alexa Site-Specific Classification of N -Linked Oligosaccharides of the Extracellular Regions of Fcγ Receptor IIIb Expressed in Baby Hamster Kidney Cells
ISSN: 2153-0637

Journal of Glycomics & Lipidomics
Open Access

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Research Article

Site-Specific Classification of N -Linked Oligosaccharides of the Extracellular Regions of Fcγ Receptor IIIb Expressed in Baby Hamster Kidney Cells

Nana Kawasaki1, Terumi Okumoto2, Yoshiki Yamaguchi2,3, Noriko Takahashi2, Wolf Herman Fridman4, Catherine Sautès-Fridman4, Hirokazu Yagi2 and Koichi Kato2,5,6,7*

1Division of Biological Chemistry and Biologicals, National Institute of Health Sciences, 1-18-1 Kami-yoga, Setagaya-ku, Tokyo 158-8501, Japan

2Faculty and Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya 467-8603, Japan

3Structural Glycobiology Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center, RIKEN Global Research Cluster, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan

4UMRS1138, University Paris Descartes, 15, rue de l’Ecole de Medecine 75270 Paris, France

5Institute for Molecular Science and Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, 5-1 Higashiyama Myodaiji, Okazaki 444-8787, Japan

6The Glycoscience Institute, Ochanomizu University, 2-1-1 Ohtsuka, Bunkyo-ku, Tokyo 112-8610, Japan

7GLYENCE Co., Ltd., 2-22-8 Chikusa, Chikusa-ku, Nagoya 464-0858, Japan

*Corresponding Author:
Koichi Kato
Faculty and Graduate School of Pharmaceutical Sciences
Nagoya City University, 3-1 Tanabe-dori
Mizuho-ku, Nagoya 467-8603, Japan
Tel: 81-564-59-5225
Fax: +81-564-59-5224
E-mail: [email protected]

Received date: May 22, 2014; Accepted date: July 14, 2014; Published date: July 25, 2014

Citation: Kawasaki N, Okumoto T, Yamaguchi Y, Takahashi N, Fridman WH, et al. (2014) Site-Specific Classification of N-Linked Oligosaccharides of the Extracellular Regions of Fcγ Receptor IIIb Expressed in Baby Hamster Kidney Cells. J Glycomics Lipidomics 4:116. doi: 10.4172/2153-0637.1000116

Copyright: © 2014 Kawasaki N, 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.



Human Fcγ receptor III (FcγRIII) consists of two isoforms that are encoded by two individual genes: transmembrane FcγRIIIa and glycosylphosphatidylinositol-linked FcγRIIIb. Both isoforms can exist as a soluble form (sFcγRIII), which is composed of their extracellular region produced by proteolytic cleavage. FcγRIII-mediated immunological functions such as antibody-dependent cell-mediated cytotoxicity and phagocytosis critically depend on the N-glycosylation of FcγRIII molecules. In our previous study, high-performance liquid chromatography-based profiling indicated that N-linked oligosaccharides released from the NA2 allele of human sFcγRIIIb expressed in baby hamster kidney cells are composed of high-mannose-type oligosaccharides and core-fucosylated complex-type oligosaccharides. Here we successfully classified the N-glycans of this glycoprotein into these two types at each of the six N-glycosylation sites by liquid chromatography (LC)-electrospray tandem mass spectrometry analysis combined with endoglycosidase treatments. Our results indicated that three sites of sFcγRIIIb, Asn38, Asn74, Asn162, and Asn169, expressed only complex-type oligosaccharides, while the remaining two sites, Asn45 and Asn64 (both are not conserved in the NA1 allele), were occupied by not only complex-type oligosaccharides but also high-mannose-type oligosaccharides, which are thought to be involved in the interaction of FcγRIIIb with complement receptor type 3. Together with the previously reported site-specific N-glycosylation profiling of recombinant sFcγRIIIa, this study underlines that both sFcγRIIIa and sFcγRIIIb produced in different production vehicles express core-fucosylated complex-type oligosaccharides as the major glycoforms at Asn74 and Asn162. These finding provide insights into the design and development of therapeutic antibodies because the Asn162 N-glycan significantly contributes to immunoglobulin G binding.

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