1/9/2024 0 Comments Igg reactivity![]() 1, 14080 México D.F.).Īddress for correspondence and reprints request * Laboratorio de Inmunoparasitología, Instituto Nacional de Cardiología I. Nadia Hernández-Becerril,* Arnulfo Nava,* Pedro A Reyes,* Víctor M Monteón* Reactividad de subclases de IgG a Trypanosoma cruzi en pacientes crónicos chagásicos All rights reserved.IgG subclass reactivity to Trypanosoma cruzi in chronic chagasic patients Together, these data document for the first time the full spectrum of cross-reactivities of mouse IgG to human FcγRs.Īffinity Cross-reactivity Deglycosylation Human Fc gamma receptor Mouse IgG subclass Surface plasmon resonance.Ĭopyright © 2020 The Authors. Importantly, deglycosylation of the least cross-reactive mIgG subclass, mIgG2b, abrogated reactivity to all hFcγRs. Deglycosylation of mIgG1 did not abrogate binding to hFcγRIIa-R131, nor did deglycosylation of mIgG2a/c and mIgG3 prevent hFcγRIa binding. No binding was observed of mIgG to hFcγRIIIb. hFcγRIIIa showed lower binding (mIgG2a/c > mIgG3), slightly favouring binding to the hFcγRIIIa-V158 over the F158 polymorphic variant. A particularly high affinity was observed for mIgG1 to the hFcγRIIa-R131 polymorphic variant. hFcγRIIa/b showed general low reactivities to all mIgG (mIgG1> mIgG2a/c > mIgG2b), with no reactivity to mIgG3. mIgG subclasses show the strongest binding to hFcγRIa, with relative affinities mIgG2a = mIgG2c > mIgG3 > mIgG2b, and no binding by mIgG1. Here, we report detailed and quantifiable characterization of binding affinities for all mIgG subclasses to hFcγRs, including functional polymorphic variants. ![]() Despite this drawback, the binding of mouse IgG (mIgG) subclasses to human FcγR (hFcγR) classes has never been fully documented. In other applications, such as immunostaining with mouse IgG monoclonal antibodies (mAbs), these cross-reactivities are undesired and prone to misinterpretation. Accordingly, binding of human IgG (hIgG) to mouse FcγRs (mFcγRs) has been utilized to study effector functions of hIgG in mice. Despite interspecies differences, IgG subclasses and FcγRs show substantial similarities and functional conservation between mammals. Electronic address: G (IgG) antibodies are important for protection against pathogens and exert effector functions through binding to IgG-Fc receptors (FcγRs) on myeloid and natural killer cells, resulting in destruction of opsonized target cells. 7 Department of Experimental Immunohematology, Sanquin Research and Landsteiner Laboratory, Amsterdam University Medical Center, University of Amsterdam, Amsterdam, The Netherlands. ![]() 6 Department of Pathology, Carter Immunology Center, University of Virginia School of Medicine, Charlottesville, Virginia, United States.5 Sanquin Reagents, Amsterdam, The Netherlands.4 Department of Immunopathology, Sanquin Research and Landsteiner Laboratory, Amsterdam University Medical Center, University of Amsterdam, Amsterdam, The Netherlands.3 Department of Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, The Netherlands.2 Department of Experimental Immunohematology, Sanquin Research and Landsteiner Laboratory, Amsterdam University Medical Center, University of Amsterdam, Amsterdam, The Netherlands Department of Immunopathology, Sanquin Research and Landsteiner Laboratory, Amsterdam University Medical Center, University of Amsterdam, Amsterdam, The Netherlands.1 Department of Experimental Immunohematology, Sanquin Research and Landsteiner Laboratory, Amsterdam University Medical Center, University of Amsterdam, Amsterdam, The Netherlands.
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