectra were also measured for mixtures of the Fab fragment and peptides containing the epitopic site, with results in agreement with those for the whole protein.

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5

Barre, Annick, Hélène Sénéchal, Christophe Nguyen, Claude Granier, Pascal Poncet i Pierre Rougé. "Structural Basis for the IgE-Binding Cross-Reacting Epitopic Peptides of Cup s 3, a PR-5 Thaumatin-like Protein Allergen from Common Cypress (Cupressus sempervirens) Pollen". Allergies 3, nr 1 (10.01.2023): 11–24. http://dx.doi.org/10.3390/allergies3010002.

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The present work was aimed at identifying the IgE-binding epitopic regions on the surface of the Cup s 3 allergen from the common cypress Cupressus sempervirens, that are possibly involved in the IgE-binding cross-reactivity reported between Cupressaceae species. Three main IgE-binding epitopic regions were mapped on the molecular surface of Cup s 3, the PR-5 thaumatin-like allergen of common cypress Cupressus sempervirens. They correspond to exposed areas containing either electropositive (R, K) or electronegative (D, E) residues. A coalescence occurs between epitopes #1 and #2, that creates an extended IgE-binding regions on the surface of the allergen. Epitope #3 contains a putative N-glycosylation site which is actually glycosylated and could therefore comprise a glycotope. However, most of the allergenic potency of Cup s 3 depends on non-glycosylated epitopic peptides. The corresponding regions of thaumatin-like allergens from other closely related Cupressaceae (Cryptomeria, Juniperus, Thuja) exhibit a very similar conformation that should account for the IgE-binding cross-reactivity observed among the Cupressaceae allergens.

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6

Barre, Annick, Christophe Nguyen, Claude Granier, Hervé Benoist i Pierre Rougé. "IgE-Binding Epitopes of Pis v 1, Pis v 2 and Pis v 3, the Pistachio (Pistacia vera) Seed Allergens". Allergies 1, nr 1 (23.03.2021): 63–91. http://dx.doi.org/10.3390/allergies1010006.

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Sequential IgE-binding epitopes were identified on the molecular surface of the Pis v 1 (2S albumin), Pis v 2 (11S globulin/legumin) and Pis v 3 (7S globulin/vicilin)—major allergens from pistachio (Pistacia vera) seeds—using the Spot technique. They essentially consist of hydrophilic and electropositively charged residues well exposed on the surface of the allergens. Most of the epitopic regions identified on Pis v 1 and Pis v 3 do not coincide with the putative N-glycosylation sites and thus are not considered as glycotopes. Surface analysis of these epitopic regions indicates a high degree of conformational similarity with the previously identified epitopic regions of the corresponding allergens Ana o 1 (vicilin), Ana o 2 (legumin) and Ana o 3 (2S albumin) from the cashew (Anacardium occidentale) nut. These results offer a molecular basis for the IgE-binding cross-reactivity often observed between pistachio and cashew nut. They support the recommendation for prescribing pistachio avoidance in cashew allergic patients. Other conformational similarities were identified with the corresponding allergens Ses i 1 (2S albumin), Ses i 3 (vicilin) and Ses i 6 (legumin) from sesame (Sesamum indicum), and Jug r 1 (2S albumin), Jug r 2 (vicilin) and Jug r 4 (legumin) from walnut (Juglans regia). Conversely, conformation of most of the epitopic regions of the pistachio allergens often differs from that of epitopes occurring on the molecular surface of the corresponding Ara h 1 (vicilin), Ara h 2 (2S albumin) and Ara h 3 (legumin) allergens from peanut (Arachis hypogaea).

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7

Mañes, S., L. Kremer, B. Vangbo, A. López, C. Gómez-Mouton, E. Peiró, J. P. Albar, I. B. Mendel-Hartvig, R. Llopis i C. Martínez-A. "Physical mapping of human insulin-like growth factor-I using specific monoclonal antibodies". Journal of Endocrinology 154, nr 2 (sierpień 1997): 293–302. http://dx.doi.org/10.1677/joe.0.1540293.

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Abstract The primary structure of recombinant human (h) insulin-like growth factor-I (IGF-I) epitopes recognized by a panel of 28 monoclonal antibodies (mAbs) is characterized. Pairwise mAb epitope mapping defines eight 'epitopic clusters' (I–VIII) which cover nearly the entire solvent-exposed IGF-I surface. Monoclonal antibody reactivity with 32 overlapping synthetic peptides and with IGF-I mutants is used to associate these epitopic clusters with the probable primary IGF-I sequences recognized. Epitopic cluster I involves residues in the C-domain and the first α-helix of the A-domain; clusters II, V and VII involve principally the B-domain; clusters III and IV map to amino acid sequences (55–70) and (1–13) respectively; cluster VI includes the A- and B-domains; and cluster VIII involves mainly the C-terminal part of the B-domain. Data indicate that this mAb panel defines 14 distinct IGF-I epitopes. The specific inhibition of HEL 92.1.7 IGF-I-promoted proliferation by these mAbs was explored. Direct correlation between mAb affinity and inhibitory activity was observed except in the case of clusters III- and VII-specific mAbs. Finally, the combination of epitopic cluster I and II mAbs detect 0·5–10 ng/ml hIGF-I in a sandwich immunoassay, with no IGF-II crossreactivity. These anti-IGF-I mAbs are, therefore, useful for both the inhibition of IGF-I mitogenic activity and for the quantification of this growth factor. The potential use of this mAb panel in tumor cell growth control is discussed. Journal of Endocrinology (1997) 154, 293–302

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8

Nakada, H., M. Inoue, A. Mellors i I. Yamashina. "S12.15 Epitopic structure of tn antigen". Glycoconjugate Journal 10, nr 4 (sierpień 1993): 299–300. http://dx.doi.org/10.1007/bf01210049.

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9

Piechaczyk, M., M. Bouanani, S. L. Salhi, J. M. Bastide, M. Bastide i B. Pau. "Epitopic specificities of anti-thyroglobulin autoantibodies". International Journal of Radiation Applications and Instrumentation. Part B. Nuclear Medicine and Biology 17, nr 7 (styczeń 1990): 719–22. http://dx.doi.org/10.1016/0883-2897(90)90095-i.

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10

Casina, Veronica C., Wenbing Hu, Jian-Hua Mao, Rui-Nan Lu, Hayley A. Hanby, Brandy Pickens, Zhong-Yuan Kan i in. "High-resolution epitope mapping by HX MS reveals the pathogenic mechanism and a possible therapy for autoimmune TTP syndrome". Proceedings of the National Academy of Sciences 112, nr 31 (22.07.2015): 9620–25. http://dx.doi.org/10.1073/pnas.1512561112.

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Acquired thrombotic thrombocytopenic purpura (TTP), a thrombotic disorder that is fatal in almost all cases if not treated promptly, is primarily caused by IgG-type autoantibodies that inhibit the ability of the ADAMTS13 (a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 13) metalloprotease to cleave von Willebrand factor (VWF). Because the mechanism of autoantibody-mediated inhibition of ADAMTS13 activity is not known, the only effective therapy so far is repeated whole-body plasma exchange. We used hydrogen–deuterium exchange mass spectrometry (HX MS) to determine the ADAMTS13 binding epitope for three representative human monoclonal autoantibodies, isolated from TTP patients by phage display as tethered single-chain fragments of the variable regions (scFvs). All three scFvs bind the same conformationally discontinuous epitopic region on five small solvent-exposed loops in the spacer domain of ADAMTS13. The same epitopic region is also bound by most polyclonal IgG autoantibodies in 23 TTP patients that we tested. The ability of ADAMTS13 to proteolyze VWF is impaired by the binding of autoantibodies at the epitopic loops in the spacer domain, by the deletion of individual epitopic loops, and by some local mutations. Structural considerations and HX MS results rule out any disruptive structure change effect in the distant ADAMTS13 metalloprotease domain. Instead, it appears that the same ADAMTS13 loop segments that bind the autoantibodies are also responsible for correct binding to the VWF substrate. If so, the autoantibodies must prevent VWF proteolysis simply by physically blocking normal ADAMTS13 to VWF interaction. These results point to the mechanism for autoantibody action and an avenue for therapeutic intervention.

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11

Yuexi, Li, Wang Xingsheng, Xie Guangyan, Liao Jianming, Yin Dengke, Guan Wenyan, Pan Mingjie i Li Jingnian. "Immunisation analysis and animal protection experiments of a recombinant multi-epitope assembly peptide from Herpes Simplex Virus Type 2 (155.35)". Journal of Immunology 186, nr 1_Supplement (1.04.2011): 155.35. http://dx.doi.org/10.4049/jimmunol.186.supp.155.35.

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Abstract Human herpes simplex virus 2 (HSV2) has been the main cause for genital herpes, causes a significant health problem worldwide, and no effective vaccine is available. Multi-epitope assembly peptides vaccination is a promising mean to achieve protective immunity and to avoid immunopathology. A recombinant Multi-Epitope Assembly Peptide (MEAP) including 12 antigen epitopies from HSV2 was expressed and purified by genetic engineering, its immunity and protection efficacy against HSV2 infection were identified in mice. The twelve epitopies contained six B cell epitopies from six envelope glycoproteins, B, C, D, E, G and I of HSV2 respectively, four CD4+ T cell epitopes from B and D, and two CD8+ T cell epitopes from D. they are responsible for the elicitation of the neutralizing antibodies and CTLs that impart protective immunity to the host. all above epitopes were inserted into the extracellular fragment of HSV-2 glycoprotein D to construct multi-epitope assembly peptides by replacing some non-epitope amino acid sequences. The MEAP could elicit high titer neutralizing antibodies and cell-mediated immune responses in mice and rabbits. The mice immunized with the MEAP were completely protected against HSV-2 infection death at a lethal dose, and the virus shedding, inflammation severity in the mice were reduced significantly compared with the control mice, which indicates that it might be a potential candidate vaccine.

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12

Clement, Gilles, Didier Boquet, Yveline Frobert, Hervé Bernard, Luc Negroni, Jean-Marc Chatel, Karine Adel-Patient, Christophe Creminon, Jean-Michel Wal i Jacques Grassi. "Epitopic characterization of native bovine β-lactoglobulin". Journal of Immunological Methods 266, nr 1-2 (sierpień 2002): 67–78. http://dx.doi.org/10.1016/s0022-1759(02)00149-7.

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13

Pan, I. C., T. C. Whyard, W. R. Hess, N. Yuasa i M. Shimizu. "Epitopic diversity of African swine fever virus". Virus Research 9, nr 2-3 (luty 1988): 93–106. http://dx.doi.org/10.1016/0168-1702(88)90025-1.

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14

Stufano, Angela, i Darja Kanduc. "Proteome-based epitopic peptide scanning along PSA". Experimental and Molecular Pathology 86, nr 1 (luty 2009): 36–40. http://dx.doi.org/10.1016/j.yexmp.2008.11.009.

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15

Ананьева, Л. П. "Molecular (epitopic) mimicry phenomenon in Lime arthritis". Rheumatology Science and Practice, nr 3 (15.06.2004): 66. http://dx.doi.org/10.14412/1995-4484-2004-1484.

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16

Madhumathi, J., P. R. Prince, D. N. Rao, A. A. Karande, M. V. R. Reddy i P. Kaliraj. "Epitope mapping ofBrugia malayiALT-2 and the development of a multi-epitope vaccine for lymphatic filariasis". Journal of Helminthology 91, nr 1 (19.02.2016): 43–54. http://dx.doi.org/10.1017/s0022149x16000055.

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AbstractHuman lymphatic filariasis is a neglected tropical disease, causing permanent and long-term disability with severe immunopathology. Abundant larval transcript (ALT) plays a crucial role in parasite establishment in the host, due to its multi-faceted ability in host immune regulation. Although ALT protein is a key filarial target, its exact function is yet to be explored. Here, we report epitope mapping and a structural model ofBrugia malayiALT-2, leading to development of a multi-epitope vaccine. Structural analysis revealed that ALT represents unique parasitic defence proteins belonging to a toxin family that carries a ‘knottin’ fold. ALT-2 has been a favourite vaccine antigen and was protective in filarial models. Due to the immunological significance of ALT-2, we mapped B-cell epitopes systematically and identified two epitope clusters, 1–30 and 89–128. To explore the prophylactic potential of epitope clusters, a recombinant multi-epitopic gene comprising the epitopic domains was engineered and the protective efficacy of recombinant ALT epitope protein (AEP) was tested in the permissive model,Mastomys coucha. AEP elicited potent antibody responses with predominant IgG1 isotype and conferred significantly high protection (74.59%) compared to ALT-2 (61.95%). This proved that these epitopic domains are responsible for the protective efficacy of ALT-2 and engineering protective epitopes as a multi-epitope protein may be a novel vaccine strategy for complex parasitic infections.

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17

Barre, Annick, Hélène Sénéchal, Christophe Nguyen, Claude Granier, Pierre Rougé i Pascal Poncet. "Identification of Potential IgE-Binding Epitopes Contributing to the Cross-Reactivity of the Major Cupressaceae Pectate-Lyase Pollen Allergens (Group 1)". Allergies 2, nr 3 (5.09.2022): 106–18. http://dx.doi.org/10.3390/allergies2030010.

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Pectate-lyase allergens, the group 1 of allergens from Cupressaceae pollen, consist of glycoproteins exhibiting an extremely well-conserved three-dimensional structure and sequential IgE-binding epitopes. Up to 10 IgE-binding epitopic regions were identified on the molecular surface, which essentially cluster at both extremities of the long, curved β-prism-shaped allergens. Most of these IgE-binding epitopes possess very similar conformations that provide insight into the IgE-binding cross-reactivity and cross-allergenicity commonly observed among Cupressaceae pollen allergens. Some of these epitopic regions coincide with putative N-glycosylation sites that most probably consist of glycotopes or cross-reactive carbohydrate determinants, recognized by the corresponding IgE antibodies from allergic patients. Pectate-lyase allergens of Cupressaceae pollen offer a nice example of structurally conserved allergens that are widely distributed in closely-related plants (Chamæcyparis, Cryptomeria, Cupressus, Hesperocyparis, Juniperus, Thuja) and responsible for frequent cross-allergenicity.

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18

Guo, Mcintosh, Czarnocka, Weetman, Rapoport i Mclachlan. "Relationship between autoantibody epitopic recognition and immunoglobulin gene usage". Clinical & Experimental Immunology 111, nr 2 (luty 1998): 408–14. http://dx.doi.org/10.1046/j.1365-2249.1998.00492.x.

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19

MILLER, YORK E., NELDA SULLIVAN i BETTY KAO. "Monoclonal Antibodies to Human Transferrin: Epitopic and Phylogenetic Analysis". Hybridoma 7, nr 1 (luty 1988): 87–95. http://dx.doi.org/10.1089/hyb.1988.7.87.

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20

Hoshino, Tomonori, Yoshio Kondo, Kan Saito, Yutaka Terao, Nobuo Okahashi, Shigetada Kawabata i Taku Fujiwara. "Novel Epitopic Region of Glucosyltransferase B from Streptococcus mutans". Clinical and Vaccine Immunology 18, nr 9 (27.07.2011): 1552–61. http://dx.doi.org/10.1128/cvi.05041-11.

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ABSTRACTIn the development of a component vaccine against caries, the catalytic region (CAT) and glucan-binding domain (GBD) of glucosyltransferase B (GtfB) fromStreptococcus mutanshave been employed as target antigens. These regions were adopted as primary targets because they theoretically include epitopes associated with enzyme function. However, their antigenicities have not been fully evaluated. Although there are many reports about successful vaccination using these components, the principle has not yet been put to practical use. For these reasons, we came to doubt the effectiveness of the epitopes in vaccine production and reevaluated the antigenic region of GtfB by usingin silicoanalyses combined within vitroandin vivoexperiments. The results suggested that the ca. 360-amino-acid variable region (VR) in the N terminus of GtfB is more reactive than CAT and GBD. This region isS. mutansand/or GtfB specific, nonconserved among other streptococcal Gtfs, and of unknown function. Immunization using an adenovirus vector-borne DNA vaccine confirmed that VR is an epitope that shows promise for the development of a caries vaccine.

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21

Rubinstein, Nimrod D., Itay Mayrose, Eric Martz i Tal Pupko. "Epitopia: a web-server for predicting B-cell epitopes". BMC Bioinformatics 10, nr 1 (2009): 287. http://dx.doi.org/10.1186/1471-2105-10-287.

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22

SHIMAZAKI, Kei-ichi, Myoung Soo NAM, Shinji HARAKAWA, Tetsuya TANAKA, Yoshitaka OMATA, Atsushi SAITO, Haruto KUMURA, Katsuhiko MIKAWA, Ikuo IGARASHI i Naoyoshi SUZUKI. "Monoclonal Antibody against Bovine Lactoferricin and Its Epitopic Site." Journal of Veterinary Medical Science 58, nr 12 (1996): 1227–29. http://dx.doi.org/10.1292/jvms.58.12_1227.

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23

Yone, Kenji, Sandrine Bajard, Noriyuki Tsunekawa i Jun Suzuki. "Epitopic Regions for Antibodies against Tumor Necrosis Factor α". Journal of Biological Chemistry 270, nr 33 (18.08.1995): 19509–15. http://dx.doi.org/10.1074/jbc.270.33.19509.

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Mason, Anne B., Chantal J. Kenney, Michael K. Miller, Robert C. Woodworth, Kokila J. Patel i Robert W. Evans. "Monoclonal antibodies to chicken ovotransferrin: epitopic and phylogenetic analysis". Comparative Biochemistry and Physiology Part A: Physiology 112, nr 3-4 (listopad 1995): 347–54. http://dx.doi.org/10.1016/0300-9629(95)02002-0.

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25

Mohammad, Kazemi, i Richard A. Finkelstein. "Mapping epitopic regions of cholera toxin B-subunit protein". Molecular Immunology 28, nr 8 (sierpień 1991): 865–76. http://dx.doi.org/10.1016/0161-5890(91)90050-t.

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26

Bauer-Delto, Angelika. "IgE-bindenden Epitopen von therapeutischen Antikörpern auf der Spur". Allergo Journal 22, nr 3 (kwiecień 2013): 207. http://dx.doi.org/10.1007/s15007-013-0108-1.

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27

Zhou, Chuanqi, i Qingshuang Wang. "Epitopic Peptides Identified by LC–ELISA and LC–MS". Chromatographia 73, nr 9-10 (6.03.2011): 879–87. http://dx.doi.org/10.1007/s10337-011-1988-4.

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28

LEVIEUX, D., A. VENIEN i A. LEVIEUX. "Epitopic Analysis and Quantification of Bovine Myoglobin with Monoclonal Antibodies". Hybridoma 14, nr 5 (październik 1995): 435–42. http://dx.doi.org/10.1089/hyb.1995.14.435.

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29

DENG, YANG-JIA, GLENN C. ANDREWS i FRED KARUSH. "Epitopic Characterization of Neuropeptide Y (NPY) by Alanine-Scanning Mutagenesis". Hybridoma 15, nr 2 (kwiecień 1996): 159–62. http://dx.doi.org/10.1089/hyb.1996.15.159.

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30

Jaume, J. C. "Evidence for Genetic Transmission of Thyroid Peroxidase Autoantibody Epitopic "Fingerprints"". Journal of Clinical Endocrinology & Metabolism 84, nr 4 (1.04.1999): 1424–31. http://dx.doi.org/10.1210/jc.84.4.1424.

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31

Zhu, X. J., S. S. Kang, K. Hargrove, D. Shochat, M. Jarrells, M. Mojesky i S. K. Chan. "The identification of epitopic sites in human α1-proteinase inhibitor". Biochemical Journal 246, nr 1 (15.08.1987): 25–36. http://dx.doi.org/10.1042/bj2460025.

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Human α 1-proteinase inhibitor (α 1-PI) yielded nine fragments on cleavage with CNBr. The amino acid sequences of these fragments were determined. Three of these CNBr-cleavage fragments, namely fragment I (residues 64-220), fragment II (residues 243-351) and fragment III (residues 1-63), were found to bind rabbit polyclonal antibodies against chemically oxidized α 1-PI and mouse polyclonal antibodies against native α 1-PI by the Bio-Dot method (enzyme-linked immunosorbent assay on nitrocellulose). These fragments, I, II and III, inhibited by 60%, 25% and 5% respectively the binding between α 1-PI and the rabbit antibodies. Fragments I, II and III were subjected to proteolytic digestion, and 15, ten and five peptides were obtained from these fragments respectively. Only four of these peptides showed binding to the mouse antibodies against native α 1-PI. These were residues 40-63, 79-86, 176-206 and 299-323. A panel of monoclonal antibodies was prepared by conventional hybridoma technology, with chemically oxidized α 1-PI as the antigen. The ability of the monoclonal antibodies to bind native α 1-PI and CNBr-cleavage fragments I-III was determined. The monoclonal antibodies fell into three categories. Most (over 90%) belonged to group I, which was capable of binding α 1-PI and only fragment I. Antibodies in groups II and III bound α 1-PI and either fragment II or fragment III respectively. The ability of the peptides derived from proteolytic digestion of fragments I, II and III to bind three monoclonal antibodies representing each of the three groups was determined. Among all the peptides tested, only one (residues 176-206) derived from fragment I showed binding to the antibodies from group I, one (residues 299-323) derived from fragment II showed binding to the antibodies from group II, and one (residues 40-63) from fragment III showed binding to the antibodies from group III. Each of these three peptides also inhibited the binding between α 1-PI and the corresponding monoclonal antibodies. From these data we concluded that at least four epitopic regions (residues 40-63, 79-86, 176-206 and 299-323) were present in α 1-PI. Specific monoclonal antibodies to three of these sites were obtained.

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PORTEFAIX, Jean-Michel, Sabine THEBAULT, Florence BOURGAIN-GUGLIELMETTI, Maguy RIO, Claude GRANIER, Jean-Claude MANI, Michel NICOLAS, Thierry SOUSSI i Bernard PAU. "FINE EPITOPIC SPECIFICITY AND AFFINITY OF VARIOUS p53 MONOCLONAL ANTIBODIES". Biology of the Cell 88, nr 1-2 (1996): 78–78. http://dx.doi.org/10.1016/s0248-4900(97)86878-5.

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Sharma, Akansha, Naveen Arora i Janendra Batra. "Mapping Epitopic Regions of Cysteine Protease Allergen from Phaseolus vulgaris." Journal of Allergy and Clinical Immunology 145, nr 2 (luty 2020): AB222. http://dx.doi.org/10.1016/j.jaci.2019.12.176.

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Velge-Roussel, F., T. Chardès, P. Mévélec, M. Brillard, J. Hoebeke i D. Bout. "Epitopic analysis of the Toxoplasma gondii major surface antigen SAG1". Molecular and Biochemical Parasitology 66, nr 1 (lipiec 1994): 31–38. http://dx.doi.org/10.1016/0166-6851(94)90033-7.

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Kierek-Jaszczuk, D. K., W. Moennig, B. Stoke, R. Neth, S. Tan, Greiser de Wilke i O. R. Kaaden. "Epitopic Mapping of Structural and Nonstructural Aleutian Disease Virus Proteins". Intervirology 26, nr 1-2 (1986): 74–84. http://dx.doi.org/10.1159/000149684.

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Šantak, M., M. Lang Balija, G. Mlinarić Galinović, S. Ljubin Sternak, T. Vilibić-Čavlek i I. Tabain. "Genotype replacement of the human parainfluenza virus type 2 in Croatia between 2011 and 2017 – the role of neutralising antibodies". Epidemiology and Infection 146, nr 11 (18.06.2018): 1372–83. http://dx.doi.org/10.1017/s0950268818001693.

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AbstractPreviously we reported on the HPIV2 genotype distribution in Croatia 2011–2014. Here we expand this period up to 2017 and confirm that G1a genotype has replaced G3 genotype from the period 2011–2014. Our hypothesis was that the G1a-to-G3 genotype replacement is an antibody-driven event. A cross-neutralisation with anti-HPIV2 sera specific for either G1a or G3 genotype revealed the presence of genotype-specific antigenic determinants. By the profound,in silicoanalyses three potential B cell epitopic regions were identified in the hemagglutinin neuraminidase (regions 314–361 and 474–490) and fusion protein (region 440–484). The region identified in the fusion protein does not show any unique site between the G1a and G3 isolates, five differentially glycosylated sites in the G1a and G3 genotype isolates were identified in epitopic regions of hemagglutinin neuraminidase. All positively selected codons were found to be located either in the region 314–316 or in the region 474–490 what indicates a strong positive selection in this region and reveals that these regions are susceptible to evolutionary pressure possibly caused by antibodies what gives a strong verification to our hypothesis that neutralising antibodies are a key determinant in the inherently complex adaptive evolution of HPIV2 in the region.

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37

Renjifo, Ximena, Stanley Wolf, Paul-Pierre Pastoret, Hervé Bazin, Jacques Urbain, Oberdan Leo i Muriel Moser. "Carrier-Induced, Hapten-Specific Suppression: A Problem of Antigen Presentation?" Journal of Immunology 161, nr 2 (15.07.1998): 702–6. http://dx.doi.org/10.4049/jimmunol.161.2.702.

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Abstract Prior immunity against a carrier protein has been shown to modulate the serologic response to injected haptens attached to the same carrier. In particular, a carrier/hapten-carrier immunization protocol induces marked suppression for IgG2a anti-hapten Ab production but does not interfere with anti-carrier Ab responses. Although the phenomenon of epitopic suppression has been amply demonstrated, the mechanism underlying the suppression remains unknown. The selective deficiency in IgG2a secretion suggests that IFN-γ-producing Th1 cells are not properly activated. We and others have shown that the nature of the APCs present during the first encounter with the Ag influences the development of selected Th populations in vivo; dendritic cells (DCs) seem to be required for the induction of primary, Th1-type responses. Since carrier priming induces the clonal expansion of specific B cells that appear to efficiently capture the Ag, we hypothesized that the hapten-carrier conjugate may be presented by B cells in preimmunized animals. Therefore, we immunized mice to the conjugate by injecting syngeneic DCs pulsed in vitro with the Ag. Our data show that an injection of DCs and IL-12 prevents epitopic suppression, suggesting that it may result from defective Ag presentation.

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Fairlie, W. D., P. G. Stanton i M. T. W. Hearn. "Immunochemical characterization of two thyroid-stimulating hormone β-subunit epitopes". Biochemical Journal 308, nr 1 (15.05.1995): 203–10. http://dx.doi.org/10.1042/bj3080203.

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The epitopes of human thyroid-stimulating hormone (hTSH) recognized by two murine monoclonal antibodies (MAbs), designated MAb 279 and MAb 299, have been characterized. These MAbs are highly specific for the beta-subunit of TSH. The epitope recognized by MAb 279 appears to be completely conserved between bovine and human TSH and partially conserved in the porcine species. The TSH beta-subunit epitope recognized by MAb 299 is only partially conserved between the human, bovine and porcine species. Both MAbs are capable of inhibiting the binding of TSH to its receptor in a TSH radioreceptor assay, indicating that the epitopes either coincide or are located close to the TSH beta-subunit receptor-binding sites. The carbohydrate moieties of the TSH beta-subunit appear to play little or no role in the epitope recognition by MAb 279 or MAb 299 while the integrity of the disulphide bonds are essential. The epitopic recognition may also involve lysine residues, as determined by the immunoreactivity with both MAbs following citraconylation of TSH. In addition, the amino acid sequence region between residues bTSH beta 34-44 could be excised by trypsin digestion of bovine TSH beta (bTSH beta) without eliminating epitopic recognition by either MAb. These results provide further insight into the relationship between the structure of the TSH beta-subunit epitopes and location of the receptor-binding sites.

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Geffard, Estelle, Léo Boussamet, Alexandre Walencik, Florent Delbos, Sophie Limou, Pierre‐Antoine Gourraud i Nicolas Vince. "HLA‐EPI : A new EPIsode in exploring donor/recipient epitopic compatibilities". HLA 99, nr 2 (16.12.2021): 79–92. http://dx.doi.org/10.1111/tan.14505.

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Harmenberg, Ulrika, Eva Ljungdahl-Ståhle, Ulla Rudén i Britta Wahren. "Search for Epitopic Sites of Antibodies to Germ Cell Alkaline Phosphatase". Cancer Communications 3, nr 10 (1.01.1991): 305–11. http://dx.doi.org/10.3727/095535491820873759.

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Wold, J. K., H. S. Slayter, J. F. Codington i R. W. Jeanloz. "Location of an epitopic site on epiglycanin by molecular immunoelectron microscopy". Biochemical Journal 227, nr 1 (1.04.1985): 231–37. http://dx.doi.org/10.1042/bj2270231.

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Antibodies of the IgM type present in rabbit anti-epiglycanin antiserum were purified by (NH4)2SO4 precipitation and by ion-exchange, affinity and gel-filtration chromatography. After papain treatment of this fraction, followed by gel filtration, the fraction with highest apparent Mr was incubated with epiglycanin, and the antigen-antibody complexes separated by gel filtration. These were examined by electron microscopy, using rotational shadow casting, and the photographs of the complexes were mapped for the locations of the antibody molecules on the extended epiglycanin molecules. Distribution of the frequency of attachment of immunoglobulin showed a strong tendency toward binding at one end of epiglycanin, suggesting the probable presence of only one epitope, probably a glycopeptide structure containing a beta-D-galactopyranosyl-(1→3)-2-acetamido-2-deoxy-D-galactose chain.

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Chan, Edward K. L., i Eng M. Tan. "Epitopic targets for autoantibodies in systemic lupus erythematosus and Sjögrenʼs syndrome". Current Opinion in Rheumatology 1, nr 3 (październik 1989): 376–82. http://dx.doi.org/10.1097/00002281-198901030-00022.

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Abdiche, Yasmina Noubia, Rian Harriman, Xiaodi Deng, Yik Andy Yeung, Adam Miles, Winse Morishige, Leila Boustany, Lei Zhu, Shelley Mettler Izquierdo i William Harriman. "Assessing kinetic and epitopic diversity across orthogonal monoclonal antibody generation platforms". mAbs 8, nr 2 (14.12.2015): 264–77. http://dx.doi.org/10.1080/19420862.2015.1118596.

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Greiser-Wilke, I., V. Moennig, O. R. Kaaden i L. T. M. Figueiredo. "Most Alphaviruses Share a Conserved Epitopic Region on Their Nucleocapsid Protein". Journal of General Virology 70, nr 3 (1.03.1989): 743–48. http://dx.doi.org/10.1099/0022-1317-70-3-743.

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Jaume, Juan Carlos, Jin Guo, David L. Pauls, Margita Zakarija, J. Maxwell McKenzie, Janice A. Egeland, C. Lynne Burek i in. "Evidence for Genetic Transmission of Thyroid Peroxidase Autoantibody Epitopic “Fingerprints”1". Journal of Clinical Endocrinology & Metabolism 84, nr 4 (kwiecień 1999): 1424–31. http://dx.doi.org/10.1210/jcem.84.4.5639.

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Polimeno, L., A. Mittelman, L. Gennero, A. Ponzetto, G. Lucchese, A. Stufano, A. Kusalik i D. Kanduc. "Sub-epitopic dissection of HCV E1315–328HRMAWDMMMNWSPT sequence by similarity analysis". Amino Acids 34, nr 3 (26.04.2007): 479–84. http://dx.doi.org/10.1007/s00726-007-0539-7.

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Fauchet, R., M. Y. Boscher i P. Paul. "Epitopic study of HA new class I molecules (induction and quantification)". Human Immunology 23, nr 2 (styczeń 1988): 95. http://dx.doi.org/10.1016/0198-8859(88)90138-3.

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Schutze, Marie-Paule, Claude Leclerc, Frederick R. Vogel i Louis Chedid. "Epitopic suppression in synthetic vaccine models: Analysis of the effector mechanisms". Cellular Immunology 104, nr 1 (styczeń 1987): 79–90. http://dx.doi.org/10.1016/0008-8749(87)90008-6.

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Chernousova, L. N., V. I. Golyshevskaya, O. A. Kalinina, N. V. Kulikovskaya, M. A. Kapina i V. I. Litvinov. "Epitopic mapping of different mycobacteria with the use of monoclonal antibodies". Bulletin of Experimental Biology and Medicine 125, nr 3 (marzec 1998): 291–93. http://dx.doi.org/10.1007/bf02496885.

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Venien, Annie, Didier Levieux, Catherine Astier, Loïc Briand, Jean-Marc Chobert i Tomasz Haertle. "Production and Epitopic Characterization of Monoclonal Antibodies Against Bovine β-Lactoglobulin". Journal of Dairy Science 80, nr 9 (wrzesień 1997): 1977–87. http://dx.doi.org/10.3168/jds.s0022-0302(97)76141-1.

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