Site-specific protein glycosylation analysis with glycan isomer differentiation (original) (raw)
Abstract
Glycosylation is one of the most common yet diverse post-translational modifications. Information on glycan heterogeneity and glycosite occupancy is increasingly recognized as crucial to understanding glycoprotein structure and function. Yet, no approach currently exists with which to holistically consider both the proteomic and glycomic aspects of a system. Here, we developed a novel method of comprehensive glycosite profiling using nanoflow liquid chromatography/mass spectrometry (nano-LC/MS) that shows glycan isomer-specific differentiation on specific sites. Glycoproteins were digested by controlled non-specific proteolysis in order to produce informative glycopeptides. High-resolution, isomer-sensitive chromatographic separation of the glycopeptides was achieved using microfluidic chip-based capillaries packed with graphitized carbon. Integrated LC/MS/MS not only confirmed glycopeptide composition but also differentiated glycan and peptide isomers and yielded structural information on both the glycan and peptide moieties. Our analysis identified at least 13 distinct glycans (including isomers) corresponding to five compositions at the single _N_-glycosylation site on bovine ribonuclease B, 59 distinct glycans at five _N_-glycosylation sites on bovine lactoferrin, 13 distinct glycans at one _N_-glycosylation site on four subclasses of human immunoglobulin G, and 20 distinct glycans at five _O_-glycosylation sites on bovine κ-casein. Porous graphitized carbon provided effective separation of glycopeptide isomers. The integration of nano-LC with MS and MS/MS of non-specifically cleaved glycopeptides allows quantitative, isomer-sensitive, and site-specific glycoprotein analysis.

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Overlaid chromatograms and associated structural assignments of glycopeptides from bovine κ-casein. Color denotes the site(s) of glycosylation from which the glycopeptide originated
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Abbreviations
bLF:
Bovine lactoferrin
CID:
Collision-induced dissociation
CNBr:
Cyanogen bromide
ECC:
Extracted compound chromatogram
Fuc:
Fucose
Gal:
Galactose
Glc:
Glucose
Hex:
Hexose
HexNAc:
_N_-acetylhexosamine
IgG:
Immunoglobulin G
Man:
Mannose
Man_X_ (where X = 5 to 9):
High mannose glycan of composition GlcNAc2Man X
NeuAc:
_N_-acetylneuraminic acid
PGC:
Porous graphitized carbon
Q-TOF:
Quadrupole time-of-flight
RNAse B:
Ribonuclease B
TIC:
Total ion chromatogram
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Acknowledgments
We would like to thank Ning Tang and Keith Waddell (Agilent Technologies Inc.) for instrumentation and technical support. Financial support was provided by the University of California Discovery Grant Program, the California Dairy Research Foundation, the NIEHS Superfund Research Program (P42 ES02710), and the CHARGE Study (P01 ES11269).
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Authors and Affiliations
- Department of Chemistry, University of California, Davis, CA, 95616, USA
Serenus Hua, Charles C. Nwosu, John S. Strum, Richard R. Seipert & Carlito B. Lebrilla - Graduate School of Analytical Science and Technology, Chungnam National University, Daejeon, 305-764, South Korea
Hyun Joo An - Department of Food Science and Technology, University of California, Davis, CA, 95616, USA
Angela M. Zivkovic & J. Bruce German - Foods for Health Institute, University of California, Davis, CA, 95616, USA
Angela M. Zivkovic, J. Bruce German & Carlito B. Lebrilla - Department of Biochemistry and Molecular Medicine, University of California, Davis, CA, 95616, USA
Carlito B. Lebrilla
Authors
- Serenus Hua
- Charles C. Nwosu
- John S. Strum
- Richard R. Seipert
- Hyun Joo An
- Angela M. Zivkovic
- J. Bruce German
- Carlito B. Lebrilla
Corresponding author
Correspondence toCarlito B. Lebrilla.
Additional information
Published in the special issue High-Resolution Mass Spectrometry with guest editors Hans H. Maurer and David C. Muddiman.
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Hua, S., Nwosu, C.C., Strum, J.S. et al. Site-specific protein glycosylation analysis with glycan isomer differentiation.Anal Bioanal Chem 403, 1291–1302 (2012). https://doi.org/10.1007/s00216-011-5109-x
- Received: 14 March 2011
- Revised: 05 May 2011
- Accepted: 13 May 2011
- Published: 08 June 2011
- Issue date: May 2012
- DOI: https://doi.org/10.1007/s00216-011-5109-x