Relevant bibliographies by topics / Antigen specificity

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
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  6. Reports

Academic literature on the topic 'Antigen specificity'

Author: Grafiati
Published: 25 May 2024

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Journal articles on the topic "Antigen specificity"

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Rhodes, S. G., D. Gavier-Widen, B. M. Buddle, A. O. Whelan, M. Singh, R. G. Hewinson, and H. M. Vordermeier. "Antigen Specificity in Experimental Bovine Tuberculosis." Infection and Immunity 68, no. 5 (May 1, 2000): 2573–78. http://dx.doi.org/10.1128/iai.68.5.2573-2578.2000.

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ABSTRACT This report describes the kinetics of T-cell responses to a panel of mycobacterial antigens (PPD-M, PPD-A, ESAT-6, Ag85, 38kD, MPB64, MPB70, MPB83, hsp16.1, hsp65, and hsp70) following experimental infection of cattle with Mycobacterium bovis. Increased antigen-specific lymphocyte proliferation, gamma interferon, and interleukin-2 responses were observed in all calves following infection. Positive lymphocyte proliferation and cytokine responses to PPD-M and ESAT-6 were observed throughout the infection period studied. In contrast, responses to all other antigens were more variable and were not constantly present, suggesting that antigen cocktails rather than individual antigens should be used for immunodiagnosis. The detection of cytokine responses in the absence of lymphocyte proliferation, particularly during the early stages of infection, suggests a role for antigen-specific cytokine readout systems in the early identification of M. bovis infection in cattle.
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Jain, Deepti, and Dinakar M. Salunke. "Antibody specificity and promiscuity." Biochemical Journal 476, no. 3 (February 5, 2019): 433–47. http://dx.doi.org/10.1042/bcj20180670.

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Abstract The immune system is capable of making antibodies against anything that is foreign, yet it does not react against components of self. In that sense, a fundamental requirement of the body's immune defense is specificity. Remarkably, this ability to specifically attack foreign antigens is directed even against antigens that have not been encountered a priori by the immune system. The specificity of an antibody for the foreign antigen evolves through an iterative process of somatic mutations followed by selection. There is, however, accumulating evidence that the antibodies are often functionally promiscuous or multi-specific which can lead to their binding to more than one antigen. An important cause of antibody cross-reactivity is molecular mimicry. Molecular mimicry has been implicated in the generation of autoimmune response. When foreign antigen shares similarity with the component of self, the antibodies generated could result in an autoimmune response. The focus of this review is to capture the contrast between specificity and promiscuity and the structural mechanisms employed by the antibodies to accomplish promiscuity, at the molecular level. The conundrum between the specificity of the immune system for foreign antigens on the one hand and the multi-reactivity of the antibody on the other has been addressed. Antibody specificity in the context of the rapid evolution of the antigenic determinants and molecular mimicry displayed by antigens are also discussed.
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Kendall-Taylor, P., D. Jones, and S. Atkinson. "The specificity of autoantibodies in Graves' ophthalmopathy." Acta Endocrinologica 116, no. 1_Suppl (August 1987): S330—S333. http://dx.doi.org/10.1530/acta.0.114s330.

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Abstract. An autoantibody to orbital antigens is found in patients with Graves' ophthalmopathy. This autoantibody also binds to skeletal muscle antigen. Occasional positive responses have been seen in patients with Hashimoto's disease and with non-organ-specific autoimmune disease. Eye muscle has a higher innervation ratio than skeletal muscle and may be of different embryological origin, but it is nevertheless closely related to skeletal muscle and it is perhaps not surprising that the antibody should interact with both these types of muscle. What remains quite unexplained, is why the disease process apparently affects eye muscle only. The antigen appears to be distinct from thyroidal antigens, but further work with a larger patient population is necessary before one can be certain of this. To date it has been possible to exclude the cytoskeletal proteins, myosin and actin, and also the TSH receptor as possible candidates for the responsible antigens. Further studies are in progress to elucidate the nature of this muscle antigen.
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Jiang, Ning, Ke-yue Ma, Alexandra A. Schonnesen, Chenfeng He, Amanda Xia, Eric Sun, Eunise Chen, Katherine Sebastian, Robert Balderas, and Mrinalini Kulkarni-Date. "High-Throughput and High-Dimensional Single Cell Analysis of Antigen-Specific CD8+ T cells." Journal of Immunology 206, no. 1_Supplement (May 1, 2021): 27.22. http://dx.doi.org/10.4049/jimmunol.206.supp.27.22.

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Abstract Although critical to T cell function, antigen specificity is often omitted in high-throughput multi-omics based T cell profiling due to technical challenges. We describe a high-dimensional, tetramer-associated T cell receptor sequencing (TetTCR-SeqHD) method to simultaneously profile TCR sequences, cognate antigen specificities, targeted gene-expression, and surface-protein expression from tens of thousands of single cells. Using polyclonal CD8+ T cells with known antigen specificity and TCR sequences, we demonstrated over 98% precision for detecting the correct antigen specificity. We also evaluated gene-expression and phenotypic differences among antigen-specific CD8+ T cells and characterized phenotype signatures of influenza- and EBV-specific CD8+ T cells that are unique to their pathogen targets. Moreover, with the high-throughput capacity of profiling hundreds of antigens simultaneously, we applied TetTCR-SeqHD to identify antigens that preferentially enrich cognate CD8+ T cells in type 1 diabetes patients compared to healthy controls, and discovered a TCR that cross reacts between diabetic and microbiome antigens. TetTCR-SeqHD is a powerful approach for profiling T cell responses.
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Lesavre, Philippe. "Antineutrophil Cytoplasmic Autoantibodies Antigen Specificity." American Journal of Kidney Diseases 18, no. 2 (August 1991): 159–63. http://dx.doi.org/10.1016/s0272-6386(12)80873-0.

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Bolhuis, Reinder L. H., Els Sturm, Jan Willem Gratama, and Eric Braakman. "Engineering T lymphocyte antigen specificity." Journal of Cellular Biochemistry 47, no. 4 (December 1991): 306–10. http://dx.doi.org/10.1002/jcb.240470404.

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Klinger, Mark, Ruth Taniguchi, Joyce Hu, Tim Hayes, Tobias Wittkop, Thomas Asbury, Martin Moorhead, et al. "A scalable multiplex assay enabling assessment of T cell receptor specificity to hundreds of self- and pathogen-derived antigens." Journal of Immunology 196, no. 1_Supplement (May 1, 2016): 209.4. http://dx.doi.org/10.4049/jimmunol.196.supp.209.4.

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Abstract Monitoring antigen-specific T cells is critical for the study of immune responses and development of biomarkers and immunotherapeutics. We previously developed and validated a novel multiplex assay (MIRA, or Multiplexed Identification of T cell Receptor Antigen specificity) that combines conventional immune monitoring techniques and TCR repertoire sequencing to assess T cell specificity to large numbers of query antigens. MIRA is a sensitive assay enabling detection of antigen-specific TCR clonotypes well below the limit of detection of conventional immune monitoring assays including flow cytometry and ELISPOT. Here we report the results from a scaled-up version of the assay using 270 different query peptide antigens (159 self- and 111 pathogen-derived). We identified >500 TCR clonotypes at frequencies as low as 1 per million T cells that were specific to 41 query antigens from 6 healthy HLA-A*02-positive individuals. Most of the antigen-specific TCRs identified recognized one of 27 different peptides derived from a variety of pathogens including CMV, EBV, Flu, Rotavirus, HSV, mTB, WNV and HIV. A subset of antigen-specific TCRs recognized one of 14 different peptides derived from self including MART1, RCC, BCL-2, MAGE, STEAP1, KLK4, CAMEL and MOG. These data support the notion that escape and survival of self antigen-specific T cells occurs without causing overt autoimmunity in healthy individuals. We show here that MIRA can be used to assess TCR specificities to hundreds of query antigens simultaneously. The assay is highly scalable and can be easily modified to accommodate thousands of additional query antigens. This technology may be used to monitor T cell specificity to antigens relevant to infection, autoimmunity and cancer.
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Shahi, Payam, Bruce Adams, Daniel Reyes, Shamoni Maheshwari, Nima Mousavi, Sreenath Krishnan, Nandhini Ramen, et al. "High-Throughput Antibody Discovery Using Barcode Enabled Antigen Mapping (BEAM." Journal of Immunology 210, no. 1_Supplement (May 1, 2023): 249.28. http://dx.doi.org/10.4049/jimmunol.210.supp.249.28.

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Abstract Multi-analyte single cell technologies have potential to greatly accelerate antibody discovery by identifying antigen-specific B cells. Barcode Enabled Antigen Mapping (BEAM) provides a high-throughput, multimodal analysis of antigen-bound B cells (BEAM-Ab) using 10x Genomics Chromium Single Cell Immune Profiling v2 Solution and novel computational approaches to discover B-cell receptor (BCR) sequences for further functional characterization. To demonstrate the antigen sensitivity of BEAM-Ab, we spiked in 5% Hen Egg Lysozyme (HEL) and 5% gp120 transgenic B cells in 90% wild type non-transgenic splenocytes. The cells were screened using a panel of barcoded antigens and then CD19+PE+ (antigen+) B cells were isolated using flow cytometry. Single cell gene expression, BCR, and antigen barcode analysis indicated clonotype specificity to the respective antigens in the sorted cells. Furthermore, we demonstrated BEAM-Ab specificity by analyzing a convalescent COVID patient sample against an antigen panel containing five different COVID antigens and a negative control. Analysis of this COVID sample suggests the clonal expansion of B cells recognizing the ectodomain of the wild type SARS-CoV2 spike protein, receptor binding domain of spike protein, and the ectodomain of the D614G mutant spike protein. We did not observe any clonal expansion to Omicron-specific antigen or the non-specific negative control in our dataset. Our data demonstrates that BEAM-Ab is an effective antibody discovery tool. BEAM-Ab unlocks the ability to rapidly screen large numbers of samples with an accurate single cell resolution and antigen specificity, with the entire workflow generating the candidate sequences just one week after sample processing.
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Tseng, Diane, Shin-Heng Chiou, Xinbo Yang, Alexandre Reuben, Julie Wilhelmy, Alana McSween, Stephanie Conley, et al. "Discovery of a novel shared tumor antigen in human lung cancer." Journal of Clinical Oncology 38, no. 15_suppl (May 20, 2020): 3087. http://dx.doi.org/10.1200/jco.2020.38.15_suppl.3087.

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3087 Background: While there has been much attention on mutation-associated neoantigens in tumors, there is less known about non-mutated tumor antigens that are shared across individuals. Understanding tumor-infiltrating T cell recognition of shared tumor antigens is important for understanding cancer immune recognition and escape, and may reveal novel targets for therapy. Methods: We have established a novel approach for discovering shared tumor antigens in human lung cancer. This approach involves identifying candidate T cell receptor (TCR) alpha/beta pairs that are predicted to exhibit specificity for shared tumor antigens in the context of a given human leukocyte antigen (HLA). We then screen the T cell receptor for binding to yeast display libraries of peptide-HLA. The Mark Davis lab at Stanford has previously developed an algorithm that groups T cell receptors into antigen specificity groups based on shared motifs within the TCR complementarity-determining region 3 (CDR3) sequences. Leveraging a dataset of over 700K CDR3 sequences from 178 HLA-typed non-small cell lung cancer (NSCLC) patients, we have found up to 4,300 antigen specificity groups after applying stringent cutoffs. We sequenced TCR alpha/beta pairs from 15 patients with lung adenocarcinoma (n = 4,705). Results: We identified an antigen specificity group enriched in tumor compared to adjacent uninvolved lungs. Antigen screening of the T cell receptor belonging to this specificity group using an A02 yeast display libraries led to the identification of a dominant peptide after four rounds of enrichment. We functionally validated that the peptide derived from the protein TMEM161A stimulated Jurkat cells expressing the TCR alpha/beta receptor of interest. We show that full-length TMEM161A protein is processed and presented into a peptide that stimulates primary T cells expressing the TCR alpha/beta receptor. We observe that a peptide from Epstein-Barr virus (EBV) protein LMP2 also stimulated the same TCR alpha/beta receptor. We have show that TMEM161A RNA and protein are overexpressed in human lung cancer compared to adjacent uninvolved lungs. Conclusions: We have demonstrated a novel approach toward antigen discovery and identified a shared tumor antigen TMEM161A in human lung cancer.
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Zollinger, Wendell D., Elizabeth E. Moran, and Deborah H. Schmiel. "Characterization of an Antibody Depletion Assay for Analysis of Bactericidal Antibody Specificity." Clinical and Vaccine Immunology 16, no. 12 (October 14, 2009): 1789–95. http://dx.doi.org/10.1128/cvi.00255-09.

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ABSTRACT Serum bactericidal antibodies are important for protection against systemic Neisseria meningitidis infections. Consequently, identifying the specific targets of bactericidal antibodies is important for understanding protective immunity to meningococcal disease and for vaccine development and evaluation. We have developed a new assay that can be used to investigate the specificity of serum bactericidal antibodies. Prior to testing for bactericidal activity, antibodies specific for a given antigen or group of antigens are depleted from a serum sample by incubation with the antigen(s) bound to the wells of a 96-well microplate. A dilution series of the antigen is bound to the plate to assess the effectiveness of the antigen in removing the bactericidal antibodies. Removal of antibodies with solid-phase antigen prior to bactericidal testing avoids depletion of complement by soluble immune complexes that can form when soluble antigen is present in the bactericidal test mixture (direct inhibition). The parameters associated with this assay are investigated and compared with those associated with a direct-inhibition assay. The bactericidal depletion assay can be an effective tool for studying the specificity of serum bactericidal antibodies.
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Dissertations / Theses on the topic "Antigen specificity"

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Košmrlj, Andrej 1981. "Statistical physics of T cell receptor development and antigen specificity." Thesis, Massachusetts Institute of Technology, 2011. http://hdl.handle.net/1721.1/68875.

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Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Physics, 2011.
Cataloged from PDF version of thesis.
Includes bibliographical references (p. 147-158).
Higher organisms, such as humans, have an adaptive immune system that usually enables them to successfully combat diverse (and evolving) microbial pathogens. The adaptive immune system is not preprogrammed to respond to prescribed pathogens, yet it mounts pathogen-specific responses against diverse microbes, and establishes memory of past infections (the basis of vaccination). Although major advances have been made in understanding pertinent molecular and cellular phenomena, the mechanistic principles that govern many aspects of an immune response are not known. In this thesis, I illustrate how complementary approaches from the physical and life sciences can help confront this challenge. Specifically, I describe work that brings together statistical mechanics and cell biology to shed light on how key regulators of the adaptive immune system, T cells, are selected to enable pathogen-specific responses. A model of T cell development is introduced and analyzed (computationally and analytically) by employing methods from statistical physics, such as extreme value distributions and Hamiltonian minimization. Results show that selected T cell receptors are enriched in weakly interacting amino acids. Such T cell receptors recognize (i.e. bind sufficiently strongly to) pathogens through several contacts of moderate strength, each of which makes a significant contribution to overall binding. Disrupting any contact by mutating the pathogen is statistically likely to abrogate T cell recognition of the mutated pathogen. We propose that this is the mechanism for the specificity of T cells for unknown pathogens. The T cell development model is also used to discuss one way in which host genetics can influence the selection of T cells and concomitantly the control of HIV infection. A model of the T cell selection process as diffusion in a random field of immobile traps that intermittently turn "on" and "off" is developed to estimate the escape probability of dangerous T cells that could cause autoimmune disease. Finally, and importantly, throughout this thesis, I describe, how the theoretical studies are closely synergistic/complementary with biological experiments and human clinical data.
by Andrej Košmrlj.
Ph.D.
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Sandberg, Johan. "CD8⁺ T cell specificity in thymic selection and in the recognitionof antigen /." Stockholm, 1999. http://diss.kib.ki.se/1999/91-628-3686-2/.

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Forsström, Björn. "Characterization of antibody specificity using peptide array technologies." Doctoral thesis, KTH, Proteomik och nanobioteknologi, 2014. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-155723.

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Antibodies play an important role in the natural immune response to invading pathogens. The strong and specific binding to their antigens also make them indispensable tools for research, diagnostics and therapy. This thesis describes the development of methods for characterization of an- tibody specificity and the use of these methods to investigate the polyclonal antibody response after immunization. Paper I describes the development of an epitope-specific serum fractionation technique based on epitope map- ping using overlapping peptides followed by chromatographic separation of polyclonal serum. This technique together with another epitope mapping technique based on bacterial display of protein fragments were then used to generate antibody sandwich pairs (Paper I), investigate epitope variations of repeated immunizations (Paper II) and to determine the ratio of antibodies targeting linear and conformational epitopes of polyclonal antibodies (Paper III). Paper IV describes the optimization of in situ-synthesized high-density peptide arrays for epitope mapping and how different peptide lengths influ- ence epitope detection and resolution. In Paper V we show the development of planar peptide arrays covering the entire human proteome and how these arrays can be used for epitope mapping and off-target binding analysis. In Paper VI we show how polyclonal antibodies targeting linear epitopes can be used for peptide enrichment in a rapid, absolute protein quantification protocol based on mass spectrometry. Altogether these investigations demonstrate the usefulness of peptide arrays for fast and straightforward characterization of antibody specificity. The work also contributes to a deeper understanding of the polyclonal anti- body response obtained after immunization with recombinant protein frag- ments.

QC 20141111

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Moots, Robert J. "The fine specificity of HLA class I-restricted antigen recognition by cytotoxic T lymphocytes." Thesis, Open University, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.315327.

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Peche, Leticia Yamila. "Evidence of functional specificity within the MAGE-I family of tumor expressed proteins." Doctoral thesis, SISSA, 2008. http://hdl.handle.net/20.500.11767/4674.

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The Melanoma Antigen Genes (MAGE) belong to a large family of highly conserved genes, sharing an elevated degree of sequence homology. The characteristic feature of MAGE proteins is a C-terminal domain present in all the members of the family, termed the MAGE homology domain (MHD). Based on their expression pattern MAGE genes are classified in MAGE-I and MAGE-II genes. MAGE-I genes expression is restricted to tumor and male germ cells, and for this reason they form part of a growing group of genes named Cancer Testis Antigens (CTA). Expression of MAGE-I genes seems to be an early event during gametogenesis and tumorigenesis, and correlates with genomewide hypomethylation, an important event frequently observed in carcinogenesis. Since their discovery in 1991, MAGE-I genes were mostly studied for their potential use in immunotherapy against cancer or as prognostic markers in tumors. The biological roles that these proteins play in tumor development and progression were poorly investigated. Moreover, due to their sequence homology, MAGE-I proteins are still considered functionally redundant proteins. In the present work, we functionally characterized different MAGE-I genes, in particular MageA2 and MageB2 genes, demonstrating their functional specificity. We show that MageA2 protein confers wild-type p53 tumor suppressor-sensitive resistance to chemotherapeutic drugs, such as etoposide, by recruitment of HDAC3 to p53/MageA2 complex, thus repressing p53 transactivation function. The mechanism responsible for the repressive effect of MageA2, relies on an impaired acetylation of both p53 and histones surrounding p53 binding sites by MageA2/HDAC3 complexes. The correlation between MAGE-A expression and resistance to apoptosis has been analyzed in short-term melanoma cell lines, where combined treatment with etoposide and trichostatin A (an inhibitor of histone deacetylases) restores the p53 response and reverts chemoresistance in cells expressing high levels of MAGE-A. We also present evidence that MageA2 is able to repress PML3-induced p53 activity in a specific manner, by affecting PML3 mediated p53 acetylation at the PML3 nuclear bodies (PML3-NBs). The relevance of MageA2 expression on PML3 activity has been analyzed in a normal cellular context, in which PML3 induces premature senescence, an important barrier against cell transformation. In this regard, we demonstrate that MageA2 impairs the senescence response associated to PML3 expression in normal human fibroblast. A possible mechanism for the inhibitory effect of MageA2 on PML3 is that MageA2 could interfere with PML3 sumoylation. The specificity of MageA2 functions is demonstrated by the fact that, despite high level of homology, MageA4 is not recruited to the NBs, it does not affect p53 activity nor is able to interfere with PML3 induced senescence. Finally, we have preliminarily characterized the MageB2 protein, showing that it specifically localizes to the nucleolus where it is able to interact with many nucleolar proteins. Nucleolar stress induces MageB2 relocalization to the nucleoplasm, a characteristic behavior of nucleolar proteins that regulate processes such as rRNA metabolism or RNA processing. Moreover, since we observed that MageB2 induces pRb relocalization to the nucleoli and increases E2F1 transactivation function, including E2F1-induced rRNA transcription, we hypothesize that it could play a positive role in the regulation of cell proliferation. Altogether the work presented here consistently supports the notion that, despite the high level of sequence homology, there is a clear degree of functional specificity within members of the MAGE-I family. Hence, we can hypothesize that different MAGE-I proteins, for instance MageA2 and MageB2, could act within different pathways in the regulation of complex processes such as apoptosis, proliferation, and senescence. By targeting different signal transduction pathways their final outcome could be related to the establishment and progression of the tumors where they are expressed. In this Thesis, we give a comprehensive view on the functional differences among MAGE-I members, focusing on Mage-A and Mage-B members. Implementation of our investigation could be the first step leading to understanding of how expression of specific MAGE-I members could impact cancer cell behaviour thus prompting the use of MAGE-I genes as novel cancer specific targets for the development of new drug-based therapies.
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RIGAMONTI, VALERIA. "Development of a quantitative chemiluminescent immunoassay for the hepatitis B. antigen detection." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2011. http://hdl.handle.net/10281/19390.

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The surface antigen of the hepatitis B (HBsAg) is the first detectable serological marker in infected patients. It enables to detect the infection in the first stages of the disease allowing a timely therapeutic intervention with a higher chance of success. A quantitative immunoassay will allow the customers to carry out the quantitative determination of the HBsAg at the start of treatment and during the follow up. Mutations that occur in a conformational surface region, called “a” loop, of HBsAg can cause an epitope loss impairing the antibody interaction deriving from host immune response as well as from vaccination and present in commercial immunoassays. DiaSorin new quantitative immunoassay has high sensibility and specificity and the ability to detect HBsAg mutants.
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Roter, Evan. "Beta2-glycoprotein I-specific T cells: antigen specificity and role in the induction of anti-phospholipid syndrome." Thesis, McGill University, 2010. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=86847.

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Antiphospholipid syndrome (APS) is an autoimmune disorder characterized by the presence of autoantibodies to phospholipid (PL)-binding proteins, such as β2-glycoprotein I (β2GPI), and clinical manifestations including thrombosis and/or recurrent pregnancy loss. APS patients have β2GPI-reactive T cells, but their origin is unclear. We hypothesized that mice immunized with human (foreign) β2GPI would produce T cells reactive with murine β2GPI. We further proposed that β2GPI oxidation, reduction, or binding to PL would alter T cell recognition of β2GPI. Splenic T cells from C57BL/6 mice immunized repeatedly with human β2GPI and lipopolysaccharide were found to produce IFN-γ in response to native human β2GPI, alone or bound to anionic PL; reduced β2GPI; and to a lesser extent oxidized β2GPI. However, the T cells did not respond to any form of murine β2GPI. β2GPI-reactive T cell hybridomas showed similar results. Antibodies to murine β2GPI were produced by immunization with human or murine β2GPI with complete Freund's adjuvant, but no β2GPI-reactive T cell response was observed. Our data indicate that a break in B cell tolerance to autologous β2GPI can occur in the absence of a detectable in vitro T cell response to this protein.
Le syndrome antiphospholipide (SAPL) est une maladie autoimmune caractérisée par la présence d'auto-anticorps antiphospholipides (aPL) dirigés contre des protéines liant les phospholipides anioniques dont la β2-glycoproteine I (β2GPI), ainsi que par des manifestations cliniques incluant la thrombose et la perte foetale récurrente. Les patients souffrant du SAPL possèdent des lymphocytes T sensibles au β2GPI mais leurs origines restent inconnues. Nous posons donc l'hypothèse que des souris immunisées avec β2GPI humain produiraient des lymphocytes T sensibles au β2GPI endogène. De surcroit, nous proposons que l'oxydation, la réduction, ou la liaison du β2GPI aux phospholipides affecterait l'identification du β2GPI par les lymphocytes T. Après de nombreuses immunisations avec du β2GPI humain, des lymphocytes T de rate provenant de souris C57BL/6 produisent de l'interferon-γ (IFN-γ) en présence soit de β2GPI humain - isolé ou lié à un phospholipide anionique; de β2GPI humain réduit; ainsi, mais à un degré moindre, de β2GPI humain oxydé. Toutefois, les lymphocytes T n'ont produit pas de réponses à aucune forme de β2GPI murin qui soient. Des résultats similaires avec hybridomes de lymphocytes T sensibles au β2GPI furent aussi obtenus. D'autre part des anticorps contre le β2GPI murin furent obtenus à la suite d'immunisations, utilisant du β2GPI humain ou murin conjointement avec de l'adjuvant de Freund, mais aucune réponse de lymphocytes T sensibles au β2GPI furent observée. Nos résultats indiquent que la tolérance des lymphocytes B au β2GPI autologue peut être brisée en absence d'une réponse détectable in vitro de lymphocytes T au β2GPI.
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Johansson, Daniel X. "Expression and interaction studies of recombinant human monoclonal antibodies /." Stockholm, 2007. http://diss.kib.ki.se/2007/978-91-7357-137-1/.

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Babakhani, Farah Kondori 1960. "IN VITRO PRODUCTION AND SPECIFICITY OF ANTI-DNA AUTO ANTIBODIES BY NEW ZEALAND BLACK/NEW ZEALAND WHITE F1 MICE." Thesis, The University of Arizona, 1986. http://hdl.handle.net/10150/276471.

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Lagardien, Zaida. "The characterisation of the peanut agglutinin an evolved plant lectin, with improved specificity to the Thompson Freidenriech antigen." Master's thesis, University of Cape Town, 2013. http://hdl.handle.net/11427/3136.

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Peanut agglutinin (PNA), a carbohydrate binding protein, is able to recognise and bind a number of distinct carbohydrate structures that have been implicated in a number of disease pathologies in humans. In vitro studies of PNA have previously been shown to have some specificity for the Thomson Freidenriech antigen (T-antigen), found on malignant human cells, and this specificity has made PNA an important target for protein engineering experiments aimed at improving its specificity and affinity. A number of tumour cells are characterised by altered states and patterns of glycosylation on cell surfaces and suitably engineered lectins may be able to recognise tumour specific carbohydrate structures. This study was aimed at carrying out the biophysical characterisation of a set of PNA mutants which showed apparent improvement in specificity for the T-Antigen. Previous studies have aimed to engineer this lectin in order to direct its recognition properties towards the T-antigen and away from lactose, the preliminary binding affinities of these mutants being determined using Surface Plasmon Resonance (SPR). Here a set of PNA mutants were characterised, proteins expressed and purified to determine binding activities to the T-antigen, N-Acetyl-Dlactosamine (LacNAc) and lactose through the use of Protein Micro Array technology as well as Enzyme linked immunosorbant assays (ELISA).
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Books on the topic "Antigen specificity"

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Schenkel-Brunner, Helmut. Human blood groups: Chemical and biochemical basis of antigen specificity. Wien: Springer-Verlag, 1995.

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Schenkel-Brunner, Helmut. Human blood groups: Chemical and biochemical basis of antigen specificity. 2nd ed. Wien: Springer, 2000.

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Human blood groups: Chemical and biochemical basis of antigen specificity. 2nd ed. Wien: Springer, 2000.

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Human blood groups: Chemical and biochemical basis of antigen specificity. Wien: Springer-Verlag, 1995.

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K, Pfeffer, ed. Function and specificity of [alpha/delta] T cells: International Workshop, Schloss Elmau, Bavaria, FRG, October 14-16, 1990. Berlin: Springer, 1991.

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Workshop on Mechanisms and Specificity of HIV Entry into Host Cells (1989 San Francisco, Calif.). Mechanisms and specificity of HIV entry into host cells. New York: Plenum Press, 1991.

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Special Programme for Research and Training in Tropical Diseases, Foundation for Innovative New Diagnostics, and Centers for Disease Control and Prevention (U.S.), eds. Malaria rapid diagnostic test performance: Results of WHO product testing of malaria RDTs : round 2 (2009). Geneva: World Health Organization on behalf of the Special Programme for Research and Training in Tropical Diseases, 2010.

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service), ScienceDirect (Online, ed. Tissue-specific vascular endothelial signals and vector targeting. Amsterdam: Elsevier, 2009.

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Landsteiner, Karl. The Specificity of Serological Reactions. Dover Publications, 1990.

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Ivanyi, Juraj, and Tom H. M. Ottenhoff, eds. Significance of antigen and epitope specificity in tuberculosis. Frontiers SA Media, 2015. http://dx.doi.org/10.3389/978-2-88919-451-3.

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Book chapters on the topic "Antigen specificity"

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Band, H., St A. Porcelli, G. Panchamoorthy, J. Mclean, C. T. Morita, S. Ishikawa, R. L. Modlin, and M. B. Brenner. "Antigens and Antigen-Presenting Molecules for γδ T Cells." In Function and Specificity of γ/δ T Cells, 229–34. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76492-9_32.

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Morris, Emma C., and J. H. F. Falkenburg. "What Defines a Good Tumour Antigen?" In The EBMT/EHA CAR-T Cell Handbook, 11–14. Cham: Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-030-94353-0_3.

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AbstractCompared to standard anticancer therapies, such as chemotherapy, small molecule inhibitors and radiation, T cell immunotherapies have the advantages of a high degree of specificity and durability of response typically associated with cellular therapies. The functional specificity of a T cell is determined by its antigen recognition receptor and the target antigen (Bjorkman et al. 1987; Garcia et al. 1996).
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Lund, Ole, Edita Karosiene, Claus Lundegaard, Mette Voldby Larsen, and Morten Nielsen. "Bioinformatics Identification of Antigenic Peptide: Predicting the Specificity of Major MHC Class I and II Pathway Players." In Antigen Processing, 247–60. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-62703-218-6_19.

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Wang, Chunlin, Huang Huang, and Mark M. Davis. "Grouping T-Cell Antigen Receptors by Specificity." In Methods in Molecular Biology, 291–307. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2712-9_15.

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Van Regenmortel, Marc H. V. "Specificity, Polyspecificity and Heterospecificity of Antibody-Antigen Recognition." In HIV/AIDS: Immunochemistry, Reductionism and Vaccine Design, 39–56. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-32459-9_4.

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Dent, A. L., and S. M. Hedrick. "Mechanisms of Development of αβ T Cell Antigen Receptor-Bearing Cells in γδ T Cell Antigen Receptor Transgenic Mice." In Function and Specificity of γ/δ T Cells, 121–31. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76492-9_17.

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De Libero, G., G. Casorati, N. Migone, and A. Lanzavecchia. "Correlation Between TCRV Gene Usage and Antigen Specificities in Human γδ T Cells." In Function and Specificity of γ/δ T Cells, 235–38. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76492-9_33.

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Powell, Daniel J., and Bruce L. Levine. "Genetically Engineered Antigen Specificity in T Cells for Adoptive Immunotherapy." In Experimental and Applied Immunotherapy, 251–78. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-980-2_12.

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Holoshitz, J., N. K. Bayne, D. R. McKinley, and Y. Jia. "A Dichotomy Between the Cytolytic Activity and Antigen-Induced Proliferative Response of Human γδ T Cells." In Function and Specificity of γ/δ T Cells, 167–72. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76492-9_22.

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Lefrancois, L., R. LeCorre, Judy Mayo, J. A. Bluestone, and T. Goodman. "Selection of Vδ+ T Cell Receptors of Intestinal Intraepithelial Lymphocytes is Dependent on Class II Histocompatibility Antigen Expression." In Function and Specificity of γ/δ T Cells, 255–67. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76492-9_36.

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Conference papers on the topic "Antigen specificity"

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Kleist, Sierra, Shawn Musial, Hanna Degefu, Pamela Rosato, and Jordan Isaacs. "1032 Uncoupling CD39 and T cell antigen specificity in brain tumors." In SITC 37th Annual Meeting (SITC 2022) Abstracts. BMJ Publishing Group Ltd, 2022. http://dx.doi.org/10.1136/jitc-2022-sitc2022.1032.

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Park, Seungtae, Sungsik Kim, Hee Joon Jeon, Na Ri Yoon, Bo Ryeong Lee, Sung-min Kim, Woong-Yang Park, and Hyung Ju Hwang. "74 DeepTCRMatch: An effective way of computing T cells antigen specificity." In SITC 37th Annual Meeting (SITC 2022) Abstracts. BMJ Publishing Group Ltd, 2022. http://dx.doi.org/10.1136/jitc-2022-sitc2022.0074.

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Chen, Liang, Chunlin Wang, and Mark Davis. "Abstract PR14: Identification of specificity TCR groups of tumor antigen specific T-cells." In Abstracts: Fourth CRI-CIMT-EATI-AACR International Cancer Immunotherapy Conference: Translating Science into Survival; September 30 - October 3, 2018; New York, NY. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/2326-6074.cricimteatiaacr18-pr14.

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Santoso, S., Y. Shibata, V. Kiefel, and C. Mueller-Eckhardt. "IDENTIFICATION OF YUK(b) ALLOANTIGEN ON PLATELET GLYCOPROTEIN IIIa*." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643528.

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Neonatal alloimmune thrombocytopenic purpura (NATP) is caused by IgG platelet alloantibodies (ab), produced by the mother and directed against antigens present on the platelets of the child. The specificity of the platelet-specific ab is anti-Pl(Al) in the majority of cases. Other specificities, i.e. anti-Pl(E2), anti-Bak(a), anti-Pen, and anti-Pl(A2) have also been found. Recently, Shibata et al (1986) have described a new platelet antigen system Yuk(a)/Yuk(b) involved in NATP. The Yuk(a) and Yuk(b) antigens are not expressed on thromb-asthenic platelets indicating that these antigens do exiŞt on glycoprotein (GP) lib and/or Ilia. In order to investigate the molecular localization of these antigens, we studied the interaction of anti-Yuk(b) purified ab with membrane components of platelets using immunoblot procedure and compared their immunochemical behaviour with that of other platelet specific ab (anti-Pl(A 1), -Lek(a), -Bak(a)).In the absence of disulfide reduction Yuk(b) ab reacted with an antigen of molecular weight (mol wt) 92 kDa with an electrophoretic mobility identical to GP Ilia. An identical result was obtained for P1(A1) ab. In contrast, the Bak(a) ab as well as Lek(a) ab detected an antigen of mol wt 134 kDa which comigrated with GP lib. After reduction with 2-mercaptoethanol binding of anti-Pi(Al) and anti-Yuk(b) was not observed. To further localize the Yuk(b) antigen on GP Ilia, immunoblotting experiments were performed with anti-Pl(Al) and anti-Yuk(b) of chymotrypsin treated platelets. While anti-Pl(Al) bound to GP IIIa and a 68 kDa component, anti-Yuk(b) bound only to GP IIIa when the platelets had been treated for 45 min with chymotrypsin.This discrepancy became even more pronounced by prolonged treatment of platelets (225 min) in that the reactivity of anti-Yuk(b) was entirely abolished, whereas binding of anti-Pl(Al) shifted completely from the 92 kDa to the 68 kDa component. Thus, unlike the P1(A1) antigen, the Yuk(b) determinant either resides on the 30 kDa fragment of GP Ilia or it is destroyed by chymotrypsin treatment.
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Silveira, A. M. V., B. Hessel, and B. Blombäck. "VON WILLEBRAND FACTOR (VWF) ANTIGENS IN URINE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644083.

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Human urine was analyzed using a sensitive enzyme linked immunosorbent assay (ELISA) for von Willebrand factor (VWF) antigen. Urine of healthy persons contained VWF immunoreactivity. In the urine of a patient with severe von Willebrand disease, the VWF antigen was only detectable after intravenous infusion of VWF-Factor VIII concentrate. The VWF antigen in normal urine was analyzed by gel permeation high performance liquid chromatography (HPLC) and gel electrophoresis combined with immunoblotting. These analyses revealed three immunoreactive components of Mr 350 kDa, 60 kDa, and 20 kDa, respectively, the 60 kDa being the major component. Monoclonal antibodies of known specificity to VWF molecule were used in ELISA and immunoblotting to analyze urinary VWF. The three components reacted with an antibody to the central part of VWF, which is called fragment I, and contains the binding site for collagen. No significant immunoreac-tion was observed with monoclonal antibodies to the Nor C-terminal portions of VWF.VWF derivatives of molecular size similar to the largest urinary antigens were also observed in normal plasma. However, there is not an obvious relationship between these plasma forms and the products in urine since reduction of plasma and urine yields different products.These results indicate that VWF antigens excreted in normal urine are most likely fragments of VWF produced by limited degradation in vivo. This degradation preserves the central part of VWF molecule, the one which reacts with the antibody that blocks the binding of VWF to collagen.
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Fisher, Jonathan, anna capsomidis, Barry Flutter, Gabriel Benthal, Rebcca Wallace, Kenth Gustafsson, Karin Straathof, Martin Pule, and John Anderson. "Abstract B128: Chimeric antigen receptor transduced gamma delta T lymphocytes provide enhanced tumor specificity." In Abstracts: CRI-CIMT-EATI-AACR Inaugural International Cancer Immunotherapy Conference: Translating Science into Survival; September 16-19, 2015; New York, NY. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/2326-6074.cricimteatiaacr15-b128.

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Adams, Gregor B., Jun Feng, Atefeh Ghogha, Armen Mardiros, Ruben Rodriguez, Tassja J. Spindler, Jed Wiltzius, and Tony Polverino. "Abstract 2135: Selectivity and specificity of engineered T cells expressing KITE-585, a chimeric antigen receptor targeting B-cell maturation antigen (BCMA)." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-2135.

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Schirmer, David, Richard Klar, Oxana Schmidt, Dirk Wohlleber, Wolfgang Uckert, Uwe Thiel, Felix Bohne, et al. "Abstract 3202: Transgenic antigen-specific, HLA-A*02:01-allo-restricted cytotoxic T cells recognize tumor-associated target antigen STEAP1 with high specificity." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-3202.

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Banerjee, Rupak K., Meinrad Praxmaraer, Ilhan Dilber, Peter Bungay, William van Osdol, and Cynthia Sung. "Numerical Simulation of Antibody Penetration in a Solid Tumor Nodule Using Finite Element Method." In ASME 1998 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 1998. http://dx.doi.org/10.1115/imece1998-0058.

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Abstract The high binding specificity that monoclonal antibodies exhibit has led to great interest in using them to target tumor-associated antigens. The antibody may be coupled to a radionuclide or cytotoxic drug to create a tumor-targeted reagent that can be used to identify sites of metastatic disease and/or deliver a lethal substance to the tumor cells. However, successful application of these compounds in a clinical setting has been hindered by a poor understanding of the factors that govern antibody accumulation in a tumor. We have used a finite element method to develop a pharmacokinetic model describing the uptake of systemically-administered antibody in an early, prevascular spherical tumor nodule embedded in normal tissue. The model incorporates such processes as plasma kinetics, transcapillary transport, interstitial diffusion, binding reactions, lymphatic clearance, and antigen internalization.
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Xiao, Yang, Yueshan Huang, Yu Zhao, Fan Xu, Qin Ren, Bing He, Jianhua Yao, and Xiao Liu. "Multimodal-AIR-BERT: A Multimodal Pre-trained Model for Antigen Specificity Prediction in Adaptive Immune Receptors." In 2023 IEEE International Conference on Bioinformatics and Biomedicine (BIBM). IEEE, 2023. http://dx.doi.org/10.1109/bibm58861.2023.10385479.

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Reports on the topic "Antigen specificity"

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Friedmann, Michael, Charles J. Arntzen, and Hugh S. Mason. Expression of ETEC Enterotoxin in Tomato Fruit and Development of a Prototype Transgenic Tomato for Dissemination as an Oral Vaccine in Developing Countries. United States Department of Agriculture, March 2003. http://dx.doi.org/10.32747/2003.7585203.bard.

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The broad objective of the project was to develop a feasible approach to combat diarrheal disease caused by ETEC through the development of a low-cost oral immunogen in tomato fruit, expressed in the context of a prototype tomato that would answer the shortcomings of plant oral vaccines, especially in terms of produce handling and control of gene escape. Specifically, the goals for Boyce Thompson Institute (BTI) on this project were to develop transgenic tomato lines that express the enterotoxigenic E. coli (ETEC) heat-labile enterotoxin (LT) subunits A and/or B for use in oral edible vaccines, and to optimize expression and assembly of these antigens in tomato fruits.LT-B is a useful vaccine antigen against ETEC disease, since antibodies against LT-B can prevent binding and delivery of the holotoxinLT. Mutant forms of the toxic LT-A subunit that have reduced toxicity can be co-expressed and assembled with LT-Bpentamers to form mutant LT (mLT) complexes that could be used as mucosaladjuvants for other oral vaccines. Work on the project is continuing at Arizona State University, after Dr. Mason moved there in August 2002. A number of approaches were taken to ensure the expression of both subunits and bring about their assembly inside the transgenic fruits. Initially, expression was driven by the fruit-specific E-8 promoter for LT-B and the constitutive CaMV 35S promoter for LT-A(K63). While LT-B accumulated up to 7 µg per gram ripe fruit, assembled LT-K63 was only 1 µg per gram. Since promoter activities for the two genes likely differed in cell type and developmental stage specificity, the ratios of A and B subunits was not optimal for efficient assembly in all cells. In order to maximize the chance of assembly of mLT in fruit, we focused on constructs in which both genes are driven by the same promoter. These included co-expression plasmids using the 35S promoter for both, while switching to attenuated mLTs (LT-R72 and LT-G192) that have shown greater potential for oral adjuvanticity than the initial LT-K63, and thus are better candidates for a plant-derived adjuvant. Other, more novel approaches were then attempted, including several new vectors using the tomato fruit-specific E8 promoter driving expression of both LT-B and mutant LT-A, as well as a dicistronic construct for co-expression of both LT-B and mutant LT-A genes from a single promoter, and a geminivirusreplicon construct. We describe in the Appendix the results obtained in transgenic tomato lines transformed with these constructs. Overall, each contributed to enhanced expression levels, but the assembly itself of the holotoxin to high levels was not observed in the fruit tissues. The Israeli lab’s specific objective was to develop transgenic tomato lines expressing the LTholotoxin antigen bearing attributes to prevent gene escape (male sterility and orange fruit color) and to improve the dissemination of the oral vaccine (long shelf-life tomato cherry fruit or tomato processing background). Breeding lines bearing a number of attributes to prevent gene escape were developed by combining material and backcrossing either to a tomato cherry background, or two different processing backgrounds. Concomitantly, (these lines can be utilized for the creation of any future oral vaccine or other therapeutic-expressing tomato, either by crosses or transformation), the lines were crossed to the holotoxin-expressing tomatoes received from the United States, and this transgenic material was also incorporated into the backcrossing programs. To date, we have finalized the preparation of the cherry tomato material, both non-transgenic (bearing all the desired attributes), and transgenic, expressing the holotoxin. The level of expression of LT-B in the cherry fruits was comparable to the original transgenic tomatoes. Since it was not higher, this would necessitate the consumption of more fruits to reach a desired dose. A final backcross has been made for both the non-transgenic and the transgenic material in the processing lines. Auxin sprays resulted in high percentages of fruit set, but the processing genotypes gave many puffed fruits.
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