Article

Glycoconjugate Journal

, 26:1055

First online:

Identification of high-mannose and multiantennary complex-type N-linked glycans containing α-galactose epitopes from Nurse shark IgM heavy chain

  • David J. HarveyAffiliated withOxford Glycobiology Institute, Department of Biochemistry, University of Oxford Email author 
  • , Max CrispinAffiliated withDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford
  • , Beryl E. MoffattAffiliated withMRC Immunochemistry Unit, Department of Biochemistry, University of Oxford
  • , Sylvia L. SmithAffiliated withDepartment of Biological Sciences, Florida International University
  • , Robert B. SimAffiliated withMRC Immunochemistry Unit, Department of Biochemistry, University of Oxford
  • , Pauline M. RuddAffiliated withNational Institute for Bioprocessing, Research and Training (NIBRT), Conway Institute, University College Dublin
  • , Raymond A. DwekAffiliated withOxford Glycobiology Institute, Department of Biochemistry, University of Oxford

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Abstract

MALDI-TOF mass spectrometry, negative ion nano-electrospray MS/MS and exoglycosidase digestion were used to identify 36 N-linked glycans from 19S IgM heavy chain derived from the nurse shark (Ginglymostoma cirratum). The major glycan was the high-mannose compound, Man6GlcNAc2 accompanied by small amounts of Man5GlcNAc2, Man7GlcNAc2 and Man8GlcNAc2. Bi- and tri-antennary (isomer with a branched 3-antenna) complex-type glycans were also abundant, most contained a bisecting GlcNAc residue (β1→4-linked to the central mannose) and with varying numbers of α-galactose residues capping the antennae. Small amounts of monosialylated glycans were also found. This appears to be the first comprehensive study of glycosylation in this species of animal. The glycosylation pattern has implications for the mechanism of activation of the complement system by nurse shark IgM.

Keywords

Nurse shark N-Glycans MALDI mass spectrometry Negative ion fragmentation α-Galactose