Relevant bibliographies by topics / Epitope

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  2. Dissertations / Theses
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  4. Book chapters
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Academic literature on the topic 'Epitope'

Author: Grafiati
Published: 4 June 2021
Last updated: 6 July 2024

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Journal articles on the topic "Epitope"

1

Madhumathi, J., P. R. Prince, D. N. Rao, A. A. Karande, M. V. R. Reddy, and P. Kaliraj. "Epitope mapping ofBrugia malayiALT-2 and the development of a multi-epitope vaccine for lymphatic filariasis." Journal of Helminthology 91, no. 1 (February 19, 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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Singh, Niraj K., Anuj Tyagi, Sumit Singhal, Anjay, Yogendra Singh Jadoun, and Anuradha Kumari. "Bio-Computational Prediction of Novel Epitopes on VP2 Protein of Infectious Bursal Disease Virus." Journal of Advances in Microbiology 24, no. 5 (June 2, 2024): 26–39. http://dx.doi.org/10.9734/jamb/2024/v24i5824.

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Aim: Recently, many viral Immunogenic peptides or epitopes have been used as potential vaccine and also immuno-diagnostic candidates. In this study, we predicted different epitopic peptides on VP2 protein of infectious bursal disease virus (IBDV) using bioinformatics tools, which can be potential vaccine as well as diagnostic candidate for IBD, in future. Study Design: In the present study, B-cell epitopes (linear or continuous, and conformational) and T-cell epitopes were predicted on VP2 protein. Place and Duration of Study: Bihar Animal Sciences University, Patna, and Guru Angad Dev Veterinary and Animal Sciences University, Ludhiana, India between June and December 2023. Methodology: For the prediction of linear B-cell epitopes, Bepipred Linear Epitope Prediction 2.0, SVMTriP, and BCPred tools were used, while Ellipro was used for conformational B-cell epitopes prediction. In the absence of immune-bioinformatics tool is available to predict poultry MHC-peptide binding, only those human MHC-I/II alleles having greater than 70% identities those of poultry MHC-I/II alleles were selected. NetMHCcons 1.1 and NetMHCIIpan - 4.0 tools were used to predict strong binding affinity of peptides with MHC-I and MHC-II, respectively. Results: As per analysis by four different tools, the peptide ‘SYDLGYVRLGDPIPAIGLDPKMV ATCDSSDRPRVYTITAADDYQFSSQYQPGGV164-217’ (EpitopeL) was predicted as the most prominent linear B-cell epitope. Two peptides, i.e. ANLNSPLKIAG (EpitopeC 1) and SSQYQPGGRTSVHGLGLTTGTDKSGGQAGDQMS (EpitopeC 2) were predicted as potent conformational B-cell epitopes. During T-cell epitopes prediction, human HLA*B 40:06, HLA*B 41:03 and HLA*B 41:04 alleles chosen as homologues of poultry MHC class I alleles while DRB1:1310, DRB1:1366, DRB1:1445, and DRB1:1482 chosen as homologues of poultry MHC class II alleles. A 9-mer GELVFQTSV236-244 peptide was predicted as MHC-I strong binder ability while, two 15-mer peptides, i.e. YTKLILSERDRLGIK389-403 and QMLLTAQNLPASYNY76-90 were predicted as MHC-II strong binder ability. Conclusion: Using bio-computational analysis, one linear and two conformational B-cell epitopes were predicted on VP2 protein of IBDV. During T-cell epitopes prediction one 9-mer peptide and two 15-mer peptides were predicted as MHC-I and MHC-II strong binding peptides, respectively. After assessing protective immune responses through in vitro and in vivo studies, these predicted peptides could be potential candidates for developing subunit vaccines.
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Yuexi, Li, Wang Xingsheng, Xie Guangyan, Liao Jianming, Yin Dengke, Guan Wenyan, Pan Mingjie, and 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, no. 1_Supplement (April 1, 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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Grahadi, Rahmat, Fatchiyah Fatchiyah, and Nia Kurniawan. "Virtual prediction of potential immunogenic epitope of candoxin protein from Malayan krait (Bungarus candidus) venom." Journal of Pharmacy & Pharmacognosy Research 10, no. 6 (November 1, 2022): 1046–57. http://dx.doi.org/10.56499/jppres22.1469_10.6.1046.

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Context: Malayan krait (Bungarus candidus) is a snake that is considered highly venomous snake and widely distributed across Southeast Asia. Envenomation by this snake is characterized by facial weakness, paralysis, respiratory muscle weakness, and in most cases, it renders the victim dead. Unfortunately, there is only one antivenom for neutralizing venom that is only available from the Thai Red Cross Society. Aims: To predict the epitopes from candoxin protein of B. candidus venom that could be a candidate for vaccine-based antivenom. Methods: In this study, IEDB and SYFPHEITHI databases were utilized to predict candoxin epitope sequences and determine their immunogenicity, conservancy, and population coverage. Next, the epitopes were modeled, and the binding interactions between epitopes and MHC-II were analyzed. The epitope that binds into the active site of human and murine MHC-II proceeded to the next step. Then, the allergenic properties of the chosen epitope were assessed to ensure its safety. Lastly, the physicochemical characteristics prediction and molecular dynamics simulation were conducted to verify the epitope’s stability when produced in vivo. Results: The results showed that epitope 47-CFKESWREARGTRIE-61 has the best binding interaction when compared to others. This epitope was confirmed that did not show potential allergenic properties. The physicochemical properties and molecular dynamics simulation demonstrated that this epitope was stable. Conclusions: The results of this study will be useful in developing a novel antivenom for Bungarus candidus using a vaccine-based method.
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Zou, Wei, Roger Mackenzie, Lina Thérien, Tomoko Hirama, Qingling Yang, Margaret A. Gidney, and Harold J. Jennings. "Conformational Epitope of the Type III Group B Streptococcus Capsular Polysaccharide." Journal of Immunology 163, no. 2 (July 15, 1999): 820–25. http://dx.doi.org/10.4049/jimmunol.163.2.820.

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Abstract The protective epitope of the type III group B streptococcal polysaccharide (GBSPIII) is length dependent and conformational. To obtain a more accurate characterization of the conformational epitope, ELISA inhibition and surface plasmon resonance studies were conducted on two GBSPIII-specific mAbs using a large panel of oligosaccharide probes. The results of the studies confirmed that 2 repeating units (RU) is the minimum binding unit and that, while increases in chain length from 2 RU to 7 RU caused further optimization of the epitope, it remained monovalent. A 3-fold increase in affinity was observed between 7 RU and 20 RU, which, by surface plasmon resonance studies on a Fab, was shown to be due to both further optimization of the individual epitope and the occurrence of multivalency of epitope. The data support our hypothesis that the conformational epitope is an extended helical segment of the GBSPIII. GBSPIII exists mainly in the random coil form, which structurally mimics short oligosaccharide self Ags, but it can infrequently and spontaneously form extended helices. Although not prevalent in GBSPIII, the immune system preferentially selects these helical epitopes because they are unique to the polysaccharide. Contrary to a previously proposed model of GBSPIII binding in which the binding of the first Ab propagates a continuum of helical epitopes, our binding kinetics are consistent only with the helical epitope’s being discontinuous and infrequent.
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Potocnakova, Lenka, Mangesh Bhide, and Lucia Borszekova Pulzova. "An Introduction to B-Cell Epitope Mapping and In Silico Epitope Prediction." Journal of Immunology Research 2016 (2016): 1–11. http://dx.doi.org/10.1155/2016/6760830.

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Identification of B-cell epitopes is a fundamental step for development of epitope-based vaccines, therapeutic antibodies, and diagnostic tools. Epitope-based antibodies are currently the most promising class of biopharmaceuticals. In the last decade, in-depth in silico analysis and categorization of the experimentally identified epitopes stimulated development of algorithms for epitope prediction. Recently, various in silico tools are employed in attempts to predict B-cell epitopes based on sequence and/or structural data. The main objective of epitope identification is to replace an antigen in the immunization, antibody production, and serodiagnosis. The accurate identification of B-cell epitopes still presents major challenges for immunologists. Advances in B-cell epitope mapping and computational prediction have yielded molecular insights into the process of biorecognition and formation of antigen-antibody complex, which may help to localize B-cell epitopes more precisely. In this paper, we have comprehensively reviewed state-of-the-art experimental methods for B-cell epitope identification, existing databases for epitopes, and novel in silico resources and prediction tools available online. We have also elaborated new trends in the antibody-based epitope prediction. The aim of this review is to assist researchers in identification of B-cell epitopes.
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Mylin, Lawrence M. "Context-Dependent Immunogenicity of an S206G-Substituted H-2Db-Restricted Simian Virus 40 Large T Antigen Epitope I Variant." Journal of Immunology 162, no. 4 (February 15, 1999): 2171–79. http://dx.doi.org/10.4049/jimmunol.162.4.2171.

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Abstract SV40 large tumor Ag (Tag) contains four H-2b-restricted (I, II/III, IV, and V) CTL epitopes. A hierarchy exists among these CTL epitopes. CTL directed against epitopes I, II/III, and IV are readily detected following immunization of H-2b mice with SV40, Tag-transformed syngeneic cells, or a vaccinia recombinant that expresses full-length Tag, while epitope V-specific CTL are not. The mechanisms that define this hierarchy remain unknown. Initial studies have shown that the locations of epitopes I and V within SV40 Tag do not determine the immunological potencies of these epitopes. Like the wild-type Tag, derivatives in which the locations of epitopes I and V were precisely reversed within Tag failed to induce epitope V-specific CTL, but did induce epitope I-specific CTL. The use of an S206G-substituted epitope I variant (GAINNYAQKL) revealed that the S206G variant sequence induced CTL when located within the native epitope I context, but failed to do so when located within the epitope V context of Tag. Mutagenesis of residues adjacent to the S206G-substituted epitope I variant revealed that the identity of the residue flanking the amino terminus of the S206G variant was critical when it resided within the epitope V location, but not within the epitope I location. These results demonstrate that effects imposed by both regional context and adjacent residues can modulate immunogenicity, but that the relative importance of such effects varies in an epitope-dependent manner.
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Lucchese, Guglielmo, Angela Stufano, and Darja Kanduc. "Proposing Low-Similarity Peptide Vaccines againstMycobacterium tuberculosis." Journal of Biomedicine and Biotechnology 2010 (2010): 1–8. http://dx.doi.org/10.1155/2010/832341.

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Using the currently available proteome databases and based on the concept that a rare sequence is a potential epitope, epitopic sequences derived fromMycobacterium tuberculosiswere examined for similarity score to the proteins of the host in which the epitopes were defined. We found that: (i) most of the bacterial linear determinants had peptide fragment(s) that were rarely found in the host proteins and (ii) the relationship between low similarity and epitope definition appears potentially applicable to T-cell determinants. The data confirmed the hypothesis that low-sequence similarity shapes or determines the epitope definition at the molecular level and provides a potential tool for designing new approaches to prevent, diagnose, and treat tuberculosis and other infectious diseases.
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Tornyi, Ilona, Jozsef Lazar, Aladar Pettko-Szandtner, Eva Hunyadi-Gulyas, and Laszlo Takacs. "Epitomics: Analysis of Plasma C9 Epitope Heterogeneity in the Plasma of Lung Cancer Patients and Control Subjects." International Journal of Molecular Sciences 24, no. 18 (September 21, 2023): 14359. http://dx.doi.org/10.3390/ijms241814359.

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The human proteome is more complex than the genetic code predicts it to be. Epitomics, or protein epitome profiling, is a tool for understanding sub-protein level variation. With the ultimate goal to explore C9 proteoforms and their relevance to lung cancer, here we report plasma C9 epitope-associated molecular heterogeneity in plasma samples of lung cancer patients and control subjects. We show three C9 epitopes (BSI0449, BSI0581, BSI0639) with markedly different association with lung cancer (“unaltered”, “upregulated” and “downregulated”). In order to exclude confounding effects, we show first that the three epitope-defining mAbs recognize C9 in purified form and in the natural context, in the human plasma. Then, we present data demonstrating the lack of major epitope interdependence or overlap. The next experiments represent a quest toward the understanding of the molecular basis of apparent disparate association with lung cancer. Using immunochemistry, SDS PAGE and LC-MS/MS technologies, we demonstrate that epitope-specific immunoprecipitates of plasma C9 seem identical regarding peptide sequence. However, we found epitope-specific posttranslational modification and coprecipitated protein composition differences with respect to control and lung cancer plasma. Epitope profiling enabled the classification of hypothetical C9 proteoforms through differential association with lung cancer.
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Moriki, Takanori, Ichiro N. Maruyama, Yusuke Yamaguchi, Atsuko Igari, Yasuo Ikeda, and Mitsuru Murata. "Identification of ADAMTS13 Epitopes Required for Binding to von Willebrand Factor Using Lambda Phage Surface Display." Blood 110, no. 11 (November 16, 2007): 2707. http://dx.doi.org/10.1182/blood.v110.11.2707.2707.

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Abstract The metalloprotease ADAMTS13 cleaves multimeric von Willebrand factor (VWF) to regulate VWF-mediated thrombus formation. We planned to search core epitopes of ADAMTS13 that is required for its binding to VWF. We constructed a random cDNA fragment library expressing various peptides of ADAMTS13 on the surface of lambda phage and screened the library using immobilized VWF as a probe. After the first screening, the C-terminus of the spacer domain from Arg670 to Glu684 (termed as epitope-1) and the middle of the cysteine-rich domain from Arg484 to Arg507 (epitope-2) were determined as epitopes. When we added the synthetic epitope-1 peptide to the second screening, a new site, from Pro618 to Glu641 (epitope-3), was found in the middle of spacer domain. While the presence of synthetic epitope-2 peptide did not affect the subsequent screening, the presence of epitope-3 peptide enhanced the isolation of clones encoding epitope-1. These results suggest that ADAMTS13 epitopes-1, -2 and -3 may interact with each other for their binding to VWF. From screening in the presence of any combination or all of the three synthetic peptides, however, no new VWF binding site was uncovered. To examine the effect of divalent metal cations on the binding of ADAMTS13 epitopes to immobilized VWF, screening was carried out in the presence or absence of 5 mM of EDTA. No new epitope site was found. We next explored inhibitory effect of the synthetic epitope peptides on ADAMTS13 protease activity using recombinant ADAMTS13 and FRETS-VWF73 as a substrate. Synthetic epitopes-2 and -3 peptides markedly inhibited the cleavage of VWF by ADAMTS13, while the synthetic epitope-1 peptide did not as efficiently as epitopes-2 and -3. The stronger inhibitory effect of epitope-3 peptide than that of epitope-1 peptide was confirmed by SDS-agarose gel electrophoresis analysis of cleavage products of denatured multimeric VWF molecules by recombinant ADAMTS13. This was consistent with the dissociation constants for the three synthetic peptides with immobilized VWF determined by surface plasmon resonance, in which epitopes-2 and -3 have higher affinities for VWF than that of epitope-1. The results described above suggest that ADAMTS13 may initially bind to immobilized VWF through the sites of epitope-1 and epitope-2 with relatively weak affinity. The binding of epitope-1 to VWF may subsequently induce the conformational change of VWF, thereby exposing a binding site for epitope-3 for the efficient catalytic cleavage of VWF by ADAMTS13.
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Dissertations / Theses on the topic "Epitope"

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Lomas, Adrian John. "Poliovirus T cell epitope chimaeras." Thesis, University of Reading, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.318621.

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Perikala, Satish Kumar. "Evolution of Epitope regions in HIV genome: Delineating Selective Forces acting on Conformational and Linear Epitopes." [Kent, Ohio] : Kent State University, 2010. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=kent1270735952.

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Thesis (M.S.)--Kent State University, 2010.
Title from PDF t.p. (viewed Apr. 28, 2010). Advisor: Helen Piontkivska. Keywords: Conformational Epitopes; Linear Epitopes; HIV; Selective Forces; synonymous changes; nonsynonymous changes; Radical changes; Conservative changes. Includes bibliographical references (p. 81-96).
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Ruppert, Jörg. "Epitope-Tagging des humanen TSH-Rezeptors." [S.l.] : [s.n.], 2000. http://www.sub.uni-hamburg.de/disse/223/Disse.pdf.

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Elmgren, Lindsay Dorn. "Epitope mapping of lyssavirus structural proteins." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape7/PQDD_0014/NQ38783.pdf.

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Short, Andrew Keith. "Epitope mapping studies in systemic vaculitis." Thesis, University of Cambridge, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.338103.

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Zhu, Yunyi. "Epitope Mapping using Local Alignment Features." Thesis, KTH, Numerisk analys, NA, 2015. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-170658.

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Our immune system uses antibodies to neutralize pathogens such as bacteria and viruses. Antibodies bind to parts of foreign proteins with high efficiency and specificity. We call such parts epitopes. The identification of epitopes, namely epitope mapping, may contribute to various immunological applications such as vaccine design, antibody production and immunological diagnosis. Therefore, a fast and reliable method that can predict epitopes from the whole proteome is highly desirable.   In this work we have developed a computational method that predicts epitopes based on sequence information. We focus on using local alignment to extract features from peptides and classifying them using Support Vector Machine. We also propose two approaches to optimize the features. Results show that our method can reliably predict epitopes and significantly outperforms some most commonly used tools.
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Marsh, Steven George Edward. "Epitope mapping in major histocompatibility systems." Thesis, Open University, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.361587.

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Sheth-Ughade, Parita. "Immunological responses to fungal epitope peptides." Thesis, University of Manchester, 2012. https://www.research.manchester.ac.uk/portal/en/theses/immunological-responses-to-fungal-epitope-peptides(1f8234cb-77e4-4577-a6ba-e57d502048a4).html.

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Introduction: Fungi are common aeroallergens responsible for at least 3% – 10% of allergic diseases worldwide, with the proportion hugely variable in different populations. Treatment is complicated by viable nature and disease causing ability of the allergen and is often only palliative. Thus, this study aimed to serve as a pilot investigation to design novel anti-allergy therapeutics to cure allergy at the molecular level. It investigates the effect of wild type fungal peptides and corresponding variant peptides on allergy associated immunological responses – cellular and cytokine based – to use such variant peptides to cause the delicate shift from an allergic to a normal immune response. Further, the study explores the role of bioinformatics in investigating allergy and designing novel therapeutics. Methods: This study used ProPred, a bioinformatics software, to predict wild type peptides from selected allergens of Aspergillus fumigatus and Alternata alternaria for a target population. These were then modified to generate single amino acid variants. Both these peptide sets were tested to compare the cellular and cytokine patterns they generated in sensitised (n = 3) and healthy volunteers (n = 3) to check for anti-allergy responses that may be exerted by certain variants. The recruited population was also subjected to skin prick testing (SPT, n = 46) to check for co-sensitisations patterns and HLA typing (n = 40) to evaluate ProPred accuracy for peptide prediction. This study also attempted an in silico search for unknown Penicillium chrysogenum allergens by comparing known Penicillium and A. fumigatus allergens to identify probable agents of co-sensitization. Results: Of the wild type and variant peptides tested in this study, one variant peptide – peptide 1.1v from Asp f 2 – was successfully identified to change the cellular and cytokine profile to promote an anti-allergic response when compared to its corresponding wild type form (1.1o). This candidate is a good target for further investigation for use in peptide immunotherapy. Further, 8 shared allergens between A. fumigatus and P. chrysogenum were identified that may possibly be agents of co-sensitization between these species. SPT results indicated maximum subject co-sensitization between A. fumigatus and Candida albicans and P. chrysogenum. HLA typing results demonstrated the efficiency of ProPred to be 96.29%, thus implying that bioinformatics can effectively be used to study allergy in this novel manner. Conclusion: This study has demonstrated that variant peptides with a single amino acid change can cause the delicate shift from an allergic to a healthy immune response in sensitised subjects. This approach – in combination with other allergy associated factors such as epitope specificity for HLA types and inherent co-sensitization patterns in a population – can effectively be used to design peptide candidates for immunotherapy to target allergy at the molecular level. With promising results obtained in this pilot study, this approach guarantees further investigation in immunotherapy. This study has also demonstrated that bioinformatics can be effectively used to design and execute allergy studies in a targeted and inexpensive manner.
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EL-Manzalawy, Yasser. "Machine learning approaches for epitope prediction." [Ames, Iowa : Iowa State University], 2008.

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Forner, Mar 1980. "Multi-epitope peptide platforms for vaccine applications." Doctoral thesis, TDX (Tesis Doctorals en Xarxa), 2021. http://hdl.handle.net/10803/671028.

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Vaccination constitutes one of the most efficient and cost-effective methods of promoting global health. Nevertheless, few vaccines are fully effective, for manifold reasons ranging from intrinsic limitations to more contingent shortcomings related, e.g., to cold chain transport, handling and storage. In this context, peptide-based vaccines that consist of a fully synthetic approach mimicking B-and T-cell epitopes have emerged as an attractive alternative to overcome many such issues. Unfortunately, short peptides have generally been related to low immunogenicity and weak protection. In this thesis, we continue the progress towards the development of efficient peptide vaccines against foot-and-mouth disease (FMD) –a highly contagious viral disease of livestock that has a major economic impact. Particularly, the protective immune response under different conditions (dose, duration, different T-cell epitopes and novel candidates) is assessed in animal models. Moreover, we report the chemical synthesis of higher polyvalent peptide dendrimers using “click” chemistry methods of chemoselective ligation.
La vacunació constitueix un dels mètodes més eficients i rendibles per promoure la salut mundial. No obstant això, poques vacunes són plenament efectives, per diverses raons que van des de limitacions intrínseques a deficiències més contingents relacionades, per exemple, amb el transport, manipulació i/o emmagatzematge en cadena de fred. En aquest context, les vacunes basades en pèptids, que plantegen un enfocament totalment sintètic en la reproducció d’epítops de cèl·lules B i T, han sorgit com una alternativa atractiva per superar molts d’aquests problemes. Malauradament, els pèptids lineals i curts s’han relacionat generalment amb baixa immunogenicitat i baixa protecció. En aquesta tesi continuem avançant cap al desenvolupament de vacunes peptídiques eficaces contra la febre aftosa, una malaltia vírica del bestiar altament contagiosa i amb important impacte econòmic. En particular, hem avaluat la resposta immune sota diverses condicions (dosi, durada, diferents epítops de cèl·lules T i nous candidats) en models animals. A més, també hem desenvolupat la síntesi de pèptids multivalents utilitzant reaccions de lligament quimioselectiu amb la coneguda química “click”.
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Books on the topic "Epitope"

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Ulrich, Reineke, and Schutkowski Mike, eds. Epitope mapping protocols. 2nd ed. New York: Humana Press, 2009.

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Ulrich, Reineke, and Schutkowski Mike, eds. Epitope mapping protocols. 2nd ed. New York: Humana Press, 2009.

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R, Westwood Olwyn M., and Hay Frank C, eds. Epitope mapping: A practical approach. Oxford: Oxford University Press, 2001.

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Morris, Glenn E. Epitope Mapping Protocols. New Jersey: Humana Press, 1996. http://dx.doi.org/10.1385/0896033759.

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Schutkowski, Mike, and Ulrich Reineke, eds. Epitope Mapping Protocols. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-59745-450-6.

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Rockberg, Johan, and Johan Nilvebrant, eds. Epitope Mapping Protocols. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-7841-0.

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E, Morris Glenn, ed. Epitope mapping protocols. Totowa, N.J: Humana Press, 1996.

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M, Eibl Martha, and Mayr W. R. 1944-, eds. Epitope recognition since Landsteiner's discovery: 100 years since the discovery of human blood groups. Berlin: Springer, 2002.

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Al-Dughaym, Abdullah Mohammed. Epitope-mapping immunodominant antigens. Manchester: University of Manchester, 1995.

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Eibl, Martha, W. R. Mayr, and G. J. Thorbecke, eds. Epitope Recognition Since Landsteiner’s Discovery. Berlin, Heidelberg: Springer Berlin Heidelberg, 2002. http://dx.doi.org/10.1007/978-3-642-56340-9.

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Book chapters on the topic "Epitope"

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Dragun, Anthony E., Paul J. Schilling, Tod W. Speer, Feng-Ming Kong, Jingbo Wang, Hedvig Hricak, Oguz Akin, et al. "Epitope." In Encyclopedia of Radiation Oncology, 223. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-540-85516-3_674.

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Lefranc, Marie-Paule. "Epitope." In Encyclopedia of Systems Biology, 672–73. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4419-9863-7_663.

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Gooch, Jan W. "Epitope." In Encyclopedic Dictionary of Polymers, 891. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_13690.

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Morris, Glenn E. "Epitope Mapping." In Springer Protocols Handbooks, 683–96. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-60327-375-6_38.

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Morris, Glenn E. "Epitope Mapping." In Springer Protocols Handbooks, 619–30. Totowa, NJ: Humana Press, 1998. http://dx.doi.org/10.1007/978-1-59259-642-3_47.

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Morris, Glenn E. "Epitope Mapping." In Immunochemical Protocols, 161–72. Totowa, NJ: Humana Press, 1998. http://dx.doi.org/10.1007/978-1-59259-257-9_16.

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Ranganathan, Shoba. "PMHC Epitope." In Encyclopedia of Systems Biology, 1718–19. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4419-9863-7_915.

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Srinivasan, Ramachandran. "Linear Epitope." In Encyclopedia of Systems Biology, 1133. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4419-9863-7_952.

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Srinivasan, Ramachandran. "Discontinuous Epitope." In Encyclopedia of Systems Biology, 574. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4419-9863-7_962.

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Morris, Glenn E. "Epitope Mapping." In Immunochemical Protocols, 255–67. Totowa, NJ: Humana Press, 2005. http://dx.doi.org/10.1385/1-59259-873-0:255.

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Conference papers on the topic "Epitope"

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Wright, D., D. Cliffel, and A. Gerdon. "Nanocluster epitope presentation." In 2006 Bio Micro and Nanosystems Conference. IEEE, 2006. http://dx.doi.org/10.1109/bmn.2006.330893.

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Nafa, Fatema, and Ryan Kanoff. "Machine Learning based to Predict B-Cell Epitope Region Utilizing Protein Features." In 8th International Conference on Artificial Intelligence and Applications (AI 2022). Academy and Industry Research Collaboration Center (AIRCC), 2022. http://dx.doi.org/10.5121/csit.2022.121811.

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Considering the current state of Covid-19 pandemic, vaccine research and production is more important than ever. Antibodies recognize epitopes, which are immunogenic regions of antigen, in a very specific manner, to trigger an immune response. It is extremely difficult to predict such locations, yet they have substantial implications for complex humoral immunogenicity pathways. This paper presents a machine learning epitope prediction model. The research creates several models to test the accuracy of B-cell epitope prediction based solely on protein features. The goal is to establish a quantitative comparison of the accuracy of three machine learning models, XGBoost, CatBoost, and LightGbM. Our results found similar accuracy between the XGBoost and LightGbM models with the CatBoost model having the highest accuracy of 82%. Though this accuracy is not high enough to be considered reliable it does warrant further research on the subject.
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Solihah, Binti, Edi Winarko, Afiahayati, Sri Hartati, and Moh Edi Wibowo. "A systematic review: B-cell conformational epitope prediction from epitope characteristics view." In 2017 3rd International Conference on Science and Technology - Computer(ICST). IEEE, 2017. http://dx.doi.org/10.1109/icstc.2017.8011859.

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Cierniewski, C. S., and A. Z. Budzynski. "CONFORMATIONAL EQUILIBRIA IN THE γ CHAIN COOH-TERMINUS OF HUMAN FIBRINOGEN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642935.

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Synthetic peptides and fragments cleaved from native fibrinogen are used in studies to localize binding sites for various ligands. We addressed the question how the native conformation of a selected γ chain segment is affected by scission of the original chain. The conformation of the γ chain COOH-terminus of intact fibrinogen and its various fragments containing this region has been compared by an immunochemical analysis. An antibody population specific for the native epitope within the γ391-405 segment was isolated by affinity chromatography on the corresponding synthetic peptide. Between 19.2 and 22.8% of antibodies were obtained from three different antisera indicating that this region represents one of the major epitopes of native fibrinogen. Anti-γ391-405 antibodies were used to determine the value of Kconf the equilibrium constant for the interconversion of the non-native and native conformations of this epitope. The measurements were done using native fibrinogen, fragments D1 and DD, γ chain and γ391-405 synthetic peptide. In addition, the effect of 5 M guanidine-HCl on the conformation of fragments D1 and DD, which is known to abolish their antipolymerizing activity, was studied. Radioiodinated fibrinogen was used in the determination of Kconf, and quantitative analytical parameters, CI50% and CIs, calculated from competition between 125I-fibrinogen and the fibrinogen derivatives under study for binding to the immunochemically purified antibody. The measurements indicated that the epitope is unperturbed by iodination of fibrinogen and that 38.3% of fragment D1, 8.9% of fragment DD, 3.6% of the γ chain and less than 0.008% of the γ391-405 molecules adopt in aqueous solution the native conformation within the epitope. Denaturation of fragment D1 with 5 M guanidine-HCl affected only slightly the conformation of this γ chain determinant. More significant changes in the conformation were observed when fragment DD was denatured. The results suggest that long-range interactions are necessary for the stabilization of the native structure in the region of fibrinogen that interacts with the antibody and which is in close vicinity to the polymerization site, crosslinking site, and platelet recognition site.
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Lo, Ying Tsang, Tun Wen Pai, Hui Huang Hsu, and Huai Kuang Tsai. "Epitope and Paratope Region Analysis." In 2014 Eighth International Conference on Complex, Intelligent and Software Intensive Systems (CISIS). IEEE, 2014. http://dx.doi.org/10.1109/cisis.2014.73.

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Chumak, N. S., and Y. I. Melnikova. "OBTAINING AND IMMUNOCHEMICAL TESTING OF APOFERRITIN." In SAKHAROV READINGS 2022: ENVIRONMENTAL PROBLEMS OF THE XXI CENTURY. International Sakharov Environmental Institute of Belarusian State University, 2022. http://dx.doi.org/10.46646/sakh-2022-1-289-293.

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The process of direct binding of monoclonal antibodies to apoferritin immobilized on polystyrene, as well as the method of competitive interaction of monoclonal antibodies with apoferritin in solution, have been experimentally studied. It was found that the immobilization of apoferritin on a polystyrene surface leads to a change in the epitope structure of this protein and to the elimination of reactive epitopes of binding of monoclonal antibodies. The soluble form of apoferritin effectively binds to monoclonal antibodies in a competitive assay, which confirms the conformational nature of the clusters of determinants on the surface of apoferritin.
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Schwarz, Tatjana, Kirsten Heiss, Florian Kurth, Leif Sander, Clemens-Martin Wendtner, Manuela Hoechstetter, Marcel Müller, Christian Drosten, Volker Stadler, and Victor Corman. "Epitope signatures in COVID-19 patients." In International Symposium on Immunobiological. Instituto de Tecnologia em Imunobiológicos, 2021. http://dx.doi.org/10.35259/isi.2021_46633.

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Berndt, M. C., X. Du, L. Beutler, W. J. Booth, and P. A. Castaldi. "LOCALIZATION OF FUNCTIONAL DOMAINS ON HUMAN PLATELET GP Ib-IX COMPLEX BY EPITOPE ANALYSIS WITH MONOCLONAL ANTIBODIES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642923.

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There is now considerable evidence that glycoprotein (GP) Ib plays an important functional role in the von Willebrand factor (vWF)-dependent adhesion of platelets to exposed vascular subendothelium and in the a-thrombin activation of platelets, and that GP IX is important for quinine/quinidine drug-dependent antibody platelet recognition. GP Ib (Mr = 170 KD) consists of two disulfide-linked subunits, Iba (Mr = 135 KD) and Ibβ (Mr = 25 KD), and exists as a heterodimer complex with GP IX (Mr = 22 KD). In this study we have used a panel of 10 antiGP Ib-IX complex monoclonal antibodies to define the functional domains on this complex. Immunoprecipitation of trypsin-treated GP Ib-IX complex revealed that the monoclonal antibodies mapped into three distinct groups: FMC 25, AK 1 and SZ 1, epitopes on the membrane-associated fragment (GP IX and an ≃25 KD remnant of the α-chain disulfide linked to the β-chain); AK 3 and WM 23, epitopes on the central macroglycopeptide core (90 KD); AN 51, SZ 2, AK 2, AP 1 and HIP 1, epitopes on peptide tail (45 KD). Crossblocking studies indicated that with the exception of AK 1 and SZ 1, the monoclonal antibodies were directed against distinct epitopes. All five monoclonal antibodies directed against the peptide tail region blocked ristocetin-dependent vWF-platelet interaction whereas the other five monoclonal antibodies were without effect, indicating that the 45 KD peptide tail region at the plasma end of the α-chain of GP Ib contained the vWF binding domain. Similarly, only the three monoclonal antibodies directed against the membrane-associated region interfered with drug-dependent antibody-platelet interaction.By western blot analysis, α-thrombin bound to the 45 KD peptide tail region. However, only AP 1 interfered significantly with the α-thrombin-dependent aggregation of platelets. This panel of epitope-defined monoclonal antibodies should be of value in further defining the structure-function relationships of this important membrane complex.
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Kosaloglu, Zeynep, Inka Zoernig, Niels Halama, Eliana Ruggiero, Benedikt Brors, and Dirk Jaeger. "The epitope landscape of CRC liver metastases analyzed by whole-exome sequencing and in silico epitope prediction." In BCB '14: ACM-BCB '14. New York, NY, USA: ACM, 2014. http://dx.doi.org/10.1145/2649387.2660777.

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Frazier, D., Shu Wha Lin, J. Ware, Kenneth Smith, Howard Reisner, M. DeSerres, A. Wallmark, R. Ljung, I. M. Nilsson, and D. W. Stafford. "MAPPING OF 6 MONOCLONAL ANTIBODIES TO HUMAN FACTOR IX." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643565.

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In order to map the regions of human factor IX recognized by monoclonal antibodies we have inserted random fragments of the coding region of the cDNA for human factor IX into the lambda phage expression vector, lambda gtll. The resultant recombinant phage were screened with monoclonal antibodies, the immunoreactive phage were isolated, and the DNA of the inserted fragment was sequenced to determine which amino acids were immunoreactive. This data, coupled with data obtained from the use of specific fragments of human factor IX expressed in E. coli from a T7 phage promoter, has allowed us to map the location of several epitopes on the surface of the factor IX molecule. In those cases where the antibodies are specific for human factor IX, additional narrowing of the epitope is possible by comparing the amino acid sequence of human factor IX to the bovine molecule. Six monoclonal antibodies from 3 different laboratories have been mapped. The immunodominant epitopes appear to be the amino terminus of the activation peptide, the amino terminus of the heavy chain and the epidermal growth factor domains.
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Reports on the topic "Epitope"

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Gershoni, Jonathan M., David E. Swayne, Tal Pupko, Shimon Perk, Alexander Panshin, Avishai Lublin, and Natalia Golander. Discovery and reconstitution of cross-reactive vaccine targets for H5 and H9 avian influenza. United States Department of Agriculture, January 2015. http://dx.doi.org/10.32747/2015.7699854.bard.

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Research objectives: Identification of highly conserved B-cell epitopes common to either H5 or H9 subtypes of AI Reconstruction of conserved epitopes from (1) as recombinantimmunogens, and testing their suitability to be used as universal vaccine components by measuring their binding to Influenza vaccinated sera of birds Vaccination of chickens with reconstituted epitopes and evaluation of successful vaccination, clinical protection and viral replication Development of a platform to investigate the dynamics of immune response towards infection or an epitope based vaccine Estimate our ability to focus the immune response towards an epitope-based vaccine using the tool we have developed in (D) Summary: This study is a multi-disciplinary study of four-way collaboration; The SERPL, USDA, Kimron-Israel, and two groups at TAU with the purpose of evaluating the production and implementation of epitope based vaccines against avian influenza (AI). Systematic analysis of the influenza viral spike led to the production of a highly conserved epitope situated at the hinge of the HA antigen designated “cluster 300” (c300). This epitope consists of a total of 31 residues and was initially expressed as a fusion protein of the Protein 8 major protein of the bacteriophagefd. Two versions of the c300 were produced to correspond to the H5 and H9 antigens respectively as well as scrambled versions that were identical with regard to amino acid composition yet with varied linear sequence (these served as negative controls). The recombinantimmunogens were produced first as phage fusions and then subsequently as fusions with maltose binding protein (MBP) or glutathioneS-transferase (GST). The latter were used to immunize and boost chickens at SERPL and Kimron. Furthermore, vaccinated and control chickens were challenged with concordant influenza strains at Kimron and SEPRL. Polyclonal sera were obtained for further analyses at TAU and computational bioinformatics analyses in collaboration with Prof. Pupko. Moreover, the degree of protection afforded by the vaccination was determined. Unfortunately, no protection could be demonstrated. In parallel to the main theme of the study, the TAU team (Gershoni and Pupko) designed and developed a novel methodology for the systematic analysis of the antibody composition of polyclonal sera (Deep Panning) which is essential for the analyses of the humoral response towards vaccination and challenge. Deep Panning is currently being used to monitor the polyclonal sera derived from the vaccination studies conducted at the SEPRL and Kimron.
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Hunt, Donald F. Neurotoxin and Epitope Structural Studies. Fort Belvoir, VA: Defense Technical Information Center, January 1991. http://dx.doi.org/10.21236/ada233710.

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Ioannides, Constantin G. Epitope Specific T Cell Immunity to Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, June 2002. http://dx.doi.org/10.21236/ada414361.

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Ioannides, Constantin. Epitope Specific T Cell Immunity to Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, August 2000. http://dx.doi.org/10.21236/ada392776.

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Ioannides, Constantin G. Epitope Specific T-Cell Immunity to Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, August 1999. http://dx.doi.org/10.21236/ada381286.

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Moores, Lee C., P. U. Ashvin, I. Fernando, and Garret W. George. Synthesis of 2-Methoxypropyl Benzene for Epitope Imprinting. U.S. Army Engineer Research and Development Center, July 2022. http://dx.doi.org/10.21079/11681/44883.

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Harmful algal blooms (HABs) are occurring with increasing frequency and severity across the globe in part due to climate change and anthropogenic pollution (Bullerjahn et al. 2016). HABs produce several classes of toxins; however, microcystins (MCs) are the most commonly studied (Lone et al. 2015) and can be potent toxins with LD50s in the range of 50 μg/kg (Puddick et al. 2014). Sample analysis in laboratories, typically by high-pressure liquid chromatography tandem mass spectrometry (HPLC-MS/MS) or by Enzyme Linked Immunosorbent Assays (ELISAs) (USEPA 2015). These analytical techniques are highly sensitive and selective for the given toxins; however, the time it takes to collect, transfer, prepare, and analyze a sample before the data can be reported is significant; often, multiple days is the most expeditious.
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Lopez Bautista, Cesar. Large scale MD to predict Epitope regions in HIV Env. Office of Scientific and Technical Information (OSTI), January 2022. http://dx.doi.org/10.2172/1841887.

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Kiertscher, Sylvia M. The Advantages of Multi-Epitope Tumor Antigens as an Approach to Treating Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, July 2001. http://dx.doi.org/10.21236/ada398108.

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Sette, Alesandro, Bjoern Peters, and Martin Blythe. Predicting the Interplay of Epitope Recognition and Evolution in RNA Viruses Under Immune Pressure. Fort Belvoir, VA: Defense Technical Information Center, April 2008. http://dx.doi.org/10.21236/ada500852.

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Kiertscher, Syvia M. The Advantages of Multi-Epitope Tumor Antigens as an Approach to Treating Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, July 2002. http://dx.doi.org/10.21236/ada407499.

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