Dissertations / Theses on the topic 'Antibody recognition'
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Bristow, Richard G. W. "Antibody recognition of HIV-1 glycoproteins." Thesis, Open University, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.315370.
Full textDavies, Julian. "Antibody VH domains as small recognition units." Thesis, University of Cambridge, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.263483.
Full textRobakiewicz, Stefania. "Minimal structural glyco-epitope for antibody recognition." Thesis, Lille 1, 2020. http://www.theses.fr/2020LIL1S101.
Full textThe biological importance of glycosylation in health and disease is broadly acknowledged. The truncated, mannose-terminating structures consisting of 1–3 mannose residues, two N-acetylglucosamines, and a variable number of fucose moieties are termed paucimannose. Paucimannosidic N-glycans are abundantly expressed in plants and invertebrates. However, in vertebrates their presence is restricted to some pathophysiological conditions, such as cancer, immune disorders, infections, and inflammation, and in healthy individuals, they are detectable only in trace amounts. Mannitou, a murine monoclonal antibody, has been demonstrated to specifically recognise paucimannose glycoepitopes. An attempt to characterise Mannitou IgM structure was made by applying homology modelling, cryo-electron microscopy, and crystallisation techniques. Full-length Mannitou antibody has been generated using hybridoma technology. Recombinant Mannitou Fab has been successfully transiently expressed in HEK293T cells. The binding specificity of Mannitou towards different paucimannose N-glycans have been unravelled by a combination of experimental methods. The microarray screening revealed the minimal glyco-epitope to be Man2GlcNAc2. In turn, Man3GlcNAc2 manifested one of the strongest interactions with Mannitou antibody. Molecular recognition studies, employing surface plasmon resonance measurements and isothermal titration calorimetry, established a micromolar binding affinity of Manniotu antibody towards Man3GlcNAc2 glycan (Kd = ~50 μM). The mapping of the binding epitope by saturation transfer difference nuclear magnetic resonance demonstrated Manα1-3 as the main residue involved in Mannitou antibody recognition. The upregulation of paucimannosidic N-glycans in pathophysiological conditions makes Mannitou antibody a promising diagnostic and therapeutic tool.For determining the minimal carbohydrate structure required for mimicking the antigenic activity of the native MenX polysaccharide, surface plasmon resonance studies were performed. The experiments involved studying the binding interactions between an anti-MenX antibody and Neisseria meningitides serogroup X capsular oligosaccharides of different length. The results suggest that the minimal saccharide portion capable of ensuring protection against MenX infections may be DP5, making it a promising candidate for vaccine development
Scherer, Erin M. "Antibody recognition of a protein epitope close to a membrane : a novel solution." Thesis, University of Oxford, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.510216.
Full textWebster, Duncan F. "Characterisation of human hepatic cytochrome P450 : comparison of metabolic markers and antibody recognition." Thesis, University of Aberdeen, 1997. http://digitool.abdn.ac.uk/R?func=search-advanced-go&find_code1=WSN&request1=AAIU530008.
Full textRaina, Monika. "Development of an impedimetric biosensor using a non-antibody based biological recognition molecule." Thesis, University of Leeds, 2013. http://etheses.whiterose.ac.uk/6844/.
Full textTopping, Katherine P. "Structural studies on serotype-specific opsonic antibody recognition of protective streptococcal M protein epitopes." Thesis, University of Newcastle Upon Tyne, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.294877.
Full textKoh, W. W. L. "Characterisation of subtype C HIV-I envelope glycoproteins and their recognition by llama antibody fragments." Thesis, University College London (University of London), 2009. http://discovery.ucl.ac.uk/18999/.
Full textNaqid, Ibrahim. "Investigation of antibody-based immune recognition of infections with Salmonella enterica serovars Typhimurium and Enteritidis." Thesis, University of Nottingham, 2016. http://eprints.nottingham.ac.uk/33141/.
Full textGrinstead, Jeffrey Scott. "Structural immunology of humoral and cellular recognition of a MUC1 breast cancer antigen /." Thesis, Connect to this title online; UW restricted, 2003. http://hdl.handle.net/1773/8180.
Full textTing, Joy Holtvluwer. "Molecular ecology of mate recognition in the harpacticoid copepod Tigriopus : antibody production, protein purification, and fitness consequences." Diss., Georgia Institute of Technology, 2001. http://hdl.handle.net/1853/25202.
Full textWang, Hongsheng. "Natural antibody recognition, signaling and surveillance in v-Ha-ras- and PKC-ß1-overexpressing 10T1/2 fibroblasts." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk2/tape17/PQDD_0003/NQ32033.pdf.
Full textMadigan, Judith. "Antibody and T-Cell recognition of MHC- and mimicking tissue-peptides in autoimmune disease, particularly ankylosing spondylitis." Thesis, King's College London (University of London), 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.444151.
Full textAl, Qaraghuli Mohammed. "Investigating the antibody recognition of different hapten classes using a combination of phage display and protein modelling." Thesis, University of Aberdeen, 2014. http://digitool.abdn.ac.uk:80/webclient/DeliveryManager?pid=214816.
Full textEaston, Donna Meredith, and n/a. "Functional and Antigenic Characterisation of the Moraxella catarrhalis protein M35." University of Canberra. n/a, 2008. http://erl.canberra.edu.au./public/adt-AUC20081217.083105.
Full textRogers, Todd H. "Receptor recognition and response of dendritic cells to biomaterials." Diss., Georgia Institute of Technology, 2010. http://hdl.handle.net/1853/37107.
Full textWriter, Michele. "Molecular analysis of the recognition of the tumour associated antigen CD55 by the mouse monoclonal antibody 791T/36." Thesis, University of Nottingham, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.342476.
Full textMeng, Guangxun. "Cellular recognition of microbial patterns through toll-like receptor (TLR) 2 analysis of molecular requirements and monoclonal antibody mediated blockage /." [S.l.] : [s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=973389672.
Full textDiestel, Uschi [Verfasser], and Yves A. [Akademischer Betreuer] Muller. "Structural Basis for TGF-β-Receptor Interaction and Antibody Recognition of HCMV Envelope Protein gB / Uschi Diestel. Gutachter: Yves A. Muller." Erlangen : Friedrich-Alexander-Universität Erlangen-Nürnberg (FAU), 2014. http://d-nb.info/1075832683/34.
Full textOtali, Dennis. "The combined effect of formalin fixation and individual steps in tissue processing on immunorecognition." Birmingham, Ala. : University of Alabama at Birmingham, 2007. https://www.mhsl.uab.edu/dt/2008r/otali.pdf.
Full textPanagiotopoulou, Maria. "Organic-inorganic composite materials for specific recognition and optical detection of environmental, food and biomedical analytes." Thesis, Compiègne, 2016. http://www.theses.fr/2016COMP2315/document.
Full textThis thesis describes the state of the art in nanomaterials-based targeted bioimaging and introduces molecularly imprinted polymers, also termed ‘plastic antibodies’ as novel biorecognition agents for labeling and imaging of cells and tissues. In fundamental biology and medical diagnostics, there is a constant need to localize and quantify specific molecular targets. Abnormal glycosylation levels or distributions of hyaluronan or sialic acids on cells are indicators of infection or malignancy. In general, bioimaging with fluorescent probes enables the localization and qualitative or quantitative determination of these pathological biomarkers. However, no reliable tools for the recognition of glycosylation sites on proteins exist, because the commercially available antibodies or lectins have poor affinity and selectivity for these targets. In this context, tailor-made molecularly imprinted polymers (MIPs) are promising synthetic receptor materials since they present a series of advantages over their natural counterparts such as the ease and low cost of preparation and their physical and chemical stability. Thus, MIPs could provide a robust and specific imaging tool for revealing the location/distribution, time of appearance and structure of glycosylation sites on/in cells, which would lead to a better insight of the tremendously diverse biological processes in which these molecules are involved. Herein, we describe the synthesis of water-compatible MIPs for the molecular imaging of hyaluronan and sialylation sites on cells and tissues. Since molecular imprinting of entire biomacromolecules like oligosaccharides is challenging, we opted for what is commonly called the ‘epitope approach’, which was inspired by nature. The monosaccharides, glucuronic acid and N-acetylneuraminic acid were imprinted, and the resulting MIPs were able to bind these molecules when present and accessible on the terminal unit of hyaluronan and sialylation sites. Fluorescent MIPs were synthesized as rhodamine-labeled nanoparticles and as MIP-coated InP/ZnS core-shell quantum dot (QD) particles. For the coating of the QDs, a novel versatile solubilization and functionalization strategy was proposed, which consists of creating polymer shells directly on QDs by photopolymerization using the particles as individual internal light sources. A standard immunostaining protocol was then successfully adapted for the application of the fluorescently labeled MIPs to image fixed and living human keratinocytes and skin tissues, by epifluorescence and confocal fluorescence microscopy. The results were comparable to those obtained with a reference method where staining was done with a biotinylated hyaluronic acid binding protein. Multiplexed and cancer cell imaging were also performed, demonstrating the potential of molecularly imprinted polymers as a versatile biolabeling and bioimaging tool. Although the MIPs were not cytotoxic at the concentrations used for bioimaging, in order to render them generally applicable in biomedicine, where toxicity of the polymerization precursors is a matter of concern, we suppressed the initiator, a toxic chemical. Initiator-free MIPs were thus synthesized by using monomers that can self-initiate under UV irradiation or heat. The specificity and selectivity of the obtained MIPs were as good as the ones prepared with initiators. In conclusion, we have demonstrated for the first time the great potential of MIPs as synthetic antibody mimics for bioimaging. The possibility to associate other functionalities such as QDs and additionally attach drugs to the same material appears rather straightforward due to the synthetic polymeric nature of MIPs, which paves the way to new potential applications in theranostics
Joel, Smita. "ENGINEERING PROTEINS WITH UNIQUE CHARACTERISTICS FOR DIAGNOSTICS AND BIOSENSORS." UKnowledge, 2011. http://uknowledge.uky.edu/gradschool_diss/180.
Full textLamendour, Lucille. "Modulation des fonctions des cellules dendritiques humaines par des fragments d'anticorps." Thesis, Tours, 2018. http://www.theses.fr/2018TOUR3303/document.
Full textThe immune system protects an organism from the development of pathogens and actively participates in maintaining immune tolerance. Dendritic cells (DC) are specialized cells in the balance and anti-inflammatory immune response. DC play an important role in many pathological contexts, including organ transplantation, oncology and inflammatory diseases. Various factors, both intrinsic and extrinsic, can modulate. Because they are capable to inducing a tolerogenic response, these cells represent interesting targets for the immune response in the context of organ transplantation and in inflammatory pathologies. Some pathogens use mechanisms of escape to the immune system by promoting the induction of immune tolerance. This modulation is achieved by targeting the pathogen recognition receptors (PRRs) present on the surface of DC, inducing the synthesis of an anti-inflammatory cytokine IL-10, one of the main inducers of immune tolerance. Our strategy was to construct a bispecific antibody targeting two different PPRs from an anti-PRR antibody library. Our work shows that this bispecific antibody is able to direct the DC to a pro-tolerogenic profile. This bispecific antibody induces a semi-mature DC phenotype with a secretion profile of pro-tolerogenic cytokines such as IL-10 and few inflammatory cytokines. The immune tolerance profile of these DC remains to be explored. Our work opens interesting perspectives on the association of PRRs in order to obtain the modulation of the cells of the immunity
Martí, Fernández Iris [Verfasser], and Wolfang [Akademischer Betreuer] Enard. "Antibodies to myelin oligodendrocyte glycoprotein (MOG): Analysis of the impact of the glycosylation site of MOG for recognition of human autoantibodies and dissection of effector functions of the anti-MOG monoclonal antibody 8-18C5 / Iris Martí Fernández ; Betreuer: Wolfang Enard." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2020. http://d-nb.info/1227840047/34.
Full textBelot, Laura. "Etude structurale et fonctionnelle de la glycoprotéine des Rhabdovirus Structural basis for the recognition of LDL-receptor family members by VSV glycoprotein Structural and cellular biology of rhabdovirus entry Monomeric Intermediates Formed by Vesiculovirus Glycoprotein during Its Low-pH-induced Structural Transition." Thesis, Université Paris-Saclay (ComUE), 2019. http://www.theses.fr/2019SACLS522.
Full textRhabdoviruses are single stranded RNA enveloped viruses. They own a unique glycoprotein G anchored on the viral membrane. G is involved in the early stages of the viral cycle. At first G binds a cellular receptor, leading to the virus endocytosis. Then G orchestrates the membrane fusion between the viral and endosomal membranes. Membrane fusion allows the release of the viral genome into the cytoplasm of the infected cell.The low-density lipoprotein receptor (LDLR) is the main receptor of VSV. The ectodomain of the LDLR is composed of a large ligand binding domain constituted of cysteine-rich domains (CR1 to CR7).In order to understand the molecular basis of the interaction between G and its receptor, we performed binding test of G with all the CR domains of the LDLR. This revealed that only CR2 and CR3 domains could bind G. When CR2 and CR3 are present in the VSV inoculum, they protect the cells from VSV infection. We crystallized G in complex with each of these CR domains. The structures reveal that CR2 and CR3 binding sites on G are identical, and that the same residues on G are involved in the binding of the two CR domains. HAP-1 cells in which the gene encoding the LDLR has been invalidated are still susceptible to VSV infection. This confirms that VSV can use other receptors than the LDLR itself to enter the cells. However, mutation of G residues that are key in the interaction with the CR domains of the LDLR abolish the infectivity of VSV in mammalian and insect cells. This indicates that the only VSV receptors in these cells are members of the LDLR family and that VSV G has specifically evolved to interact with their CR domains. Moreover, we have shown that G mutated for key residues involved in the interaction with CR domains, are still able to induce fusion. This work shows that receptor recognition and G fusion activities can be decoupled. This paves the way to develop glycoproteins derived from G with modified tropism.In Rhabdoviruses, G is the only target of neutralizing antibodies. There is no structure of a Rhabdovirus G in complex with an antibody. The 8G5F11 antibody neutralizes several genotypes of the genus Vesiculovirus including VSV. We have shown that FAB 8G5F11 prevents infection of cells by VSV Indiana on the one hand and that they recognize the pre- and post-fusion form of VSV G with a 1: 1 G: FAB stoichiometry on the other hand. We have developed the observation conditions of the G-FAB complex in cryo-electron microscopy, which could be useful to obtain the structure of the G-FAB complex.We also started a study to characterize the glycoproteins of other Rhabdoviruses of the Lyssavirus genus. We produced and purified G ectodomains of rabies virus (RABV), Mokola virus (MOKV) and West Caucasian bat virus (WCBV). We characterize these G by electron microscopy at different pHs. The measurements made on G at pH 8 are compatible with those expected for a pre-fusion monomer of G. At pH 6, these ectodomains could correspond to a monomeric late intermediate in the structural transition. Obtaining the crystallographic structure of the G ectodomain of MOKV could validate these results
Chauvet, Margaux. "Étude de la modulation, par l'hémoglobine S, de la présentation des antigènes plasmodiaux à la surface du globule rouge infecté par Plasmodium falciparum, et de la réponse immunitaire contre le paludisme Impact of hemoglobin S trait on cell surface antibody recognition of Plasmodium falciparum infected erythrocytes in pregnancy-associated malaria." Thesis, Sorbonne Paris Cité, 2019. http://www.theses.fr/2019USPCB037.
Full textMalaria is a tropical disease resulting from infection by the parasite Plasmodium falciparum transmitted by mosquito bite. The symptoms of malaria are caused by the development of P. falciparum in red blood cells (RBCs). For centuries, malaria has put pressure on the human genome, having selected mutations conferring protection against severe forms of the disease. This is the case of the mutation of the hemoglobin gene (HbA), the principal constituent of RBCs. The mutated form of the gene produces abnormal hemoglobin (HbS). In contrast to sickle cell disease (HbSS), the heterozygous carriage (sickle cell trait) of this mutation (HbAS) is asymptomatic. Healthy HbAS carriers are protected from severe symptoms of malaria. Today, the mechanisms responsible for this protection remain partially understood. During its intra-erythrocytic development, P. falciparum modifies the RBC membrane and cytoskeleton to expose parasite proteins at the surface of the erythrocyte. Among these proteins, the major parasitic adhesin, "P. falciparum erythrocyte membrane protein 1" (PfEMP1), binds to endothelial receptors, resulting in cytoadherence and sequestration of infected RBCs. This cytoadherence permits the infected RBCs to avoid splenic clearance. Studies have shown that infected HbAS RBCs have a reduced cytoadherence, in association with an abnormal PfEMP1 display. This PhD project attempts to decipher the mechanisms of resistance conferred by the sickle cell trait against P. falciparum malaria. The first part of this project considers the phosphoproteome of the infected HbAA and HbAS red cell membranes. Parasitic proteins exposed on the surface of RBCs interact with erythrocyte proteins involved in the anchorage of the cytoskeleton to the erythrocyte membrane. These human proteins belong to the Ankyrin-R and the junctional complexes. The oxidative stress generated by sickle cell trait, and by parasite invasion, disrupts the kinase / phosphatase balance, leading to modulation of protein phosphorylation. As protein interactions could be regulated by their state of phosphorylation, this modulation may interfere in parasite antigens' display. Thus, protein membrane extracts of infected HbAA and HbAS RBCs were produced and analyzed by mass spectrometry and Western-Blot. This study showed that the sickle cell trait modulated the phosphorylation of erythrocyte proteins of the infected RBCs (membrane transporters and cytoskeletal proteins mainly), but also that of parasite proteins. The second part of the project deals with the anti-VAR2CSA antibody response in the context of pregnancy-associated malaria according to the heterozygous carriage of hemoglobin S. Placental malaria is one of the severe forms of malaria, resulting from the cytoadherence of infected RBCs in the placenta. This cytoadherence results from the interaction of a particular PfEMP1, VAR2CSA, with chondroitin sulfate A expressed on syncytiotrophoblasts. 159 plasma samples of HbAA and HbAS Beninese women, collected at delivery, were used to measure their ability to recognize VAR2CSA on the surface of infected HbAA and HbAS RBCs. Immune recognition of infected HbAS RBCs by plasma from HbAS mothers is significantly lower than the immune recognition of infected HbAA RBCs by HbAA mothers' plasma. In addition, other genetic diseases affecting RBCs may influence the antibody response to parasitized red blood cells. Co-carriage of G6PD deficiency and alpha-thalassemia with HbS were assessed for this study group. G6PD deficiency and alpha-thalassemia were present in, respectively, 26.7% and 51.7% of the women. These data underline the importance of simultaneously considering the different erythrocyte disorders present at high prevalence among the population considered, in order to study the protective mechanisms conferred by the carriage of HbS against malaria
Santoro, Lyse. "Appretement et présentation d'un anticorps monoclonal murin par une lignée monocytaire ou lymphocytaire B humaine : influence de la liaison covalente entre anticorps et fragment C3b du complément." Grenoble 1, 1994. http://www.theses.fr/1994GRE10126.
Full textParker, Matthew J. "Protein recognition of clinically-relevant carbohydrates." Thesis, 2015. http://hdl.handle.net/1828/6264.
Full textGraduate
mj3parker@gmail.com
Cobaugh, Christian Wessel 1971. "Single scaffold antibody libraries created with high rates of mutagenesis or diversity focused for peptide recognition." 2007. http://hdl.handle.net/2152/15990.
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Wolf, Cornel [Verfasser]. "Structured antibody surfaces for bio-recognition and a label-free detection of bacteria / Cornel Wolf." 2010. http://d-nb.info/1009999826/34.
Full textAgnew, Heather Dawn. "Rapid Construction of Protein Capture Agents with Chemically Designed Stability and Antibody-Like Recognition Properties." Thesis, 2010. https://thesis.library.caltech.edu/5583/11/Thesis.pdf.
Full textThis thesis describes technologies for the rapid and scalable production of high-affinity, high-specificity protein capture agents which possess the affinities and specificities of antibodies, but also exhibit improved chemical, biochemical, and physical stability. I will discuss how the chemical flexibility of comprehensive, one-bead-one-compound (OBOC) libraries of oligopeptides may be combined with iterative in situ click chemistry to select multi-ligand capture agents. Large OBOC libraries form the basis of individual peptide ligands, and also permit chemically designed stability through the incorporation of artificial (azide or acetylene) and non-natural amino acid building blocks. The in situ click chemistry method then utilizes the target protein as the catalyst, or template, for assembling its own biligand via formation of a 1,2,3-triazole linkage between two individual ligands (azide and acetylene). This process can be repeated to produce triligands, tetraligands, and other higher-order multi-ligands with an accompanying increase in affinity and specificity through cooperative interactions. Once found, multi-ligand capture agents can be produced in gram amounts via conventional synthetic methods such as the Cu(I)-catalyzed azide-alkyne cycloaddition (CuAAC). This is a general and robust strategy for the inexpensive, high-throughput construction of protein capture agents that can be exploited to detect protein biomarkers in multi-parameter clinical diagnostic assays.
While high-affinity protein capture agents represent a significant technology advance, they are just one component of what is necessary for highly multiplexed measurements of protein biomarkers. It is also important to develop or optimize the actual assay platforms that can enable sensitive multi-parameter protein measurements using these capture agents. Silicon nanowire (SiNW) nanoelectronic sensors can provide quantitative, label-free multi-parameter measurements of protein biomarkers in real time. However, SiNW sensors can be challenging to deploy because unprotected Si forms a native oxide layer that can significantly reduce the detection sensitivity of the nanowire sensors via dielectric shielding. Another technical challenge is the development of chemistries which allow for the selective encoding of nanowire surfaces with the capture agents. To overcome these challenges, the final part of this thesis presents a general method to functionalize organic and biological molecules on highly passivated Si(111) surfaces with minimal surface oxidation.
Yu-Ming, Wang. "Specific Recognition Force, Dissociation and Thermodynamics of Single-pair Antibody-Antigen Interaction Using Atomic Force Microscopy." 2006. http://www.cetd.com.tw/ec/thesisdetail.aspx?etdun=U0001-1110200612471100.
Full textWang, Yu-Ming, and 王裕銘. "Specific Recognition Force, Dissociation and Thermodynamics of Single-pair Antibody-Antigen Interaction Using Atomic Force Microscopy." Thesis, 2006. http://ndltd.ncl.edu.tw/handle/32594189490753914708.
Full text國立臺灣大學
應用力學研究所
95
Molecular recognition and intermolecular binding are essential for implementing many biochemical and biological processes in living organisms. To further understand the molecular binding mechanisms, this study used atomic force microscopy as a force-based senor for investigation of the force strength between antibody and antigen complex in a single pair level with varied physiological (pH and temperature) and physical (loading rate) conditions. The results provided direct evidence of unbinding force, dissociation rate and thermodynamic parameters that explained intermolecular behavior of human IgG1/anti-human IgG1 complex and glucagon/anti-glucagon IgG complexes, respectively. Mean measured forces of human IgG1 and its specific antibody system with pH-varied liquid environments showed a sharp decrease with a decrease of pH value (acidic environment), and a gradual decrease with an increase of pH value (alkaline environment) from a reference level at neutrality. This could have corresponded to the pH-induced change in conformational change and outer functional groups of amino acids which are protonated. As a result of change in pH environment of human IgG1/anti-human IgG1 complex, surface protonated properties and conformation weakened intermolecular force. Molecular dynamic behavior and free energy change were also contributed to a high probability of bonds breaking and a low magnitude of energy barrier when molecules were immersed in acidic or alkaline solution. Temperature-dependent unbinding force experiments were also carried out. The results showed that the unbinding forces decreased with an increase of environmental temperatures. This could be largely due to temperature-induced conformational change in volume expansion and strong Brownian motion. As a result, interaction forces decreased. Estimated dynamic behavior and thermodynamic parameters also showed weak interactions under high temperatures. This could have corresponded to looser molecular structure and weaker intermolecular interaction in high temperature, thereby increasing entropy and enthalpy. The interaction between glucagon and anti-glucagon IgG with pH- varied liquid environment exhibited weak interaction force, low energy barriers and high dissociation rates under acidic and alkaline solutions. This indicated that molecular interactions turned out weak forces when pH values increased or decreased away from neutrality. Force measurement as a function of temperature exhibited a nearly linear decrease of force strength with an increase of temperature. This could have been attributed to molecular charge-free conformational changes, resulting in incomplete binding. The thermodynamic enthalpy and entropy for interaction showed an increase with increasing temperature. Specific interactions of human IgG1/anti-human IgG1 pairs and glucagon/anti-glucagon IgG pairs have been successfully investigated by the atomic force microscope. With the use of an extended Bell and Evans model, the molecular dynamic behavior, free energy change and thermodynamic parameters can be obtained by varying physiological (pH and temperature) and physical (loading rate) conditions. The results provided directly evidence to explain the biological interactions.
Wang, Hongsheng. "Natural antibody recognition, signaling and surveillance in v-Ha-ras- and PKC-B1-overexpressing 10T1/2 fibroblasts." 1998. http://hdl.handle.net/1993/1574.
Full textKuo, Ting Yu, and 郭庭佑. "A study of antibody X in the recognition of Helicobacter pylori neutrophil-activating protein as a new antigen." Thesis, 2016. http://ndltd.ncl.edu.tw/handle/15235655246083217830.
Full text國立清華大學
分子與細胞生物研究所
104
Helicobacter pylori (H. pylori) is a major pathogen involved in gastritis, peptic ulcer disease, and gastric cancer. Helicobacter pylori neutrophil-activating protein (HP-NAP) is an important virulence factor of H. pylori. The inflammation of the gastric mucosa caused by H. pylori infection might be resulted from the cytokines and reactive oxygen species (ROS) produced by HP-NAP-stimulated human leukocytes. Thus, H. pylori-induced inflammation of the gastric mucosa could be attenuated by blocking the activity of HP-NAP. Here, I found that antibody X not only detected their target protein but also detected recombinant HP-NAP. By western-blot, enzyme linked immunosorbent assay (ELISA) and native western-blot analyses, the antibody X detects denatured and native form recombinant HP-NAP of H. pylori 26695 strain. To determine the epitope sequence of the antibody X on HP-NAP, HP-NAP mutants were generated by using the modified PCR-based site-directed mutagenesis method and then purified by one-step DEAE anion-exchange chromatography. The antibody X is able to recognize HP-NAP through a new set of epitope sequence which is different from the original epitope of antibody X. The epitope sequence is conserved in all H. pylori strains. The non-identical amino acid residues which nearby the epitope sequence of HP-NAP in various H. pylori strains were then subjected to site-directed mutagenesis. I found that the antibody X could detect these mutated HP-NAP, indicating that antibody X is able to detect HP-NAP of various H. pylori strains. Furthermore, antibody X is able to inhibit HP-NAP-stimulated ROS production by human neutrophils. Thus, antibody X is able to detect HP-NAP and block its activity through the new epitope sequence of HP-NAP.
Meng, Guangxun [Verfasser]. "Cellular recognition of microbial patterns through toll-like receptor (TLR) 2 : analysis of molecular requirements and monoclonal antibody mediated blockage / Guangxun Meng." 2004. http://d-nb.info/973389672/34.
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