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Order Lefavirales
Published in Paul Pumpens, Peter Pushko, Philippe Le Mercier, Virus-Like Particles, 2022
Paul Pumpens, Peter Pushko, Philippe Le Mercier
It should be noted that the baculovirus-infected insect cells were developed as a display platform for class II MHC (MHCII) molecules covalently bound to a library of potential peptide mimotopes (Crawford et al. 2004). The peptide mimotope/MHC complexes that bound to the soluble receptors and stimulated T cells bearing the same receptors were gained by the “fishing” in this library with soluble fluorescent T cell receptors. Next, this approach was adapted for use with MHCI (Wang Yibing et al. 2005) and extensively reviewed by Crawford et al. (2006).
Biologic Therapies for Rheumatoid Arthritis
Published in Thomas F. Kresina, Monoclonal Antibodies, Cytokines, and Arthritis, 2020
Ian R. Mackay, Merrill J. Rowley, Claude C. A. Bernard
As another possibility for therapy directed at the antigen-presenting cell, we can refer to analogs of the culprit antigen, designated mimotopes. This of course depends on knowing the identity and structural sequence of the antigen, particularly the sequence that binds to the MHC class II molecule. This sequence is known as the agretope. The idea is that an analog of the agretope, the mimotope, competes with the agretope for the binding site on the MHC class II molecule and so interferes with presentation of the antigen to the T cell receptor. This approach to immunotherapy may appear conceptual rather than applicable, but we draw attention to the demonstrated competition in vivo in mice between self peptides and foreign antigens for MHC class II binding, with resulting interference in T cell activation (28). This has led to studies in experimental models to show that a mimotope can indeed block the expression of an autoimmune disease by competing with autoantigen at the level of the antigen presenting cell (29).
A nanobody-derived mimotope against VEGF inhibits cancer angiogenesis
Published in Journal of Enzyme Inhibition and Medicinal Chemistry, 2020
Elmira Karami, Jean-Marc Sabatier, Mahdi Behdani, Shiva Irani, Fatemeh Kazemi-Lomedasht
Different mimotopes have been designed by various approaches for cancer treatment. For example, a study focussed on a mimotope mimicking specific epitopes that induced antibodies against VEGF. Of note, this mimotope was established using the phage display method47. In another study, mimotopes (with low molecular weights) were expressed on the surface of phage particles and were used as a substitute of natural EGFR to induce an ‘active’ immunity responsible for a long term humoral response48. In an additional study, a mimotope was extracted from tocilizumab which could induce dual humoral and cellular responses of the immune system49. Pourhashem et al. also designed a mimotope against HER3 using in silico studies, but not fully characterised and requiring further in vitro and in vivo experiments24.
Preclinical evaluation of an affinity-enhanced MAGE-A4-specific T-cell receptor for adoptive T-cell therapy
Published in OncoImmunology, 2020
Joseph P Sanderson, Darragh J Crowley, Guy E Wiedermann, Laura L Quinn, Katherine L Crossland, Helen M Tunbridge, Terri V Cornforth, Christopher S Barnes, Tina Ahmed, Karen Howe, Manoj Saini, Rachel J Abbott, Victoria E Anderson, Barbara Tavano, Miguel Maroto, Andrew B Gerry
These studies cannot completely eliminate the risk of adverse events due to off-target reactivity in the clinic. In particular, several novel approaches to evaluating TCR specificity have been recently published, which allow the identification of mimotope peptides with minimal sequence similarity to the known index peptide,42,43 in contrast to the X-scan which is limited to relatively conservative substitutions. In addition, the primary cell screen is performed without regard to the gene expression profile of the cell types and would benefit from a more systematic approach to selecting cells, with the aim of maximizing genomic coverage amongst the panel of cells tested. These cells could additionally be treated with IFNγ to induce the immunoproteosome and replicate the immunopeptidome exposed during inflammatory events.
Engineering an anti-CD52 antibody for enhanced deamidation stability
Published in mAbs, 2019
Huawei Qiu, Ronnie Wei, Julie Jaworski, Ekaterina Boudanova, Heather Hughes, Scott VanPatten, Anders Lund, Jaime Day, Yanfeng Zhou, Tracey McSherry, Clark Q. Pan, Rebecca Sendak
CD52 binding affinity was determined by Biacore. Low level of a CD52 peptide mimotope (CGQNDTSQTSSPSAD) was immobilized on a CM5 chip via thiol chemistry using an N-terminal Cys. A new surface was immobilized on each assay occasion and the level of binding was checked with an internal reference standard (wild-type). Antibodies were diluted in HBS-EP running buffer (10 mM HEPES, 150 mM NaCl, 3 mM EDTA, 0.005% Tween-20 pH 7.4) to either a single concentration for relative binding comparison or several concentrations for kinetic analysis. The diluted antibodies were injected for 3 min over the surface to monitor the binding at 30 μL/min flow-rate. Either a report point was taken at the end of injection to calculate % of wild-type binding or kinetic analysis was performed with a 1:1 binding model using the Scrubber2 software. In early studies, binding measurements were performed a single time in “screening mode,” but for the final leads, KD was carefully determined using kinetic mode.