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Author Notes:

Correspondence and requests for materials should be addressed to J.-X.S. (email: jshe@augusta.edu)

J.X.S., P.G.W., R.D.C., S.P., and B.D. were involved with conception of the project.

S.P. and Y.T. were responsible for creation of the MGBA and profiling of lectins and serum samples.

T.L., G.W., J.S., X.S., L.L. synthesized the glycan compounds.

A.S. was responsible for data analysis.

B.D. created anti-glycan antibodies.

D.M., S.G. and B.R. contributed to clinical samples.

All authors contributed to writing and editing of the manuscript.

The authors declare no competing financial interests.

Subjects:

Research Funding:

This work was supported by National Institute of Health (NIH)/ National Cancer Institute (NCI) grant 1 R21 CA199868 and U01CA221242 to JXS, PGW, RDC and SP, as well as the P41GM103694 to RDC.

Keywords:

  • Science & Technology
  • Multidisciplinary Sciences
  • Science & Technology - Other Topics
  • INFLAMMATORY-BOWEL-DISEASE
  • MICROARRAY STRATEGY
  • SEROLOGIC MARKERS
  • SERUM ANTIBODIES
  • OVARIAN-CANCER
  • PROSTVAC-VF
  • GLYCOSYLATION
  • IMMUNOASSAY
  • DIAGNOSIS
  • REVEALS

Multiplex glycan bead array for high throughput and high content analyses of glycan binding proteins

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Journal Title:

Nature Communications

Volume:

Volume 9, Number 1

Publisher:

, Pages 258-258

Type of Work:

Article | Final Publisher PDF

Abstract:

Glycan-binding proteins (GBPs) play critical roles in diverse cellular functions such as cell adhesion, signal transduction and immune response. Studies of the interaction between GBPs and glycans have been hampered by the availability of high throughput and high-content technologies. Here we report multiplex glycan bead array (MGBA) that allows simultaneous analyses of 384 samples and up to 500 glycans in a single assay. The specificity, sensitivity and reproducibility of MGBA are evaluated using 39 plant lectins, 13 recombinant anti-glycan antibodies, and mammalian GBPs. We demonstrate the utility of this platform by the analyses of natural anti-glycan IgM and IgG antibodies in 961 human serum samples and the discovery of anti-glycan antibody biomarkers for ovarian cancer. Our data indicate that the MGBA platform is particularly suited for large population-based studies that require the analyses of large numbers of samples and glycans.

Copyright information:

© The Author(s) 2018

This is an Open Access work distributed under the terms of the Creative Commons Attribution 4.0 International License (https://creativecommons.org/licenses/by/4.0/).
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