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Dataset from HDX-MS Studies of IgG1 Glycoforms and Their Interactions with the FcγR1a (CD64) Receptor

Published

Author(s)

Kyle Anderson, Kerry Scott, Ioannis Karageorgos, Elyssia Gallagher, Venkata Tayi, Michael Butler, Jeffrey W. Hudgens

Abstract

This database gives hydrogen-deuterium exchange mass spectrometry (HDX-MS) data from measurements of three purified IgG1 glycoform samples, predominantly G0F, G2F, and SAF, in isolation and in complexation with the high-affinity receptor, FcγR1a (CD64). The IgG1 antibody used in this study, aIL8hFc, is a murine-human chimeric IgG1, which inhibits IL-8 binding to human neutrophils. The working datasets comprise 17,750 deuterium uptake measurements in peptides from the receptor and the light and heavy chains of aIL8hFc obtained during 7 experiments, each comprising three runs of six exchange times. The data illuminate on the hydrogen exchange dynamics in isolated receptor, isolated IgG1 glycoforms, and receptor-IgG1 complexes.
Citation
Journal of Research (NIST JRES) -
Volume
126

Keywords

antibody-receptor interaction, chromatography, hydrogen-deuterium exchange, glycosylation, mass spectrometry, monoclonal antibody, precision, peptide, protein, proteolysis, proteomics, receptor.

Citation

Anderson, K. , Scott, K. , Karageorgos, I. , Gallagher, E. , Tayi, V. , Butler, M. and , J. (2021), Dataset from HDX-MS Studies of IgG1 Glycoforms and Their Interactions with the FcγR1a (CD64) Receptor, Journal of Research (NIST JRES), National Institute of Standards and Technology, Gaithersburg, MD, [online], https://doi.org/10.6028/jres.126.010, https://tsapps.nist.gov/publication/get_pdf.cfm?pub_id=931995 (Accessed October 25, 2021)
Created June 17, 2021