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Glycobiology Advance Access published online on December 23, 2003
Glycobiology, doi:10.1093/glycob/cwh031
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Submitted on September 27, 2003
Revised on November 7, 2003
Accepted on November 10, 2003

© 2003 Oxford University Press

ORIGINAL ARTICLES

Site specific N-glycosylation of chicken serum IgG

Noriko Suzuki 1* and Yuan C. Lee 1

1 Department of Biology, The Johns Hopkins University, Baltimore, MD, 21218

* To whom correspondence should be addressed. E-mail: nrsuzuki{at}jhu.edu.

Abstract

Avian serum immunoglobulin, abbreviated as either IgG or IgY, is functionally equivalent to mammalian IgG, but has one additional constant region domain (CH2) in its heavy (H) chain. In chicken IgG, each H chain contains two potential N-glycosylation sites located on CH2 and CH3 domains. To clarify characteristics of N-glycosylation on avian IgG, we analyzed N-glycans from chicken serum IgG by derivatization with 2-aminopyridine (PA) and identified by HPLC and MALDI-TOF-MS. There were two types of N-glycans: i) high-mannose-type oligosaccharides (monoglucosylated 26.8%, others 10.5%), and ii) biantennary complex-type oligosaccharides (neutral, 29.9%; monosialyl, 29.3%; disialyl, 3.7%) on molar basis of total N-glycans. To investigate the site-specific localization of different N-glycans, chicken serum IgG was digested with papain and separated into Fab [containing variable regions (VH+VL) + CH1+CL] and Fc (containing CH3+CH4) fragments. Con A stained only Fc(CH3+CH4), and RCA-I stained only Fab fractions, suggesting that high-mannose-type oligosaccharides were located on Fc(CH3+CH4) fragments, while variable regions of Fab contains complex-type N-glycans. Mass spectrometric analysis of chicken IgG-glycopeptides revealed that chicken CH3 domain (structurally equivalent to mammalian CH2 domain) contained only high-mannose-type oligosaccharides, while chicken CH2 domain contained only complex-type N-glycans. The N-glycosylation pattern on avian IgG is more analogous to that in mammalian IgE than IgG, presumably reflecting the structural similarity to mammalian IgE.


Asn297, chicken serum IgG, IgG-Fc, monoglucosylated high-mannose-type, N-glycan processing
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