Relevant bibliographies by topics / Antibody-toxin conjugates – theraputic use

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Academic literature on the topic 'Antibody-toxin conjugates – theraputic use'

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Published: 4 June 2021
Last updated: 26 January 2023

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Journal articles on the topic "Antibody-toxin conjugates – theraputic use"

1

Senter, Peter D., Marilyn J. Tansey, John M. Lambert, and Walter A. Blattler. "NOVEL PHOTOCLEAVABLE PROTEIN CROSSLINKING REAGENTS AND THEIR USE IN THE PREPARATION OF ANTIBODY-TOXIN CONJUGATES." Photochemistry and Photobiology 42, no. 3 (September 1985): 231–37. http://dx.doi.org/10.1111/j.1751-1097.1985.tb08936.x.

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KIEREK-JASZCZUK, DANUTA, RONALD R. MARQUARDT, and DAVID ABRAMSON. "Use of a Heterologous Solid-Phase Antigen in an Indirect Competitive Antibody-Capture Enzyme-Linked Immunosorbent Assay for T-2 Mycotoxin." Journal of Food Protection 60, no. 3 (March 1, 1997): 321–27. http://dx.doi.org/10.4315/0362-028x-60.3.321.

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Anti- T-2 toxin (T-2) antibodies raised in chicken hosts were isolated as total IgY (chicken immunoglobulins of IgY isotype) from serum and the egg yolk. They were used for quantitation of T-2 toxin in an indirect competitive enzyme-linked immunosorbent assay (ELISA) which employed molecularly distinct toxin-carrier conjugates as solid-phase assay antigens. The sensitivities of the assays utilizing any of the purified IgY or unfractionated serum were similar but varied with respect to the type of conjugate used and could be improved by lowering the concentration of assay antigens or antibodies. Low concentrations of both immunoreactants resulted in assays of superb sensitivity, although the standard curves generated with some assay antigens decreased markedly in slopes and impractically long incubation times were required to develop sufficiently high read-out signals. However, high optical signals were obtained in a very short period of time when an amplified substrate system instead of para-nitrophenyl phosphate (pNPP) was used for the detection of a reporter enzyme, alkaline phosphatase. The use of an amplified substrate and of a solid-phase antigen that was prepared with Iso T-2 toxin attached directly to a carrier protein yielded an ELISA that had an improved ability to detect T-2.
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Lefeber, Dirk J., Barry Benaissa-Trouw, Johannes F. G. Vliegenthart, Johannis P. Kamerling, Wouter T. M. Jansen, Kees Kraaijeveld, and Harm Snippe. "Th1-Directing Adjuvants Increase the Immunogenicity of Oligosaccharide-Protein Conjugate Vaccines Related to Streptococcus pneumoniae Type 3." Infection and Immunity 71, no. 12 (December 2003): 6915–20. http://dx.doi.org/10.1128/iai.71.12.6915-6920.2003.

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ABSTRACT Oligosaccharide (OS)-protein conjugates are promising candidate vaccinesagainst encapsulated bacteria, such as Haemophilus influenzae, Neisseria meningitidis, and Streptococcus pneumoniae. Although the effects of several variables such as OS chain length and protein carrier have been studied, little is known about the influence of adjuvants on the immunogenicity of OS-protein conjugates. In this study, a minimal protective trisaccharide epitope of Streptococcus pneumoniae type 3 conjugated to the cross-reacting material of diphtheria toxin was used for immunization of BALB/c mice in the presence of different adjuvants. Subsequently, half of the mice received a booster immunization with conjugate alone. Independent of the use and type of adjuvant, all mice produced long-lasting anti-polysaccharide type 3 (PS3) antibody levels, which provided full protection against challenge with pneumococcal type 3 bacteria. All adjuvants tested increased the anti-PS3 antibody levels and opsonic capacities as measured by an enzyme-linked immunosorbent assay and an in vitro phagocytosis assay. The use of QuilA or a combination of the adjuvants CpG and dimethyl dioctadecyl ammonium bromide resulted in the highest phagocytic capacities and the highest levels of Th1-related immunoglobulin G (IgG) subclasses. Phagocytic capacity correlated strongly with Th1-associated IgG2a and IgG2b levels, to a lesser extent with Th2-associated IgG1 levels, and weakly with thiocyanate elution as a measure of avidity. Thus, the improved immunogenicity of OS-protein conjugates was most pronounced for Th1-directing adjuvants.
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Chen, Zhaochun, Rachel Schneerson, Julie A. Lovchik, Zhongdong Dai, Joanna Kubler-Kielb, Liane Agulto, Stephen H. Leppla, and Robert H. Purcell. "Bacillus anthracis Capsular Conjugates Elicit Chimpanzee Polyclonal Antibodies That Protect Mice from Pulmonary Anthrax." Clinical and Vaccine Immunology 22, no. 8 (June 3, 2015): 902–8. http://dx.doi.org/10.1128/cvi.00137-15.

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ABSTRACTThe immunogenicity ofBacillus anthraciscapsule (poly-γ-d-glutamic acid [PGA]) conjugated to recombinantB. anthracisprotective antigen (rPA) or to tetanus toxoid (TT) was evaluated in two anthrax-naive juvenile chimpanzees. In a previous study of these conjugates, highly protective monoclonal antibodies (MAbs) against PGA were generated. This study examines the polyclonal antibody response of the same animals. Preimmune antibodies to PGA with titers of >103were detected in the chimpanzees. The maximal titer of anti-PGA was induced within 1 to 2 weeks following the 1st immunization, with no booster effects following the 2nd and 3rd immunizations. Thus, the anti-PGA response in the chimpanzees resembled a secondary immune response. Screening of sera from nine unimmunized chimpanzees and six humans revealed antibodies to PGA in all samples, with an average titer of 103. An anti-PA response was also observed following immunization with PGA-rPA conjugate, similar to that seen following immunization with rPA alone. However, in contrast to anti-PGA, preimmune anti-PA antibody titers and those following the 1st immunization were ≤300, with the antibodies peaking above 104following the 2nd immunization. The polyclonal anti-PGA shared the MAb 11D epitope and, similar to the MAbs, exerted opsonophagocytic killing ofB. anthracis. Most important, the PGA-TT–induced antibodies protected mice from a lethal challenge with virulentB. anthracisspores. Our data support the use of PGA conjugates, especially PGA-rPA targeting both toxin and capsule, as expanded-spectrum anthrax vaccines.
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Niculescu-Duvaz, I., and C. J. Springer. "Antibody-Directed Enzyme Prodrug Therapy (ADEPT): A Targeting Strategy in Cancer Chemotherapy." Current Medicinal Chemistry 2, no. 3 (October 1995): 687–706. http://dx.doi.org/10.2174/092986730203220223143057.

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<P>Antibody-Directed Enzyme Prodrug Therapy (ADEPT) is a new conceptual approach designed to improve the selectivity of anti-cancer drugs. ADEPT separates the cytotoxic from the targeting function of immunoconjugates in a two phase system that has benefits over one phase chemo-, toxin- or radio-immunoconjugates. <P> This review, while discussing the basic prinicples of ADEPT and the main requirements for all the components (enzymes, prodrugs and antibodies) of the systems, also summarizes the latest results obtained with this technolo­ gy. The main components of ADEPT are described. These include the targeting of cancer cells by the antibody-enzyme conjugates, the enzymatic activation of the prodrugs, the selection of the prodrug/drug (and/or enzyme/prodrug) systems. A special emphasis has been placed on the prodrug/drug systems, the rationale behind their design and the in vitro and in vivo results obtained with the different types of the prodrugs. <P> The analysis of the advantages and disadvantages of the ADEPT system has led to the potential for clinical use of this sytem, which enables higher drug concentrations at the tumor compared to classical chemotherapy.</P>
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Tedder, T. F., V. S. Goldmacher, J. M. Lambert, and S. F. Schlossman. "Epstein Barr virus binding induces internalization of the C3d receptor: a novel immunotoxin delivery system." Journal of Immunology 137, no. 4 (August 15, 1986): 1387–91. http://dx.doi.org/10.4049/jimmunol.137.4.1387.

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Abstract Epstein Barr virus (EBV) infection of human B lymphocytes is initiated by selective binding of the virus to the C3d receptor (EBV/C3d receptor) on the cell surface and results in polyclonal proliferation of infected cells. In these studies we examined the fate of the EBV/C3d receptor during viral infection by using an immunotoxin made from a monoclonal antibody (HB5) reactive with the receptor and the potent toxin, gelonin. Binding of the HB5-gelonin conjugate to the EBV/C3d receptor before EBV infection (at concentrations as low as 10(-11) M) significantly inhibited the subsequent polyclonal proliferation of virus-infected B lymphocytes. HB5 antibody and gelonin alone did not inhibit proliferation. Because internalization of gelonin-antibody conjugates is required to cause cytotoxicity, these results indicate that infection of B lymphocytes with EBV selectively induced endocytosis of the EBV/C3d receptor with concomitant internalization of the immunotoxin. Proliferation of B lymphocytes that were activated by prior infection with EBV, or activated by cross-linking of their surface immunoglobulin molecules, was not inhibited by the antibody-toxin conjugate even at concentrations as high as 10(-7) M. Also, the growth of B lymphoblastoid cell lines cultured in the presence or absence of infectious EBV was not inhibited by HB5-gelonin. Thus, our results suggest that the EBV/C3d receptor is internalized only during the infection of normal B lymphocytes by EBV, with co-internalization of immunotoxin, and indicate that internalization of the EBV/C3d receptor-immunotoxin complex does not occur simply as a consequence of activation and proliferation of B lymphocytes. The use of a ligand to induce endocytosis of its receptor offers a new strategy for the selective delivery of immunotoxins to cells and may be more generally applicable.
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Akter, Sultana, Teemu Kustila, Janne Leivo, Gangatharan Muralitharan, Markus Vehniäinen, and Urpo Lamminmäki. "Noncompetitive Chromogenic Lateral-Flow Immunoassay for Simultaneous Detection of Microcystins and Nodularin." Biosensors 9, no. 2 (June 18, 2019): 79. http://dx.doi.org/10.3390/bios9020079.

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Cyanobacterial blooms cause local and global health issues by contaminating surface waters. Microcystins and nodularins are cyclic cyanobacterial peptide toxins comprising numerous natural variants. Most of them are potent hepatotoxins, tumor promoters, and at least microcystin-LR is possibly carcinogenic. In drinking water, the World Health Organization (WHO) recommended the provisional guideline value of 1 µg/L for microcystin-LR. For water used for recreational activity, the guidance values for microcystin concentration varies mostly between 4–25 µg/L in different countries. Current immunoassays or lateral flow strips for microcystin/nodularin are based on indirect competitive method, which are generally more prone to sample interference and sometimes hard to interpret compared to two-site immunoassays. Simple, sensitive, and easy to interpret user-friendly methods for first line screening of microcystin/nodularin near water sources are needed for assessment of water quality and safety. We describe the development of a two-site sandwich format lateral-flow assay for the rapid detection of microcystins and nodularin-R. A unique antibody fragment capable of broadly recognizing immunocomplexes consisting of a capture antibody bound to microcystins/nodularin-R was used to develop the simple lateral flow immunoassay. The assay can visually detect the major hepatotoxins (microcystin-LR, -dmLR, -RR, -dmRR, -YR, -LY, -LF -LW, and nodularin-R) at and below the concentration of 4 µg/L. The signal is directly proportional to the concentration of the respective toxin, and the use of alkaline phosphatase activity offers a cost efficient alternative by eliminating the need of toxin conjugates or other labeling system. The easy to interpret assay has the potential to serve as a microcystins/nodularin screening tool for those involved in water quality monitoring such as municipal authorities, researchers, as well as general public concerned of bathing water quality.
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Lu, Ying-Jie, Sophie Forte, Claudette M. Thompson, Porter W. Anderson, and Richard Malley. "Protection against Pneumococcal Colonization and Fatal Pneumonia by a Trivalent Conjugate of a Fusion Protein with the Cell Wall Polysaccharide." Infection and Immunity 77, no. 5 (March 2, 2009): 2076–83. http://dx.doi.org/10.1128/iai.01554-08.

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ABSTRACT Cell wall polysaccharide (CWPS), pneumolysin, and surface adhesin A (PsaA) are antigens common to virtually all serotypes of Streptococcus pneumoniae (pneumococcus), and all have been studied separately for use in protection. Previously we showed that protection against nasopharyngeal (NP) colonization by intranasal vaccination of mice with killed pneumococci is mediated by TH17 cells and correlates with interleukin-17A (IL-17A) expression by T cells in vitro; we have also shown that CWPS and other species-common antigens protect against colonization by a similar mechanism. Here we made a fusion protein of PsaA with the pneumolysin nontoxic derivative PdT and then coupled CWPS to the fusion protein, aiming to enhance immune responses to all three antigens. When given intranasally with cholera toxin adjuvant, the fusion conjugate induced higher serum antibody titers and greater priming for IL-17A responses than an equimolar mixture of the three antigens. The conjugate administered intranasally protected mice against experimental NP colonization by a strain of serotype 6B, while mice immunized with the mixture or with bivalent conjugates were not protected. Subcutaneous immunization with the conjugate and alum adjuvant likewise induced higher antibody titers than the mixture, primed for IL-17A responses, and reduced colonization. The conjugate, but not the antigen mixture, fully protected mice from fatal pneumonia caused by a highly virulent serotype 3 strain. Thus, a covalent construct of three antigens common to all serotypes exhibits protection with both mucosal and systemic administration.
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9

Pestka, James J. "Enhanced Surveillance of Foodborne Mycotoxins by Immunochemical Assay." Journal of AOAC INTERNATIONAL 71, no. 6 (November 1, 1988): 1075–81. http://dx.doi.org/10.1093/jaoac/71.6.1075.

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Abstract Mycotoxins are a chemically diverse group of fungal secondary metabolites with a wide range of toxic effects. Conventional thin-layer and instrumental methods of mycotoxin analysis are time-consuming and make routine safety and quality control screening of these compounds in agricultural commodities difficult. As an alternative, specific polyclonal and monoclonal antibodies have been raised against mycotoxin-protein conjugates and used in sensitive radioimmunoassays (RIAs) and enzyme-linked immunosorbent assays (ELISAs). One of the simplest ELISA approaches involves competition for a solid-phase antibody between a mycotoxin-enzyme conjugate and an unconjugated mycotoxin in the sample extract. ELISAs have been developed for aflatoxins B, and M„ zearalenone, T-2 toxin, and deoxynivalenol, which are highly specific, rapid (10 min), easily adaptable for analyzing large numbers of samples, and directly applicable to assaying methanol-water extracts of a wide range of foods. Several commercial mycotoxin ELISAs using this approach (most typically for aflatoxin B,) are currently being marketed. Since ELISAs will be used in large part by personnel with limited technical expertise, individual kits must be critically evaluated by analytical chemists for suggested sampling procedures, efficiency of extraction, crossreactivity, mycotoxin recovery, assay reproducibility, and product shelf-life prior to routine use in food safety and quality control screening
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10

Pui, CH, FG Behm, and WM Crist. "Clinical and biologic relevance of immunologic marker studies in childhood acute lymphoblastic leukemia." Blood 82, no. 2 (July 15, 1993): 343–62. http://dx.doi.org/10.1182/blood.v82.2.343.343.

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Abstract Immunologic marker studies of the lymphoid leukemias have greatly improved the precision of diagnosis of these disorders by providing specific information regarding the lineage and stage of maturation of the malignant cells. Such studies have also enhanced our understanding of normal lymphocyte development, permitting reproducible identification of lymphoid cells in discrete developmental stages. By elucidating the functions of lymphoid cell differentiation antigens, it has been possible to gain insight into the signal transduction mechanisms by which these cells interact among themselves and with other cell types. Similar studies have shown that ALL is an immunophenotypically heterogeneous disease with clinically important subtypes representing clonal expansions of lymphoblasts at different stages of maturation. Furthermore, successful correlation of immunophenotype with certain karyotypic and molecular abnormalities, which appear to underlie most or all leukemias, were made possible by the inclusion of immunologic marker assessment. Interestingly, many of these phenotype-related abnormalities have involved either the Ig or TCR genes, thus providing additional clues to the mechanisms of leukemogenesis. Knowledge of the immunologic features of leukemic cells has been essential for the generation of phenotype-specific response data in the context of modern therapy for ALL. With wider use of intensive treatment, the traditional prognostic distinctions among immunophenotypes have begun to disappear; however, certain classes of agents have more favorable toxicity/efficacy ratios against some immunophenotypes than others, justifying continued efforts to target therapy by immunologic species of ALL. Antibody-toxin conjugates, or immunotoxins, have induced complete responses in preliminary trials and may prove clinically useful, perhaps in combination with chemotherapy, if their toxic side effects can be controlled. Finally, immunologic markers may serve as sensitive targets for the detection of minimal residual disease; the clinical usefulness of this approach will depend on prospective comparisons with molecular methods.
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Dissertations / Theses on the topic "Antibody-toxin conjugates – theraputic use"

1

Ng, Wai-yun Louisa, and 吳慧欣. "Production of variants of mitogillin with reduced IgE bindingactivity." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2004. http://hub.hku.hk/bib/B31972093.

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"Construction of a Recombinant Immunotoxin." University of Technology, Sydney. Faculty of Science, 1995. http://hdl.handle.net/2100/270.

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In recent years a number of therapeutically useful immunotoxins have been produced using recombinant gene technology. In general, this involves fusion of a toxin gene with sequence encoding a variety of clinically relevant proteins or peptides. Using these techniques a recombinant immunotoxin has been engineered by fusing the genes encoding an antibody fragment with the sequence of a small cytolytic peptide, melittin. The antibody fragment consists of the antigen binding site derived from a murine monoclonal antibody K- 1-21, which binds to human free kappa light chains and recognises a specific epitope (KMA) expressed on the surface of human myeloma and lymphoma cells. The toxic portion of the molecule is melittin, a 26 amino acid, membrane lytic peptide which is a major component of bee venom. Using PCR a single chain Fv (scFv) was constructed by linking VH and VL genes with an oligonucleotide encoding a flexible, hydrophilic peptide. The melittin gene was synthesised as an oligonucleotide and extended by PCR. Nucleotide sequence encoding a linker peptide was added to the 5' end and a primer encoding a FLAG peptide was used to extend the 3' end. This gene construct was then ligated into the recombinant expression vector, pPOW scFv, to create the fusion gene encoding the recombinant immunotoxin. The gene construct was expressed in the periplasm of E.coli (TOPP2) using the secretion signal pelB . Expression of the foreign protein was monitored by western blot using a monoclonal antibody which recognises the FLAG peptide encoded at the carboxy terminal region of the gene construct. Expression of the recombinant immunotoxin was optimised and the resulting protein was purified using anti-FLAG M2 affinity chromatography. Antigen binding activity was assessed by ELISA and flow cytometry using a human myeloma cell line, HMy2, which expresses the KMA antigen.Binding of the immunotoxin to a control human cell line, K562, which does not express KMA on the cell surface was also assessed. The results indicated that the recombinant immunotoxin retained antigen binding specificity and it was cytotoxic towards the target cell line (HMy2).
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"Construction of a recombinant immunotoxin." Thesis, University of Technology, Sydney. Faculty of Science, 1995. http://hdl.handle.net/10453/20069.

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University of Technology, Sydney. Faculty of Science.
In recent years a number of therapeutically useful immunotoxins have been produced using recombinant gene technology. In general, this involves fusion of a toxin gene with sequence encoding a variety of clinically relevant proteins or peptides. Using these techniques a recombinant immunotoxin has been engineered by fusing the genes encoding an antibody fragment with the sequence of a small cytolytic peptide, melittin. The antibody fragment consists of the antigen binding site derived from a murine monoclonal antibody K- 1-21, which binds to human free kappa light chains and recognises a specific epitope (KMA) expressed on the surface of human myeloma and lymphoma cells. The toxic portion of the molecule is melittin, a 26 amino acid, membrane lytic peptide which is a major component of bee venom. Using PCR a single chain Fv (scFv) was constructed by linking VH and VL genes with an oligonucleotide encoding a flexible, hydrophilic peptide. The melittin gene was synthesised as an oligonucleotide and extended by PCR. Nucleotide sequence encoding a linker peptide was added to the 5' end and a primer encoding a FLAG peptide was used to extend the 3' end. This gene construct was then ligated into the recombinant expression vector, pPOW scFv, to create the fusion gene encoding the recombinant immunotoxin. The gene construct was expressed in the periplasm of E.coli (TOPP2) using the secretion signal pelB . Expression of the foreign protein was monitored by western blot using a monoclonal antibody which recognises the FLAG peptide encoded at the carboxy terminal region of the gene construct. Expression of the recombinant immunotoxin was optimised and the resulting protein was purified using anti-FLAG M2 affinity chromatography. Antigen binding activity was assessed by ELISA and flow cytometry using a human myeloma cell line, HMy2, which expresses the KMA antigen.Binding of the immunotoxin to a control human cell line, K562, which does not express KMA on the cell surface was also assessed. The results indicated that the recombinant immunotoxin retained antigen binding specificity and it was cytotoxic towards the target cell line (HMy2).
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Books on the topic "Antibody-toxin conjugates – theraputic use"

1

Ramakrishnan, S. Cytotoxic conjugates. Austin: R.G. Landes Co., 1993.

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1960-, Tyle Praveen, and Ram Bhanu P. 1951-, eds. Targeted therapeutic systems. New York: Dekker, 1990.

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1947-, Wiley Ronald G., and Lappi Douglas A, eds. Molecular neurosurgery with targeted toxins. Totowa, N.J: Humana Press, 2005.

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Immunotoxin Methods and Protocols. Humana Press, 2001.

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Frankel, A. Clinical Applications of Immunotoxins (Current Topics in Microbiology and Immunology). Springer-Verlag Telos, 1998.

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Carl-Wilhelm, Vogel, ed. Immunoconjugates: Antibody conjugates in radioimaging and therapy of cancer. New York: Oxford University Press, 1987.

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Antibodydrug Conjugates And Immunotoxins From Preclinical Development To Therapeutic Applications. Springer, 2012.

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1927-, Baldwin R. W., Byers Vera S, and Mann Ronald D. 1928-, eds. Monoclonal antibodies and immunoconjugates. Carnforth, Lancs, UK: Parthenon Pub. Group, 1990.

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W, Baldwin R., Byers Vera S, and Mann R. D. 1928-, eds. Monoclonal antibodies and immunoconjugates in cancer treatment. Carnforth: Parthenon Publishing, 1990.

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1935-, Quash Gerard A., Rodwell John D. 1946-, Institut national de la santé et de la recherche médicale (France), and CYTOGEN Corporation, eds. Covalently modified antigens and antibodies in diagnosis and therapy. New York: Dekker, 1989.

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