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Glycobiology Advance Access originally published online on July 9, 2007
Glycobiology 2007 17(10):1061-1069; doi:10.1093/glycob/cwm074
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© The Author 2007. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

VIPL has sugar-binding activity specific for high-mannose-type N-glycans, and glucosylation of the {alpha}1,2 mannotriosyl branch blocks its binding

Daisuke Yamaguchi2, Norihito Kawasaki2, Ichiro Matsuo3, Kiichiro Totani3, Hideto Tozawa2, Naoki Matsumoto2, Yukishige Ito3,4, and Kazuo Yamamoto1,2,4,

2 Department of Integrated Biosciences, Graduate School of Frontier Sciences, University of Tokyo, Bioscience BLD 602, 5-1-5 Kashiwanoha, Kashiwa, Chiba 277-8562, Japan
3 RIKEN, Saitama 351-0198, Japan
4 CREST, JST, Saitama 332-1102, Japan

1 To whom correspondence should be addressed; Tel: +81-4-7136-3614; Fax: +81-4-7136-3619; e-mail: yamamoto{at}k.u-tokyo.ac.jp

Received on February 9, 2007; revised on July 1, 2007; accepted on July 1, 2007

VIP36-like protein (VIPL) was identified as an endoplasmic reticulum (ER) resident protein with homology to VIP36, a cargo receptor involved in the transport of glycoproteins within cells. Although VIPL is structurally similar to VIP36, VIPL is thought not to be a lectin, because its sugar-binding activity has not been detected in several experiments. Here, recombinant soluble VIPL proteins (sVIPL) were expressed in Escherichia coli, biotinylated with biotin ligase and oligomerized with R-phycoerythrin (PE)-labeled streptavidin (SA). As measured with flow cytometry, PE-labeled sVIPL–SA bound to deoxymannojirimycin (DMJ)- or kifunensine (KIF)- but not to swainsonine (SW)-treated HeLaS3 cells in the presence of calcium. A surface plasmon resonance analysis showed that the avidity of sVIPL was enhanced after it formed a complex with SA. The binding of PE-labeled sVIPL–SA was abrogated by endo ß-N-acetylglucosaminidase H treatment of the DMJ- or KIF-treated cells. Competition with several high-mannose-type N-glycans inhibited VIPL binding, and indicated that VIPL recognizes the Man{alpha}1–2Man{alpha}1–2Man sequence. Glucosylation of the outer mannose residue of this portion decreased the binding. Although the biochemical characteristics of VIPL are similar to those of VIP36, the sugar-binding activity of VIPL was stronger at neutral pH, corresponding to the pH in the lumen of the ER, than under acidic conditions.

Key words: high mannose type / lectin / N-glycan / VIPL


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