alexa N-Glycosylation Profiles of Chicken Immunoglobulin Y Glycoproteins Expressed by Different Production Vehicles | OMICS International | Abstract
ISSN: 2153-0637

Journal of Glycomics & Lipidomics
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Special Issue Article

N-Glycosylation Profiles of Chicken Immunoglobulin Y Glycoproteins Expressed by Different Production Vehicles

Sachiko Kondo1,2, Hirokazu Yagi1, Yukiko Kamiya1,3, Akihiko Ito4, Motoki Kuhara5, Ayako Kudoh5, Noriko Takahashi1 and Koichi Kato1,2,3,6*
1Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya, 467-8603, Japan
2Glyence Co., Ltd., 2-22-8 Chikusa, Chikusa-ku, Nagoya 464-0858, Japan
3Institute for Molecular Science and Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, 5-1 Higashiyama Myodaiji, Okazaki 444-8787, Japan
4Department of Pathology, Faculty of Medicine, Kiniki University 377-2 Ohno-Higashi, Osaka-Sayama, Osaka 589-8511, Japan
5Antibody Development Department Manufacturing Division, Medical & Biological Laboratories Co. Ltd., 1063-103, Terasawaoka, Ina, Nagano, 396-0002, Japan
6The Glycoscience Institute, Ochanomizu University, 2-1-1 Ohtsuka, Bunkyo-ku, Tokyo 112-8610, Japan
Corresponding Author : Koichi Kato
Institute for Molecular Science and
Okazaki Institute for Integrative Bioscience
National Institutes of Natural Sciences
5-1 Higashiyama Myodaiji, Okazaki 444-8787, Japan
Tel: 81-564-59-5225
Fax: +81-564-59-5224
E-mail: [email protected]
Received April 20, 2012; Accepted May 21, 2012; Published May 23, 2012
Citation: Kondo S, Yagi H, Kamiya Y, Ito A, Kuhara M, et al. (2012) N-Glycosylation Profiles of Chicken Immunoglobulin Y Glycoproteins Expressed by Different Production Vehicles. J Glycomics Lipidomics S5:002. doi: 10.4172/2153-0637.S5-002
Copyright: © 2012 Kondo S, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Abstract

Immunoglobulin Y (IgY), abundant in egg yolk, is widely used as an immunochemical reagent and has been recently appreciated as a potential therapeutic tool. The Fc portion of IgY conserves an N-glycosylation site at Asn407, which is structurally equivalent to conserved glycosylation sites of other Ig classes in mammals. Despite such similarities, IgYs from chicken serum and egg yolk have been shown to be distinct glycoforms, best exemplified by the high incidence of monoglucosylated high mannose-type oligosaccharides, which are rarely found in mammalian glycoproteins. To gain further insight into the glycosylation properties of IgY, we report a comparative N-glycosylation profiling of recombinant chicken IgYs that have identical amino acid sequences in their variable regions but are expressed by different production vehicles. The N-linked oligosaccharides cleaved from these IgYs were subjected to multidimensional HPLC mapping in conjunction with mass spectrometric analyses. N-glycosylation profiles of the IgYs showed obviously different patterns depending on the production vehicle. While IgY expressed by chicken hybridoma cells retained the premature high mannose-type oligosaccharides, IgY expressed by CHO cells experienced extensive N-glycan processing and displayed high antennary oligosaccharides. Significant differences were also observed in the levels of core fucosylation and bisecting N-acetylglucosaminylation and in sialyl linkage types among the IgYs expressed by different vehicles. Despite such differences, the recombinant IgY antibodies commonly expressed considerable populations of monoglucosylated glycoforms, suggesting that this glycosylation feature is, to some extent, associated with the distinctive quaternary structure of IgY-Fc, which, at least partially, masks the Asn407 N-glycans and sequesters them from chaperone mechanisms in the endoplasmic reticulum. We suggest that the timing and efficiency of N-glycan processing and the quaternary structure formation of IgY are considerably different from those of IgE and depend on the vehicles used for recombinant IgY production, resulting in varying incidence of monoglucosylated species.

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