Campus Units

Biochemistry, Biophysics and Molecular Biology, Roy J. Carver Department of, Office of Biotechnology

Document Type

Article

Publication Version

Accepted Manuscript

Publication Date

11-1-2019

Journal or Book Title

Molecular & Cellular Proteomics

Volume

18

Issue

11

First Page

2178

Last Page

2190

DOI

10.1074/mcp.RA119.001607

Abstract

Post-translational modification confers diverse functional properties to immune system proteins. The composition of serum proteins such as immunoglobulin G (IgG) strongly associates with disease including forms lacking a fucose modification of the crystallizable fragment (Fc) asparagine(N)-linked glycan that show increased effector function, however, virtually nothing is known about the composition of cell surface receptors or their bound ligands in situ due to low abundance in the circulating blood. We isolated primary NK cells from apheresis filters following plasma or platelet donation to characterize the compositional variability of Fc g receptor IIIa / CD16a and its bound ligand, IgG1. CD16a N162-glycans showed the largest differences between donors; one donor displayed only oligomannose-type N-glycans at N162 that correlate with high affinity IgG1 Fc binding while the other donors displayed a high degree of compositional variability at this site. Hybrid-type N-glycans with intermediate processing dominated at N45 and highly modified, complex-type N-glycans decorated N38 and N74 from all donors. Analysis of the IgG1 ligand bound to NK cell CD16a revealed a sharp decrease in antibody fucosylation (43.2 ±11.0%) versus serum from the same donors (89.7 ±3.9%). Thus, NK cells express CD16a with unique modification patterns and preferentially bind IgG1 without the Fc fucose modification at the cell surface.

Comments

This research was originally published in Molecular and Cellular Proteomics. Patel, Kashyap R., Joel D. Nott, and Adam W. Barb. "Primary human natural killer cells retain proinflammatory IgG1 at the cell surface and express CD16a glycoforms with donor-dependent variability." Molecular & Cellular Proteomics 2019; 18:2178-2190. © Patel et al. doi: 10.1074/mcp.RA119.001607.

Copyright Owner

Patel et al.

Language

en

File Format

application/pdf

Published Version

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