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Glycome characterization of immunoglobulin G from buffalo (Bubalus bubalis) colostrum

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Abstract

Immunoglobulin G (IgG) is a major glycoprotein in ruminant colostrum. First day buffalo colostrum protein was purified on Sephadex G-100 and its mass was determined by MALDI-TOF as 147.848 KDa. The PMF data of protein subunits revealed its homology to IgG, which was supported by the identification of peptide sequences LLIYGATSR and VYNEYLPAPIVR corresponding to light and heavy chains of IgG by CID MS/MS analysis. The N-glycan microheterogeneity was established based on chemoselective glycoblotting technique with the identification of high mannose, neutral complex/hybrid and sialylated complex/hybrid glycans. A complete structural assignment of 54 N-linked oligosaccharides were identified and the ratio of sialyl oligosaccharides was found to be higher compared to neutral saccharides. The fucosylation observed in more than 20 oligosaccharides, high mannose and trisialyl oligosaccharides were present in diminutive amount. The high non-fucosyl and sialyl oligosaccharides in buffalo colostrum IgG provide ample scope for its utilization in targeted therapies to elicit effective ADCC and anti-inflammatory responses.

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Abbreviations

MALDI-TOF:

Matrix-assisted laser desorption/ionization-time of flight

LC-MS/MS:

Liquid chromatography–mass spectrometry

PNGase F:

Peptide -N-Glycosidase F

PHM:

1-propanesulfonic acid 2-hydroxyl-3-myristamido

DTT:

Dithiothreitol

IAA:

Iodoacetic acid CID, Collision induced dissociation

PMF:

Peptide mass fingerprinting

ADCC:

Antibody-dependent cellular cytotoxicity

CDC:

Complement-dependent cytotoxicity

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Acknowledgments

HSA thanks INSA-JSPS for the award of overseas associateship and Mamatha Bhanu thanks University Post-graduate cell for the award of fellowship. Authors also thank protemics facility, IISc, Bangalore.

Conflict of interest

The authors declare no commercial or financial conflict of interest.

Funding

This work was supported by the Indian National Science Academy (INSA) and the Japan Society for the Promotion of Science (JSPS) fund.

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Authors and Affiliations

  1. Department of Biotechnology, University of Mysore, Manasagangotri, Mysore, 570006, India

    L. S. Mamatha Bhanu & H. S. Aparna

  2. Faculty of Advanced Life Sciences, Hokkaido University, Sapporo, 001-0021, Japan

    M. Amano & S.-I. Nishimura

Authors
  1. L. S. Mamatha Bhanu
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  2. M. Amano
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  3. S.-I. Nishimura
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  4. H. S. Aparna
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Correspondence to H. S. Aparna.

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Bhanu, L.S.M., Amano, M., Nishimura, SI. et al. Glycome characterization of immunoglobulin G from buffalo (Bubalus bubalis) colostrum. Glycoconj J 32, 625–634 (2015). https://doi.org/10.1007/s10719-015-9608-4

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