@article{0939929598f446c788980aadd90cf9c5,
title = "Antigen-Induced Allosteric Changes in a Human IgG1 Fc Increase Low-Affinity Fcγ Receptor Binding",
abstract = "Orlandi et al. show that antigen binding to Fab increases binding of IgG1 Fc to low-affinity FcγR by conformational allostery. Leucine to alanine mutations at positions 234 and 235 in the lower hinge of IgG1 globally alter Fc structure and biological activity by configurational allostery.",
keywords = "Fc receptor binding, Fc-effector function, HDX-MS, IgG1 LALA variants, RFADCC Assay, antigen binding, configurational allostery, conformational allostery, immunoglobulin",
author = "Chiara Orlandi and Daniel Deredge and Krishanu Ray and Neelakshi Gohain and William Tolbert and DeVico, {Anthony L.} and Patrick Wintrode and Marzena Pazgier and Lewis, {George K.}",
note = "Funding Information: The authors thank our colleagues in the Division of Vaccine Research, Institute of Human Virology for helpful comments and criticism of the work. In addition, the authors thank Dr. Daniel Bonsor of Institute of Human Virology of University of Maryland for his technical help with the ITC measurements and analysis. The research was supported by grant OPP1033109, Bill and Melinda Gates Foundation (to G.K.L.) as well as NIH grants R01AI087181 (to G.K.L.), 5P01AI120756 (to A.L.D. G.K.L. and G. Tomaras PI), P01AI124912 (to A.L.D. G.K.L. and R. Gallo PI), R01AI116274 (to M.P.), R01AI129769 (to M.P.), and R01AI150447 (to K.R.). The Research was also supported in part by the NIH-funded Research Resource for Biomedical Glycomics (NIH grant P41GM10349010). In addition, the research was supported by internal funds of the Institute of Human Virology as well as the University of Maryland Baltimore, School of Pharmacy Mass Spectrometry Center (SOP1841-IQB2014). Conceptualization, G.K.L. C.O. K.R. M.P. and A.L.d.V.; Methodology, G.K.L. C.O. K.R. M.P. A.L.d.V. P.W. and D.D.; Investigation, C.O. K.R. W.T. N.G. and D.D.; Writing – Original Draft, C.O.; Writing – Review & Editing, G.K.L. C.O. K.R. M.P. A.L.d.V. W.T. N.G. P.W. and D.D.; Visualization, G.K.L. M.P. K.R. P.W. D.D. and C.O.; Supervision, G.K.L.; Project Administration, G.K.L.; Funding Acquisition, G.K.L. K.R. M.P. and A.L.d.V. The authors declare no competing interests. Funding Information: The authors thank our colleagues in the Division of Vaccine Research, Institute of Human Virology for helpful comments and criticism of the work. In addition, the authors thank Dr. Daniel Bonsor of Institute of Human Virology of University of Maryland for his technical help with the ITC measurements and analysis. The research was supported by grant OPP1033109 , Bill and Melinda Gates Foundation (to G.K.L.) as well as NIH grants R01AI087181 (to G.K.L.), 5P01AI120756 (to A.L.D., G.K.L., and G. Tomaras PI), P01AI124912 (to A.L.D., G.K.L., and R. Gallo PI), R01AI116274 (to M.P.), R01AI129769 (to M.P.), and R01AI150447 (to K.R.). The Research was also supported in part by the NIH -funded Research Resource for Biomedical Glycomics ( NIH grant P41GM10349010 ). In addition, the research was supported by internal funds of the Institute of Human Virology as well as the University of Maryland Baltimore , School of Pharmacy Mass Spectrometry Center ( SOP1841-IQB2014 ). Publisher Copyright: {\textcopyright} 2020 Elsevier Ltd",
year = "2020",
month = may,
day = "5",
doi = "10.1016/j.str.2020.03.001",
language = "English",
volume = "28",
pages = "516--527.e5",
journal = "Structure",
issn = "0969-2126",
number = "5",
}