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Author Notes:

To whom correspondence may be addressed: Emory University School of Medicine, Atlanta, GA 30322. Tel.: 404-727-5962; Fax: 404-727-2738; E-mail: rdcummi@emory.edu.

The contributions of the first two authors are equal.

We thank Jamie Heimburg-Molinaro (Emory University School of Medicine) for help in data management and manuscript preparation.

A. Varki is a cofounder of Sialix, Inc. (formerly Gc-Free, Inc.).

N. Hurtado-Ziola is currently an employee of Sialix, Inc.


Research Funding:

This work was supported, in whole or in part, by National Institutes of Health Grants R01GM32373 and U01 CA128442 (to A. V.), RO1GM085448 (to D. F. S.), and R01GM076360 (to X. C.) and a bridging grant from the Consortium for Functional Glycomics under National Institutes of Health, NIGMS, Grant GM62116 (to R. D. C.).

This work was also supported by an International Sepharadic Education Foundation postdoctoral fellowship (to V. P.-K.) and Defense Advanced Research Projects Agency Grant HR0011-10-00 (to R. D. C.).


  • Antibodies
  • Antigen
  • Carbohydrate
  • Carbohydrate-binding Protein
  • Glycobiology
  • Glycomics
  • Microarray
  • Sialic Acid
  • Cross-comparison
  • Glycan Microarray

Cross-comparison of Protein Recognition of Sialic Acid Diversity on Two Novel Sialoglycan Microarrays

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Journal Title:

Journal of Biological Chemistry


Volume 287, Number 27


, Pages 22593-22608

Type of Work:

Article | Final Publisher PDF


Background: Various glycan microarrays are currently widely used, but systematic cross-comparisons are lacking. Results: We compare and contrast two sialoglycan microarrays using a variety of sialic acid-binding proteins. Conclusion: Diverse array formats can strengthen the quality of information, but differences between arrays may be observed. Significance: Glycan arrays with similar glycan structures cannot be simply assumed to give similar results.

Copyright information:

© 2012 by The American Society for Biochemistry and Molecular Biology, Inc.

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