Skip Navigation


Glycobiology Advance Access originally published online on April 2, 2003
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow All Versions of this Article:
13/7/539    most recent
cwg071v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (10)
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Choi, O.
Right arrow Articles by Lee, Y. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Choi, O.
Right arrow Articles by Lee, Y. C.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Glycobiology, 2003, Vol. 13, No. 7 539-548
© 2003 Oxford University Press

N-glycan structures of human transferrin produced by Lymantria dispar (gypsy moth) cells using the LdMNPV expression system

One Choi2,3, Noboru Tomiya2, Jung H. Kim3, James M. Slavicek4, Michael J. Betenbaugh5 and Yuan C. Lee1,2

2 Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, USA
3 Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Yusong-gu, Taejon 305-701, Korea
4 USDA Forest Service, Northeastern Research Station, Forestry Sciences Laboratory, 359 Main Road, Delaware, OH 43015, USA
5 Department of Chemical and Biomolecular Engineering, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, USA

Received on January 9, 2003; revised on March 14, 2003; accepted on March 14, 2003

N-glycan structures of recombinant human serum transferrin (hTf) expressed by Lymantria dispar (gypsy moth) 652Y cells were determined. The gene encoding hTf was incorporated into a Lymantria dispar nucleopolyhedrovirus (LdMNPV) under the control of the polyhedrin promoter. This virus was then used to infect Ld652Y cells, and the recombinant protein was harvested at 120 h postinfection. N-glycans were released from the purified recombinant human serum transferrin and derivatized with 2-aminopyridine; the glycan structures were analyzed by a two-dimensional HPLC and MALDI-TOF MS. Structures of 11 glycans (88.8% of total N-glycans) were elucidated. The glycan analysis revealed that the most abundant glycans were Man1–3(±Fuc{alpha}6)GlcNAc2 (75.5%) and GlcNAcMan3(±Fuc{alpha}6)GlcNAc2 (7.4%). There was only ~6% of high-mannose type glycans identified. Nearly half (49.8%) of the total N-glycans contained {alpha}(1,6)-fucosylation on the Asn-linked GlcNAc residue. However {alpha}(1,3)-fucosylation on the same GlcNAc, often found in N-glycans produced by other insects and insect cells, was not detected. Inclusion of fetal bovine serum in culture media had little effect on the N-glycan structures of the recombinant human serum transferrin obtained.

1 To whom correspondence should be addressed; e-mail: yclee{at}jhu.edu


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
N. Tomiya, S. Narang, J. Park, B. Abdul-Rahman, O. Choi, S. Singh, J. Hiratake, K. Sakata, M. J. Betenbaugh, K. B. Palter, et al.
Purification, Characterization, and Cloning of a Spodoptera frugiperda Sf9 beta-N-Acetylhexosaminidase That Hydrolyzes Terminal N-Acetylglucosamine on the N-Glycan Core
J. Biol. Chem., July 14, 2006; 281(28): 19545 - 19560.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.