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The N-glycolyl form of mouse sialyl Lewis X is recognized by selectins but not by HECA-452 and FH6 antibodies that were raised against human cells

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Abstract

E-, P- and L-selectins critically function in lymphocyte recirculation and recruiting leukocytes to inflammatory sites. MECA-79 antibody inhibits L-selectin-mediated lymphocyte adhesion in several species and does not require sialic acid in its epitope. Many other antibodies, however, recognize human selectin ligands expressing N-acetylneuraminic acid but not mouse selectin ligands expressing N-glycolylneuraminic acid, suggesting that difference in sialic acid in sialyl Lewis X leads to differential reactivity. We found that HECA-452 and FH6 monoclonal antibodies bind Chinese hamster ovary (CHO) cells expressing N-acetylneuraminyl Lewis X oligosaccharide but not its N-glycolyl form. Moreover, synthetic N-acetylneuraminyl Lewis X oligosaccharide but not its N-glycolyl oligosaccharide inhibited HECA-452 and FH6 binding. By contrast, E-, P- and L-selectin bound to CHO cells regardless of whether they express N-acetyl or N-glycolyl form of sialyl Lewis X, showing that selectins have a broader recognition capacity than HECA-452 and FH-6 anti-sialyl Lewis x antibodies.

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Abbreviations

NeuGc:

N-glycolylneuraminic acid

NeuAc:

N-acetylneuraminic acid

HEV:

high endothelial venule

DMB:

1,2-diamino-4.5-methylene-dioxybenzene

Cmah:

CMP-NeuAc hydroxylase

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Acknowledgement

We thank Yoav Altman and Anette Flesman for technical assistance, Dr. Elise Lamar for critical reading of the manuscript, and Aleli Morse for organizing the manuscript.

This work was supported by NIH grants (CA48737 to M.F., CA71932 to M.F. and P.H.S., and HL85607 to R.O.C.), the Biotechnology and Biological Sciences Research Council BBSRC (to A.D. and H.R.M.), and NIH grant GM62116 for Consortium for Functional Glycomics. A.D. is a BBSRC Professor Fellow.

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Author notes

  1. Junya Mitoma

    Present address: Tohoku Pharmaceutical University, Sendai, Japan

  2. Tatsuo Miyazaki

    Present address: Department of Applied Life Sciences, Niigata University of Pharmacy and Applied Life Sciences, Niigata, Japan

Authors and Affiliations

  1. Glycobiology Program, Cancer Research Center, Burnham Institute for Medical Research, 10901 N. Torrey Pines Rd., La Jolla, CA, 92037, USA

    Junya Mitoma, Tatsuo Miyazaki, Misa Suzuki, Hideo Saito, Jiunn-Chern Yeh, Ole Hindsgaul, Peter H. Seeberger & Minoru Fukuda

  2. Division of Molecular Biosciences, Faculty of Natural Sciences, Imperial College London, London, UK

    Mark Sutton-Smith, Maria Panico, Stuart M. Haslam, Howard R. Morris & Anne Dell

  3. Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, ON, Canada

    Takehiro Kawano

  4. Department of Biochemistry, Emory University School of Medicine, Atlanta, GA, USA

    Richard D. Cummings

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Mitoma, J., Miyazaki, T., Sutton-Smith, M. et al. The N-glycolyl form of mouse sialyl Lewis X is recognized by selectins but not by HECA-452 and FH6 antibodies that were raised against human cells. Glycoconj J 26, 511–523 (2009). https://doi.org/10.1007/s10719-008-9207-8

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