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Relevant bibliographies by topics / Protein-Antibody recognition

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Academic literature on the topic 'Protein-Antibody recognition'

Author: Grafiati

Published: 9 March 2023

Last updated: 10 March 2023

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Journal articles on the topic "Protein-Antibody recognition"

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Addis, Philip W., Catherine J. Hall, Shaun Bruton, Vaclav Veverka, Ian C. Wilkinson, Frederick W. Muskett, Philip S. Renshaw, et al. "Conformational Heterogeneity in Antibody-Protein Antigen Recognition." Journal of Biological Chemistry 289, no. 10 (January 16, 2014): 7200–7210. http://dx.doi.org/10.1074/jbc.m113.492215.

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Ferrigno, Paul Ko. "Non-antibody protein-based biosensors." Essays in Biochemistry 60, no. 1 (June 30, 2016): 19–25. http://dx.doi.org/10.1042/ebc20150003.

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Biosensors that depend on a physical or chemical measurement can be adversely affected by non-specific interactions. For example, a biosensor designed to measure specifically the levels of a rare analyte can give false positive results if there is even a small amount of interaction with a highly abundant but irrelevant molecule. To overcome this limitation, the biosensor community has frequently turned to antibody molecules as recognition elements because they are renowned for their exquisite specificity. Unfortunately antibodies can often fail when immobilised on inorganic surfaces, and alternative biological recognition elements are needed. This article reviews the available non-antibody-binding proteins that have been successfully used in electrical and micro-mechanical biosensor platforms.

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Pierce, Brian G., Zhen-Yong Keck, Patrick Lau, Catherine Fauvelle, Ragul Gowthaman, Thomas F. Baumert, Thomas R. Fuerst, Roy A. Mariuzza, and Steven K. H. Foung. "Global mapping of antibody recognition of the hepatitis C virus E2 glycoprotein: Implications for vaccine design." Proceedings of the National Academy of Sciences 113, no. 45 (October 26, 2016): E6946—E6954. http://dx.doi.org/10.1073/pnas.1614942113.

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The E2 envelope glycoprotein is the primary target of human neutralizing antibody response against hepatitis C virus (HCV), and is thus a major focus of vaccine and immunotherapeutics efforts. There is emerging evidence that E2 is a highly complex, dynamic protein with residues across the protein that are modulating antibody recognition, local and global E2 stability, and viral escape. To comprehensively map these determinants, we performed global E2 alanine scanning with a panel of 16 human monoclonal antibodies (hmAbs), resulting in an unprecedented dataset of the effects of individual alanine substitutions across the E2 protein (355 positions) on antibody recognition. Analysis of shared energetic effects across the antibody panel identified networks of E2 residues involved in antibody recognition and local and global E2 stability, as well as predicted contacts between residues across the entire E2 protein. Further analysis of antibody binding hotspot residues defined groups of residues essential for E2 conformation and recognition for all 14 conformationally dependent E2 antibodies and subsets thereof, as well as residues that enhance antibody recognition when mutated to alanine, providing a potential route to engineer E2 vaccine immunogens. By incorporating E2 sequence variability, we found a number of E2 polymorphic sites that are responsible for loss of neutralizing antibody binding. These data and analyses provide fundamental insights into antibody recognition of E2, highlighting the dynamic and complex nature of this viral envelope glycoprotein, and can serve as a reference for development and rational design of E2-targeting vaccines and immunotherapeutics.

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Huang, Jiachen, Darren Diaz, and Jarrod J. Mousa. "Antibody recognition of the Pneumovirus fusion protein trimer interface." PLOS Pathogens 16, no. 10 (October 9, 2020): e1008942. http://dx.doi.org/10.1371/journal.ppat.1008942.

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Wang, Meryl, David Zhu, Jianwei Zhu, Ruth Nussinov, and Buyong Ma. "Local and global anatomy of antibody-protein antigen recognition." Journal of Molecular Recognition 31, no. 5 (December 8, 2017): e2693. http://dx.doi.org/10.1002/jmr.2693.

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Margulies, David, and Andrew D. Hamilton. "Combinatorial protein recognition as an alternative approach to antibody-mimetics." Current Opinion in Chemical Biology 14, no. 6 (December 2010): 705–12. http://dx.doi.org/10.1016/j.cbpa.2010.07.017.

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Kanaujia, G. V., S. Motzel, M. A. Garcia, P. Andersen, and M. L. Gennaro. "Recognition of ESAT-6 Sequences by Antibodies in Sera of Tuberculous Nonhuman Primates." Clinical Diagnostic Laboratory Immunology 11, no. 1 (January 2004): 222–26. http://dx.doi.org/10.1128/cdli.11.1.222-226.2004.

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ABSTRACT Previous work in our laboratory showed that the ESAT-6 protein of Mycobacterium tuberculosis and Mycobacterium bovis induces strong antibody responses in a large proportion (∼90%) of experimentally or naturally infected nonhuman primates. Here, the antibody response to ESAT-6 in tuberculous monkeys was characterized at the epitope level by measuring antibodies to overlapping, synthetic peptides spanning the ESAT-6 sequence. The antibody response against the COOH-terminal portion of the protein was the strongest in both experimentally and naturally infected animals. Moreover, these antibodies became detectable the earliest during experimental infection, suggesting an ordered expansion of ESAT-6-specific B-cell clones in the course of infection. The data support use of synthetic peptides in lieu of the full-length ESAT-6 protein in diagnostic antibody detection assays.

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Fuchs, Stephen M., Krzysztof Krajewski, Richard W. Baker, Victoria L. Miller, and Brian D. Strahl. "Influence of Combinatorial Histone Modifications on Antibody and Effector Protein Recognition." Current Biology 21, no. 1 (January 2011): 53–58. http://dx.doi.org/10.1016/j.cub.2010.11.058.

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Lak, Parnian, Spandana Makeneni, Robert J. Woods, and Todd L. Lowary. "Specificity of Furanoside-Protein Recognition through Antibody Engineering and Molecular Modeling." Chemistry - A European Journal 21, no. 3 (November 20, 2014): 1138–48. http://dx.doi.org/10.1002/chem.201405259.

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Otlewski, J., and W. Apostoluk. "Structural and energetic aspects of protein-protein recognition." Acta Biochimica Polonica 44, no. 3 (September 30, 1997): 367–87. http://dx.doi.org/10.18388/abp.1997_4392.

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Specific recognition between proteins plays a crucial role in a great number of vital processes. In this review different types of protein-protein complexes are analyzed on the basis of their three-dimensional structures which became available in recent years. The complexes which are analyzed include: those resulting from different types of recognition between proteinase and protein inhibitor (canonical inhibitors of serine proteinases, hirudin, inhibitors of cysteine proteinases, carboxypeptidase inhibitor), barnase-barstar, human growth hormone-receptor and antibody-antigen. It seems obvious that specific and strong protein-protein recognition is achieved in many different ways. To further explore this question, the structural information was analyzed together with kinetic and thermodynamic data available for the respective complexes. It appears that the energy and rates of specific recognition of proteins are influenced by many different factors, including: area of interacting surfaces; complementarity of shapes, charges and hydrogen bonds; water structure at the interface; conformational changes; additivity and cooperativity of individual interactions, steric effects and various (conformational, hydration) entropy changes.

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Dissertations / Theses on the topic "Protein-Antibody recognition"

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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.

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Topping, 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.

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Easton, 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.

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This thesis reports the characterisation of a novel outer membrane protein (OMP) from M. catarrhalis, designated M35, with a molecular mass of 36.1 kDa. This protein is structurally homologous to classic Gram-negative porins, such as OMP C from E. coli and OMP K36 from K. pneumoniae, with a predicted structure of 8 surface loops connecting 16 antiparallel -sheets. Comparison of the DNA sequences of the M35 genes from 18 diverse clinical isolates showed that the gene was highly conserved (99.6-100 % of nucleotides) with only one isolate (ID78LN266) having base variations that resulted in amino acid substitutions. A single amino acid mutation in the 3rd external loop of M35 in isolate ID78LN266 significantly affected antibody recognition, indicating that loop 3 contains an immunodominant B-cell epitope. The reduction in antibody-binding to M35 from ID78LN266 was similar to that caused by complete removal of loop 3. Since loop 3 folds into the porin channel in the classic structure, the antibody specificity to loop 3 was hypothesised to be a potential mechanism for evasion of host immune responses targeted to M35, potentially explaining the high degree of conservation across isolates. A series of recombinant proteins were constructed to analyse the binding to M35 of antibodies specificity for loop 3 or the remainder of the protein. It was found that loop 3- specific antibodies were not able to bind to M35 on the surface of M. catarrhalis and that this corresponds both with a lack of ability to enhance opsonophagocytosis in vitro and bacterial clearance in vivo. Additionally, antibodies raised against a version of M35 lacking loop 3 and M35 from the variant isolate ID78LN266 were both no less effective than the full consensus M35 by both these measures. It therefore appears that while the majority of antibodies raised against M35 are specific for loop 3 these antibodies do not mediate anti-M. catarrhalis actions. Two deletion mutant strains of M. catarrhalis that do not contain the outer membrane protein M35 were created by insertional inactivation of the M35 gene. Growth comparisons between these mutant strains and their wildtype parent strains initially led to the hypothesis that M35 is necessary for efficient glutamic acid uptake by M. catarrhalis, however this hypothesis was later shown to be incorrect. Efficient uptake of glutamic acid seemed to be mediated by a novel 40 kDa protein that was up-regulated in the deletion mutant strains, presumably to compensate for the lack of M35. M35 was also found to be essential for in vivo survival of M. catarrhalis in the nasal cavities of mice, indicating that it is an essential functional protein for colonisation of the mucosal surface.

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Al, 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.

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Ting, 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.

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Diestel, 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.

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Joel, Smita. "ENGINEERING PROTEINS WITH UNIQUE CHARACTERISTICS FOR DIAGNOSTICS AND BIOSENSORS." UKnowledge, 2011. http://uknowledge.uky.edu/gradschool_diss/180.

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Proteins possess a broad range of structural and functional properties and, therefore, can be employed in a variety of biomedical applications. While a good number of protein-based biosensing systems and biosensors for target analytes have been developed, the search for versatile, highly sensitive and selective sensors with long term stability able to provide fast detection of target analytes continues to be a challenge. To that end, we now report the design and development of modified proteins with tailored characteristics and their further utilization in the development of biosensing systems. We take advantage of binding proteins that undergo a change in conformation upon binding to their respective target ligand analytes for the development of highly selective biosensing systems. The first class of binding proteins that was explored for this purpose was antibodies. A non-canonical site in the variable region of a monoclonal antibody was tagged with a fluorescent probe to sense the binding of analyte to its corresponding antigen-binding site. The strategy employed for designing antibodysensing molecules is universal as it can be employed for sensing any biomolecule of interest provided that there is an available antibody against the target ligand analyte. In a second strategy, we utilized designer glucose recognition proteins (GRPs) that were prepared by incorporation of unnatural amino acids in the glucose/galactose binding protein (GBP) of Escherichia coli and its truncated fragments. By taking advantage of the global incorporation method, we were able to fine-tune the binding affinity and thermal stability of the proteins, thus, allowing for the development of a reagentless fluorescence based fiber optic glucose biosensor capable of monitoring glucose in the hypoglycemic, normal, and hyperglycemic range, as well as in the hypothermic and hyperthermic temperature range.

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SIRONI, LAURA. "Nanoparticles for in-vitro and in-vivo biosensing and imaging." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2011. http://hdl.handle.net/10281/19278.

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In the last two decades several groups have investigated the changes of chemical and physical properties of materials with size in nanometric scales. These studies have highlighted a number of possible applications for nanostructures, which are now employed, for example, in biology and medicine for imaging, disease detection, diagnosis, sensing and therapy. Noble metals (especially gold and silver nanoparticles) are particularly versatile for these applications due to the phenomenon known as surface plasmon resonance (SPR), an in-phase oscillations of all the conduction band electrons that resonates with the light wave electric field. The resonance frequency depends on the size, shape, orientation and dielectric constant of the nanoparticle. This coupling of SPR with the electromagnetic field leads to a large enhancement of all the nanoparticle radiative properties, such as absorption and scattering. The extinction cross section of these nanoparticles is 10^5-10^6 larger than that of organic dyes and in contrast to common molecular chromophores they are extremely photostable and, depending on the shape, they convert efficiently light into heat. The SPR, tunable in the visible (for spherical NPs) and near-infrared region (for anisotropic Nps) of the electromagnetic spectrum, can also interact, for gold nanoparticles a few nanometers in size, with the fluorescence emission of dyes and substantially modify their brightness and excited-state lifetime. Depending on the fluorophores-NP distance and the NPs anisotropy one can obtain fluorescence enhancement or quenching. In both cases we expect that any change in the dielectric constant of the NP surface, induced, for example, by a biorecognition process that occurs on the surface itself, can produce a change in the emission properties of the fluorophores. SPR effect becomes also particularly important when combined with two-photon excitation (TPE), which consists in the simultaneous absorption of two photons, each carrying about half the energy necessary to excite the molecule. TPE offers a series of unique features for biological investigation both in vitro and in vivo. First, the two-photon absorption bands of the dyes commonly used in biological studies are wider than their one-photon analogous allowing the simultaneous excitation of multiple fluorophores with a single excitation wavelength. Second, the stimulating light beam has a high penetration depth because of the long infrared wavelengths used, allowing experiments in turbid media. Third, excitation takes place only at the plane of focus, due to the scaling of the probability of simultaneous photon absorption with the square of the light intensity. As a consequence TPE avoids the simultaneous absorption of photons outside the specimen drastically reducing both photo-toxicity and fluorophore bleaching. These advantages make nowadays TPE a well established tool for scientific biological and medical research and can be coupled to anisotropic gold nanoparticles. In fact, the luminescence (TPL) induced by TPE is enhanced (when coupled with an appropriate plasmon resonance) by many orders of magnitude in non spherically symmetric NPs of noble metal with respect to the single photon excitation on smooth noble metal surfaces. These properties promise to improve the usefulness of these nanoparticles for in-vivo imaging in the NIR region of the electromagnetic spectrum. According to these considerations we have developed our project on two lines related to the use of gold nanoparticles for sensing and non linear imaging. The aim of the first part of this research project is to exploit changes of the dye excited-state lifetime and brightness induced by its interaction with the gold surface plasmons for detection of tiny amounts of protein in solution under physiological conditions. The system we investigated is based on 10 and 5 nm diameter gold NPs coupled (via a biotin- streptavidin linker) to the FITC dye and to a specific protein antibody. The interaction of the fluorophore with the gold surface plasmon resonances, mainly occurring through quenching, affects the excited state lifetime that is measured by fluorescence burst analysis in highly diluted suspensions. The binding of protein to the gold NPs through antigen-antibody recognition further modifies the dye excited-state lifetime, which change can then be used to measure the protein concentration. In particular, we have tested the nanodevice measuring the change of the fluorophore excited-state lifetime after the binding of the model protein bovine serum albumin (BSA); then we have applied the nanoassay in order to recognize the p53 protein, whose detection in the body is highly valuable as marker for early cancer diagnosis and prognosis, both in standard solutions and in total cell extracts. The selectivity of the construct with respect other globular proteins has been also addressed. The data indicate that the FITC excited-state lifetime is a very sensitive parameter in order to detect tiny amounts of protein in solution with an estimated limit of detection of about 5 pM, mostly determined by the statistical accuracy of the lifetime measurement. In the second part of the project we focused on the exploitation of anisotropic gold nanoparticles as probes in cellular imaging. We have then studied their photoluminescence (TPL) properties under two photon excitation. We have focused on gold nanorods that can easily be obtained by synthesis with the standard surfactant CTAB (cetyl trimethylammonium bromide). The synthesis of asymmetric branched gold nanoparticles, obtained using for the first time in the seed growth method approach a zwitterionic surfactant, laurylsulphobetaine (LSB), has been developed in collaboration with the University of Pavia (Prof. P.Pallavicini). We have shown that LSB concentration in the growth solution allows to control the dimension of the NPs and the SPR position, that can be tuned in the 700-1100 nm Near Infrared range. The samples have been analyzed with a number of structural techniques to obtain a complete characterization: absorption spectra in the UV-Visible region, TEM images of the suspensions, Fluorescence Correlation Spectroscopy (FCS) and Dynamic Light Scattering (DLS) experiments in suspensions. From these data we reached information on the nanoparticles shapes, dimensions and aggregation. In particular, three different populations have been found: nanospheres with diameter lower than 20 nm, nanostars characterized by large trapezoidal branches, and asymmetric branched nanoparticles with high aspect ratio (3-4). A full characterization of the NPs TPL was performed for imaging applications by employing two photon excitation (TPE). The dependence of the TPL intensity on the power, wavelength and polarization of the incident light intensity was studied and TPL was exploited to study the cellular uptake of the nanoparticles in different cell lines (macrophages and HEK cells).

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Agnew, 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.

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This 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.

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Kuo, 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.

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碩士
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.

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Books on the topic "Protein-Antibody recognition"

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1929-, Laver William Graeme, Air Gillian, and Cold Spring Harbor Laboratory, eds. Immune recognition of protein antigens. Cold Spring Harbor, N.Y: Cold Spring Harbor Laboratory, 1985.

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Adler, M. Properties and potential of protein–DNA conjugates for analytic applications. Edited by A. V. Narlikar and Y. Y. Fu. Oxford University Press, 2017. http://dx.doi.org/10.1093/oxfordhb/9780199533053.013.25.

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This article examines the properties of protein-DNA conjugates and their potential for analytic applications. It begins with a discussion of DNA as a rigid construction tool for protein networks, reducing its functionality to the molecular equivalent of a steel bar in 'large-scale' architecture. It then describes DNA functionality in protein-DNA conjugates, like specific recognition of nucleotide sequences or its unique use as an amplification template. It also considers a range of applications for protein-DNA conjugates, including the use of artificial DNA-protein nanostructures as supramolecular building blocks and DNA-antibody conjugates for ultrasensitive antigen detection. Finally, it evaluates DNA-directed immobilization of protein-DNA adaptor molecules for flexible protein arrays. It shows that protein-DNA conjugates can be used as analytical targets for challenging and calibrating the properties of high-resolution atomic force microscopy, as well as analytical reagents for ultrasensitive target detection in immuno-PCR and related techniques.

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Book chapters on the topic "Protein-Antibody recognition"

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Janin, Joël, Jacqueline Cherfils, and Stéphane Duquerroy. "Principles of Protein — Protein Recognition in Protease-Inhibitor and Antigen-Antibody Complexes." In Computation of Biomolecular Structures, 103–14. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-77798-1_9.

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"Macromolecule-Imprinted Polymers: Antibody/Receptor Mimics for Protein Recognition and Catalysis." In Biomedical Nanosensors, 35–72. Jenny Stanford Publishing, 2012. http://dx.doi.org/10.1201/b13721-4.

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LAVER, W. G., P. M. COLMAN, G. M. AIR, R. G. WEBSTER, J. N. VARGHESE, A. T. BAKER, P. A. TULLOCH, and W. R. TULIP. "Recognition of Protein Antigens by Antibodies: Crystal Structure of Antibody Fab Fragments Complexed with Influenza Virus Neuraminidase." In Immune Recognition and Evasion: Molecular Aspects of Host�parasite Interaction, 77–86. Elsevier, 1990. http://dx.doi.org/10.1016/b978-0-12-711710-2.50010-8.

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Sundberg, Eric J., and Roy A. Mariuzza. "Molecular recognition in antibody-antigen complexes." In Advances in Protein Chemistry, 119–60. Elsevier, 2002. http://dx.doi.org/10.1016/s0065-3233(02)61004-6.

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Conference papers on the topic "Protein-Antibody recognition"

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Lord, S. T. "DIRECTED MUTAGENESIS OF HUMAN FIBRINOGEN: Aα CHAIN SUBSTITUTIONS THAT ALTER THROMBIN CLEAVAGE AND ANTIBODY RECOGNITION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642887.

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The initial event in fibrin clot formation is the thrombin catalized cleavage of the Aa chain of fibrinogen between Argl6 and Glyl7, releasing fibrinopeptide A. Previous data indicate that most of the information required for thrombin recognition and cleavage of the Aa chain lies within the amino terminal 51 residue CNBr fragment. In order to use protein engineering techniques to study the interaction of thrombin with the Aa chain, we have constructed a plasmid expression vector which encodes a tripartite protein consisting of amino acids 1-50 of the Aa chain of human fibrinogen followed by 60 amino acids of chicken collagen, and the beta-galactosidase protein from Escherichia coli. The codons for an initiator methionine and amino acids 1-50 were assembled from 7 oligonucleotides. Protein blot analysis of bacterial lysates of cells induced to synthesize this tribrid protein show a single band (MW = 125,000) crossreactive with a monoclonal antibody, Y-18, which recognizes the Aa chain of fibrinogen but not the products of thrombin cleavage. When these lysates are incubated with thrombin, fibrinopeptide A is released as demonstrated both by protein blot analysis and radioimmunoassay. By including one heterogeneous oligonucleotide in the assembly process, we have constructed plasmids which encode specific amino acid substitutions within residues 1-23. One of these substitutions, Glyl4 to val, significantly alters both cleavage by thrombin and recognition by Y-18. Substitution of ilu for Arg23 alters neither thrombin cleavage nor monoclonal recognition while substitution of leu for Argl6 alters thrombin cleavage, but not recognition by Y-18.

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White, Mitch, James Head, Grith Sorensen, Uffe Holmskov, Erika Crouch, and Kevan L. Hartshorn. "Monoclonal Antibody Assisted Structure-function Analysis Of The Carbohydrate Recognition Domain Of Surfactant Protein D." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a4973.

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Pancham, N., M. Dumas, J. Brown, T. C. Michaud, and W. J. Knowles. "SYNTHETIC PEPTIDE ANTIBODIES RECOGNIZE PLASMA AND RECOMBINANT FVIII." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644027.

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Monoclonal antibodies were raised against synthetic peptides corresponding to the N-termini of the 90kd and 80kd subunits of human FVIII. Preliminary screening was performed directly against the peptides (linked to albumin) coated onto polystyrene wells. IgG was purified by Protein A-Sepharose and affinity purified using the immunogen peptides linked to Sepharose. Immunoreactivity with both plasma and recombinant FVIII was compared by Western blotting, two-site ELISA employing a neutralizing rabbit anti-FVIII IgG as capture antibody, and inhibition in a fluid phase FVIII activity assay. None of the antibodies neutralized clotting or amidolytic activities associated with either FVIII protein. All of the antibodies immunoblotted intacl or thrombin digested FVIII polypeptides according to their anticipated epitope recognition sites; this was useful in determining identity between the two types of FVIII protein. Furthermore, when either FVIII protein was bound to polyclonal IgG coated onto polystyrene microtiter wells, the 80kd antipeptide antibody was capable of detecting both antigens with equal affinity. These results, coupled with results using the 90k antipeptide suggest that epitope accessibility for these antipeptide antibodies is the same for plasma and recombinant FVIII under the conditions tested.

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Torres-Almonacid, Jorge, David Medina-Ortiz, Diego Alvarez-Saravia, Julio Aguila-Guerrero, Alvaro Olivera-Nappa, and Marcelo Navarrete. "Pattern recognition on antigen-antibody interactions from protein microarrays based on data mining and bioinformatics analysis." In 2019 38th International Conference of the Chilean Computer Science Society (SCCC). IEEE, 2019. http://dx.doi.org/10.1109/sccc49216.2019.8966421.

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Vermeer, C., BA M. Soute, and MM W. Ulrich. "IN VITRO CARBOXYLATION OF EXOGENOUS PROTEIN SUBSTRATES BY VITAMIN K-DEPENDENT CARBOXYLASE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643994.

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In vivo treatment of experimental animals with vitamin K-antagonists induces the accumulation of non-carboxylated coagulation factor precursors in the liver, where they are tightly bound to vitamin K-dependent carboxylase. If hepatic carboxylase is isolated from warfarin-treated animals, it is obtained therefore almost exclusively in the form of an enzyme/substrate complex. If carboxylase is prepared from non-treated animals, on the other hand, the resulting enzyme is predominantly substrate-free. Small substrates like F L E E L or decarboxylated osteocalcinare carboxylated equally well by both types of carboxylase, but protein substrates(Mr > 30 000) are recognized exclusively by substrate-free carboxylase.Initial attempts to purify carboxylasewere performed with livers from warfarin-treated cows as a starting material. Antibodies against the normal blood coagulation factors crossreact with the hepatic precursor proteins so that the enzyme/substrate complexes could be specifically extracted from detergent-solubilized microsomes by the substrate/antibody interaction. This procedure resulted ina substantial purification of carboxylase, but because its endogenous substrate remained firmly bound, even after it had been carboxylated in vitro, the enzyme system was not suitable for the carboxylation of protein substrates.Therefore a second strategy was developed by which substrate-free carboxylase (from normal livers) was partly purified by sequential extraction of the microsomal membranes with detergents, followed by ammonium sulfate precipitation and size exclusion chromatography.This procedure resulted in a soluble carboxylase complex, still consisting of 7 proteins and phosphatidylcholine. Although further dissociation of the complex resulted in a complete loss of activity, it is not sure if all components play a role in the carboxylation reaction. Exogenous substrates which could be carboxylated by substrate-free carboxylase were: the penta-peptide F L E E L, descarboxyprothrombin from bovine plasma, thermally decarboxylated osteocalcin from bovine bone and non-car-boxy lated coagulaton factor precursors which had been produced by recombinant-DNA techniques in various laboratories. The . efficiency of CO^ incorporation was: 1 mole per 100 moles of F L E E L, 1 mole per 240 moles of descarboxy-prothrombin, 1 mole per mole of decarboxylated osteocalcin and 8 moles per mole of a recombinant factor IX precursor. We assume that the high efficiency with which the recombinant coagulation factor precursors were carboxylated is due to the presence of at least part of their leader sequence. The importance of the aminoacid chain preceding the first carboxylatable Glu residue is demonstrated by the fact that descarboxylated osteocalcin of bovine origin is carboxylated with a relatively high efficiency, whereas descarboxylated osteocalcin from monkey bone is not recognized atal.. Yet the only difference between the two substrates is found in their aminoacids 3 and 4, whereas the first carboxylatable Glu occurs at position 17. It seems, therefore, that the aminoacids 1-16 in bovine osteocalcin mimic to some extent part of the leader sequence in the coagulation factor precursors. Chemical or biochemical modification of decarboxylated osteocalcin might reveal which structural features contribute to its recognition by hepatic carboxylase.The optimal conditions for carboxylation include a high concentration of dithiols (e.g. DTT) and under these conditions disulfide bridges are reduced. Obviously this will lead to a complete destruction of the biological activity of various carboxylated products. Therefore we have searched for a more natural reducing system and it was found that the bacterial thioredoxin/thiore-doxin-reductase system in the presence of 40 uM NADFH was able to replace DTT in the reaction mixtures. Since a comparable system also occurs in calf liver it seems not unlikely that this is the physiological counterpart of the dithiols used in vitro.

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Lima, Beatriz Alves, Andressa da Silva Pereira, Bruna Alves Lima, Diana Gonçalves Lima, Leonardo Ferreira Pucci, Renato Moraes Ferreira, Tiago Castro Ferreira, and Henrique Ferreira Pucci. "PREDICTORS OF BREAST CANCER PROGNOSIS BASED ON TUMOR BIOMARKERS." In Abstracts from the Brazilian Breast Cancer Symposium - BBCS 2021. Mastology, 2021. http://dx.doi.org/10.29289/259453942021v31s2022.

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Objective: To analyze the tumor biological markers of breast cancer associated with the prognostic of the disease. Methodology: A systematic review was carried out on the Scielo, PubMed, and the National Cancer Institute databases on the topic. Descriptors used were: tumor biomarkers, breast cancer, and prognosis. Thus, 15 articles published between 2001 and 2020 were selected. Results: Breast cancer, characterized by the disordered multiplication of breast cells, is the most incident in women in the world, representing 24.2% of the total cases in 2018, and the most frequent cause of death in this gender. Accordingly, tumor markers are complementary tests for early diagnosis, since they are macromolecules derived from the tumor and biological fluids. The evaluation of tumor markers is of paramount importance due to the great diversity in clinical progression of breast cancer, for example, those hormone receptors (estrogen and progesterone), MIB-1, Ki-67, PCNA, p53, and c-erbB-2. Hence, about two-thirds of breast cancers are positive for hormone receptors and are related to a more favorable prognosis. PCNA (36 kDa protein perceptible in the cell nucleus from the late G1 to the S phase of the cell cycle) and MIB-1 (direct antibody against parts of the Ki-67 antigen) have a high proportion of tumor cells associated with a high-degree tumor differentiation, indicating a worse prognosis. Furthermore, mutations in the p53 and c-erbB-2 genes report low levels of estrogen and progesterone receptors, leading to a worse prognosis. Conclusion: In brief, the recognition of the main markers helps in the identification of patients with potentially aggressive tumors and in the mortality reduction of breast cancer, through treatments that can alter the course of the disease. On account of this, it is known that the tumor markers must be used in combination with the other methods such as diagnostic, prognostic, and therapeutic modifications.

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Reports on the topic "Protein-Antibody recognition"

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Spiegel, Yitzhak, Michael McClure, Itzhak Kahane, and B. M. Zuckerman. Characterization of the Phytophagous Nematode Surface Coat to Provide New Strategies for Biocontrol. United States Department of Agriculture, November 1995. http://dx.doi.org/10.32747/1995.7613015.bard.

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Chemical composition and biological role of the surface coat (SC) of the root-knot nematodes, Meloidogyne spp. are described. SC proteins of M. incognita race 3 infective juveniles (J2) were characterized by electrophoresis and western blotting of extracts from radioiodine and biotin-labelled nematodes. J2 labelled with radioiodine and biotin released 125I and biotin-labelled molecules into water after 20 hours incubation, indicating that SC proteins may be loosely attached to the nematode. Antiserum to the principal protein reacted with the surface of live J2 and with surface proteins previously separated by electrophoresis. Human red blood cells (HRBC) adhered to J2 of several tylenchid nematodes over the entire nematode body. HRBC adhered also to nylon fibers coated with SC extracted from M. javanica J2; binding was Ca++/Mg++ dependent, and decreased when the nylon fibers were coated with bovine serum albumin, or pre-incubated with fucose and mannose. These experiments support a working hypothesis that RBC adhesion involves carbohydrate moieties of HRBC and carbohydrate-recognition domain(s) (CRD) distributed on the nematode surface. To our knowledge, this is the first report of a surface CRD i the phylum Nematoda. Gold-conjugated lectins and neoglycoproteins combined with silver enhancement have been used for the detection of carbohydrates and CRD, respectively, on the SC of M. javanica J2. Biotin reagents were used to trace surface proteins, specifically, on live J2. The labile and transitory nature of the SC was demonstrated by the dynamics of HRBC adherence to detergent-treated J2, J2 at different ages or fresh-hatched J2 held at various temperatures. SC recovery was demonstrated also by a SDS-PAGE profile. Monoclonal antibodies developed to a cuticular protein of M. incognita J2 gave a slight, but significant reduction in attachment of Pasteuria penetrans spores. Spore attachment as affected by several enzymes was inconsistent: alcian blue, which specifically blocks sulfyl groups, had no afffect on spore attachment. Treatment with cationized ferritin alone or catonized ferritin following monoclonal antibody caused significant decreases in spore attachment. Those results suggest a role in attachment by negatively charged groups.

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