Bibliografías temáticas / FAB-ANTIGENS COMPLEX STRUCTURE

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Literatura académica sobre el tema "FAB-ANTIGENS COMPLEX STRUCTURE"

Autor: Grafiati

Publicado: 10 de marzo de 2023

Última modificación: 31 de julio de 2025

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Artículos de revistas sobre el tema "FAB-ANTIGENS COMPLEX STRUCTURE"

Zimanyi, Marcell, Kaitlin Hulce, Charles Craik, and Yifan Cheng. "Cryo-EM Determines the Epitope of a 28 kD Viral Protease in Complex with an Antibody Fragment." Structural Dynamics 12, no. 2_Supplement (2025): A304. https://doi.org/10.1063/4.0000610.

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Cryo-Electron Microscopy (cryo-EM) is an enabling technology for structure-guided antibody drug design. The 50 kD antibody fragment antigen-binding (Fab) is particularly amenable to cryo-EM due to its clear features and its ability to make rigid complexes with antigens. However, the technical challenges of analyzing macromolecular complexes under 100 kD hinders the analysis of Fabs bound to a large portion of the druggable genome. We were able to determine the structure of a Fab in complex with a 28 kD viral protease where the entire Fab and its binding interface (epitope) are resolved below 3

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Yazaki, Shuma, Misaki Komatsu, Jinhua Dong, Hiroshi Ueda, and Ryoichi Arai. "Crystal Structures of Antigen-Binding Fragment of Anti-Osteocalcin Antibody KTM219." International Journal of Molecular Sciences 26, no. 2 (2025): 648. https://doi.org/10.3390/ijms26020648.

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Osteocalcin is a useful biomarker for bone formation and bone-related diseases. KTM219 is an anti-osteocalcin C-terminal peptide antibody. The single-chain variable region (scFv) and antigen-binding fragment (Fab) of KTM219 are applicable to the Quenchbody (Q-body) immunoassay. Q-body is a new type of fluorescent immunosensor, which is scFv or Fab labeled with a fluorescent dye. When Q-body binds to its antigen, the fluorescence intensity increases. The highly sensitive detection of antigens by changes in fluorescence intensity is performed in a single step by mixing the sample and reagent. In

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Panda, Abir Kumar, Kannan Natarajan, Surajit Sinha, et al. "Inhibition of Ly-49/LILRB-MHC-I interactions by anti-MHC-I augments innate and adaptive immunity." Journal of Immunology 210, no. 1_Supplement (2023): 169.14. http://dx.doi.org/10.4049/jimmunol.210.supp.169.14.

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Abstract Mouse NK cells recognize MHC-I antigens via stochastically expressed inhibitory Ly49 receptors. The loss of MHC-I expression on tumor cells (“missing self”) abrogates inhibitory signals, resulting in NK activation. We have identified an anti-mouse pan MHC-I mAb (M1/42), which blocks Ly49-MHC-I interactions but not TCR-MHC-I interactions. Administration of M1/42 in vivo markedly activated IFNg-producing NK cells that further drove the proliferation of NK cells and memory phenotype (MP) T cells and profoundly augmented adaptive immunity against viral infection and cancer metastasis. In

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Radwańska, Malwina J., Mateusz Jaskółowski, Elena Davydova, et al. "The structure of the C-terminal domain of the nucleoprotein from the Bundibugyo strain of the Ebola virus in complex with a pan-specific synthetic Fab." Acta Crystallographica Section D Structural Biology 74, no. 7 (2018): 681–89. http://dx.doi.org/10.1107/s2059798318007878.

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The vast majority of platforms for the detection of viral or bacterial antigens rely on immunoassays, typically ELISA or sandwich ELISA, that are contingent on the availability of suitable monoclonal antibodies (mAbs). This is a major bottleneck, since the generation and production of mAbs is time-consuming and expensive. Synthetic antibody fragments (sFabs) generated by phage-display selection offer an alternative with many advantages over Fabs obtained from natural antibodies using hybridoma technology. Unlike mAbs, sFabs are generated using phage display, allowing selection for binding to s

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Verdaguer, Nuria, Noemi Sevilla, Mari Luz Valero, et al. "A Similar Pattern of Interaction for Different Antibodies with a Major Antigenic Site of Foot-and-Mouth Disease Virus: Implications for Intratypic Antigenic Variation." Journal of Virology 72, no. 1 (1998): 739–48. http://dx.doi.org/10.1128/jvi.72.1.739-748.1998.

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ABSTRACT The three-dimensional structures of the Fab fragment of a neutralizing antibody raised against a foot-and-mouth disease virus (FMDV) of serotype C1, alone and complexed to an antigenic peptide representing the major antigenic site A (G-H loop of VP1), have been determined. As previously seen in a complex of the same antigen with another antibody which recognizes a different epitope within antigenic site A, the receptor recognition motif Arg-Gly-Asp and some residues from an adjacent helix participate directly in the interaction with the complementarity-determining regions of the antib

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Vukovich, Matthew J., Andrea R. Shiakolas, Jared Lindenberger, et al. "Isolation and characterization of IgG3 glycan-targeting antibodies with exceptional cross-reactivity for diverse viral families." PLOS Pathogens 20, no. 9 (2024): e1012499. http://dx.doi.org/10.1371/journal.ppat.1012499.

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Broadly reactive antibodies that target sequence-diverse antigens are of interest for vaccine design and monoclonal antibody therapeutic development because they can protect against multiple strains of a virus and provide a barrier to evolution of escape mutants. Using LIBRA-seq (linking B cell receptor to antigen specificity through sequencing) data for the B cell repertoire of an individual chronically infected with human immunodeficiency virus type 1 (HIV-1), we identified a lineage of IgG3 antibodies predicted to bind to HIV-1 Envelope (Env) and influenza A Hemagglutinin (HA). Two lineage

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Pan, Jingxi, and Sara Zhang. "Antibody epitope mapping at single residue resolution for unpurified antigens." Journal of Immunology 202, no. 1_Supplement (2019): 131.36. http://dx.doi.org/10.4049/jimmunol.202.supp.131.36.

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Abstract The vast majority of antigen-antibody interactions rely upon binding to conformational epitopes, which are composed of amino acids that are discontinuous in the protein sequence but are brought together upon three-dimensional protein folding. This character has made conformational epitopes particularly difficult to map because they are only formed in the native structure of the antigen protein. X-ray crystallography is a gold-standard method for mapping conformational epitopes at high-resolution, but it only works for highly purified antigens and is time consuming, and is not applicab

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Mitropoulou, Alkistis N., Holly Bowen, Tihomir S. Dodev, et al. "Structure of a patient-derived antibody in complex with allergen reveals simultaneous conventional and superantigen-like recognition." Proceedings of the National Academy of Sciences 115, no. 37 (2018): E8707—E8716. http://dx.doi.org/10.1073/pnas.1806840115.

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Antibodies classically bind antigens via their complementarity-determining regions, but an alternative mode of interaction involving V-domain framework regions has been observed for some B cell “superantigens.” We report the crystal structure of an antibody employing both modes of interaction simultaneously and binding two antigen molecules. This human antibody from an allergic individual binds to the grass pollen allergen Phl p 7. Not only are two allergen molecules bound to each antibody fragment (Fab) but also each allergen molecule is bound by two Fabs: One epitope is recognized classicall

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Onuoha, Shimobi, Mathieu Ferrari, Anna Bulek, et al. "Structure Guided Engineering of Highly Specific Chimeric Antigen Receptors for the Treatment of T Cell Lymphomas." Blood 132, Supplement 1 (2018): 1661. http://dx.doi.org/10.1182/blood-2018-99-119564.

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Abstract Introduction Mature T cell lymphomas are aggressive, treatment resistant cancers that are associated with poor prognosis. Clinical application of immunotherapeutic approaches has been limited by a lack of target antigens that discriminate malignant from healthy T cells. Unlike B cell depletion, pan-T cell aplasia is prohibitively toxic. Previously we reported a targeting strategy based on the mutually exclusive expression of T cell receptor beta-chain constant domains 1 and 2 (TRBC1 and TRBC2). We identified an antibody with unique TRBC1 specificity and demonstrated that anti TRBC1 ch

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Danska, J. S., A. M. Livingstone, V. Paragas, T. Ishihara, and C. G. Fathman. "The presumptive CDR3 regions of both T cell receptor alpha and beta chains determine T cell specificity for myoglobin peptides." Journal of Experimental Medicine 172, no. 1 (1990): 27–33. http://dx.doi.org/10.1084/jem.172.1.27.

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The T cell receptor alpha/beta (TCR-alpha/beta) is encoded by variable (V), diversity (D), joining (J), and constant (C) segments assembled by recombination during thymocyte maturation to produce a heterodimer that imparts antigenic specificity to the T cell. Unlike immunoglobulins (Igs), which bind free antigen, the ligands of TCR-alpha/beta are cell surface complexes of intracellularly degraded antigens (i.e., peptides) bound to and presented by polymorphic products of the major histocompatibility complex (MHC). Therefore, antigen recognition by T cells is defined as MHC restricted. A model

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Tesis sobre el tema "FAB-ANTIGENS COMPLEX STRUCTURE"

BIANCHI, FEDERICA, LUCIA BANCI, CLAUDIO LUCHINAT, DOMENICO MAIONE, ROBERTA COZZI, and LAURA SANTINI. "Characterization of the human immune response after vaccination with Bexsero through structural and functional studies of human Fabs from a longitudinal memory B-cell repertoire." Doctoral thesis, 2018. http://hdl.handle.net/2158/1142497.

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The multi-component vaccine 4CMenB (Bexsero) is the first recombinant vaccine for the prevention of invasive meningococcal disease licensed in over 35 countries. The meningococcal factor H binding protein (fHbp), one of three main protein antigens in 4CMenB, specifically binds human factor H (hfH) and thereby down-regulates the human complement cascade. Over 1000 distinct amino acid sequences of fHbp have been identified and can be classified in three variants which are immunologically distinct. Within the fHbp variant groups the sequence identity is usually above 87%, while between variant gr

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Capítulos de libros sobre el tema "FAB-ANTIGENS COMPLEX STRUCTURE"

LAVER, W. G., P. M. COLMAN, G. M. AIR, et al. "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. Elsevier, 1990. http://dx.doi.org/10.1016/b978-0-12-711710-2.50010-8.

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