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Chemically-blocked Antibody Microarray for Multiplexed High-throughput Profiling of Specific Protein Glycosylation in Complex Samples
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Chemically-blocked Antibody Microarray for Multiplexed High-throughput Profiling of Specific Protein Glycosylation in Complex Samples

Published on: May 4, 2012

High-throughput carbohydrate microarray profiling of 27 antibodies demonstrates widespread specificity problems.

Joseph C Manimala1, Timothy A Roach, Zhitao Li

  • 1Laboratory of Medicinal Chemistry, Center for Cancer Research, National Cancer Institute, 376 Boyles Street, Building 376, Room 109, Frederick, MD 21702, USA.

Glycobiology
|May 8, 2007
PubMed
Summary

Many carbohydrate-specific antibodies cross-react with unintended targets, leading to inaccurate diagnostic conclusions. This study evaluated antibody specificities, revealing significant cross-reactivity issues in glycan and glycoprotein research.

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Area of Science:

  • Glycobiology
  • Immunology
  • Biochemistry

Background:

  • Understanding carbohydrate biology is crucial for diagnostics and therapeutics but remains challenging.
  • Current methods for monitoring carbohydrate expression rely heavily on antibody and lectin binding.
  • Significant limitations exist in the specificity of antibodies used in glycan research.

Purpose of the Study:

  • To evaluate the specificities of 27 antiglycan antibodies against a diverse carbohydrate microarray.
  • To identify cross-reactivity issues among antibodies targeting histo-blood group, Lewis, and tumor-associated antigens.
  • To assess the reliability of current antibody-based methods for carbohydrate expression analysis.

Main Methods:

  • Utilized a carbohydrate microarray with 80 different glycans and glycoproteins.
  • Tested the binding specificities of 27 antiglycan antibodies, including those for histo-blood group, Lewis, and tumor-associated antigens.
  • Analyzed over 2000 individual carbohydrate-protein interactions to determine antibody cross-reactivity.

Main Results:

  • Over half of the antibodies tested showed cross-reactivity with glycans other than their intended targets.
  • Identified significant cross-reactivity among antibodies for histo-blood group A, B, and H antigens.
  • Demonstrated cross-reactivity in antibodies targeting Lewis antigens and other tumor-associated antigens.

Conclusions:

  • The high prevalence of antibody cross-reactivity challenges the accuracy of current glycan detection methods.
  • Misidentification of antigens due to cross-reactive glycans can lead to erroneous conclusions in clinical and basic research.
  • Re-evaluation of antibody specificities is essential for reliable carbohydrate-based diagnostics and therapeutics.