Glycoconjugate Journal

, Volume 31, Issue 2, pp 145–159 | Cite as

Avian influenza H5 hemagglutinin binds with high avidity to sialic acid on different O-linked core structures on mucin-type fusion proteins

  • Stefan Gaunitz
  • Jining Liu
  • Anki Nilsson
  • Niclas Karlsson
  • Jan Holgersson


The interaction between P-selectin glycoprotein ligand-1/mouse IgG2b (PSGL-1/mIgG2b) fusion protein carrying multiple copies of the influenza hemagglutinin receptor Siaα2-3Gal on different O-glycan chains and recombinant human influenza H5N1 A/Vietnam/1203/04 hemagglutinin was investigated with a Biacore biosensor. The fusion protein was produced by stable cell lines in large scale cultures and purified with affinity- and gel filtration chromatography. The C-P55 and 293-P cell lines were established by transfecting the Chinese hamster ovary (CHO)-K1 and Human embryonic kidney (HEK)-293 cell lines with plasmids encoding the PSGL-1/mIgG2b fusion protein, while the C-PSLex cell line was engineered by transfecting CHO-K1 cells with the plasmids encoding the core 2 β1,6GnT-I and FUT-VII glycosyltransferases. Glycosylation was characterized by lectin Western blotting of the proteins and liquid chromatography - mass spectrometry of released non-derivatized O-glycans. Biacore experiments revealed that PSGL-1/mIgG2b is a good binding partner of H5. The binding curves displayed a slow dissociation indicating a multivalent binding. The H5 hemagglutinin binds with similar strength to PSGL-1/mIgG2b carrying mostly sialylated core 1 (clone C-P55), a mix of sialylated core 1 and sialylated lactosamine (clone 293-P) or mainly sialylated lactosamine (clone C-PSLex) O-glycans, indicating that this hemagglutinin is unable to discriminate between these structures. The potential use of the large, flexible PSGL-1/mIgG2b mucin-type fusion protein carrying Siaα2-3Gal as a multivalent inhibitor of influenza virus is discussed.


Mucins Avian influenza Hemagglutinin Mass spectrometry Biacore 


P-selectin glycoprotein ligand-1/mouse IgG2b



liquid chromatography mass spectrometry












chinese hamster ovary cells


N-acetylneuraminic acid


sialic acid



We acknowledge Dr. Jin Chunsheng and Liaqat Ali for their assistance with the liquid chromatography mass spectrometry analysis. We acknowledge Recopharma AB that provided PSGL-1/mIgG2b produced in C-P55, P-PM and C-PSLex and allowed us to use the Wave Bioreactor for the production of the 293-P cells. We thank Åsa Bergström for access to the Biacore 2000 instrument at the Department of Biosciences and Nutrition, Karolinska Institutet. We acknowledge Tom Morton at BioLogic Software for providing the Scrubber 2 software. We thank Catherine Hayes for helping us to publish the mass spectrometry data in the UniCarb-DB.

Conflicts of interest

J.H. is a part time CEO/CSO, board member and shareholder of Recopharma AB.


This work was supported by the Swedish Research Council [K2011-65X-3031-01-6 to J.H. and 621-2010-5322 to N.G.K.], the County Council of Västra Götaland (ALF) to J.H. and Karolinska Institute Faculty funds (KID-funding) to S.G. The mass spectrometer was obtained by a grant from the Swedish Research Council [342-2004-4434].


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Copyright information

© Springer Science+Business Media New York 2013

Authors and Affiliations

  • Stefan Gaunitz
    • 1
  • Jining Liu
    • 2
  • Anki Nilsson
    • 3
  • Niclas Karlsson
    • 4
  • Jan Holgersson
    • 2
  1. 1.Division of Clinical Immunology and Transfusion Medicine, Department of Laboratory Medicine, Karolinska University HospitalKarolinska InstituteHuddingeSweden
  2. 2.Department of Clinical Chemistry and Transfusion Medicine, Institute of Biomedicine, the Sahlgrenska AcademyUniversity of GothenburgGothenburgSweden
  3. 3.Recopharma ABGothenburgSweden
  4. 4.Department of Medical Biochemistry, Institute of Biomedicine, Sahlgrenska AcademyUniversity of GothenburgGothenburgSweden

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