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J. Biol. Chem., Vol. 278, Issue 47, 46293-46306, November 21, 2003

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N-Glycan Structures of Pigeon IgG

A MAJOR SERUM GLYCOPROTEIN CONTAINING Gal1–4Gal TERMINI^*

Noriko Suzuki, Kay-Hooi Khoo, Chin-Mei Chen, Hao-Chia Chen¶, and Yuan C. Lee||

From the Department of Biology, The Johns Hopkins University, Baltimore, Maryland 21218, Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan, and ^¶Endocrinology and Reproduction Research Branch, NICHD, National Institutes of Health, Bethesda, Maryland 20892

We had shown previously that all major glycoproteins of pigeon egg white contain Gal1–4Gal epitopes (Suzuki, N., Khoo, K. H., Chen, H. C., Johnson, J. R., and Lee, Y. C. (2001) J. Biol. Chem. 276, 23221–23229). We now report that Gal1–4Gal-bearing glycoproteins are also present in pigeon serum, lymphocytes, and liver, as probed by Western blot with Griffonia simplicifolia-I lectin (specific for terminal -Gal) and anti-P₁ (specific for Gal1–4Gal1–4GlcNAc1–) monoclonal antibody. One of the major glycoproteins from pigeon plasma was identified as IgG (also known as IgY), which has Gal1–4Gal in its heavy chains. High pressure liquid chromatography, mass spectrometric (MS), and MS/MS analyses revealed that N-glycans of pigeon serum IgG included (i) high mannose-type (33.3%), (ii) disialylated biantennary complex-type (19.2%), and (iii) -galactosylated complex-type N-glycans (47.5%). Bi- and tri-antennary oligosaccharides with bisecting GlcNAc and 1–6 Fuc on the Asn-linked GlcNAc were abundant among N-glycans possessing terminal Gal1–4Gal sequences. Moreover, MS/MS analysis identified Gal1–4Gal1–4Gal1–4GlcNAc branch terminals, which are not found in pigeon egg white glycoproteins. An additional interesting aspect is that about two-thirds of high mannose-type N-glycans from pigeon IgG were monoglucosylated. Comparison of the N-glycan structures with chicken and quail IgG indicated that the presence of high mannose-type oligosaccharides may be a characteristic of these avian IgG.

Received for publication, July 3, 2003 , and in revised form, September 4, 2003.

^* This work was supported by National Institutes of Health Research Grant DK09970 (to N. S. and Y. C. L.) and by Academia Sinica (to K. H. K. and C. M. C.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains Figs. S1–S8.

^|| To whom correspondence should be addressed. Tel.: 410-516-7041; Fax: 410-516-8716; E-mail: yclee{at}jhu.edu.

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