4.2 Article

Comparison of printed glycan array, suspension array and ELISA in the detection of human anti-glycan antibodies

Journal

GLYCOCONJUGATE JOURNAL
Volume 28, Issue 8-9, Pages 507-517

Publisher

SPRINGER
DOI: 10.1007/s10719-011-9349-y

Keywords

Glycan array; Carbohydrate; Multiplex assay; Ovarian cancer

Funding

  1. Oncosuisse [02115-08-2007]
  2. Swiss National Foundation [320000-12543, PBZHP3-133289]
  3. European Science Foundation
  4. Cancer Institute NSW [09/CRF/2-02]
  5. RANZCOG
  6. William Maxwell Trust
  7. Cellexicon, Inc. La Jolla, CA, USA
  8. National Cancer Institute, USA [1U01CA128526]
  9. RAS Presidium
  10. [2011-1.2-512-013-008]
  11. Swiss National Science Foundation (SNF) [PBZHP3-133289] Funding Source: Swiss National Science Foundation (SNF)

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Anti-glycan antibodies represent a vast and yet insufficiently investigated subpopulation of naturally occurring and adaptive antibodies in humans. Recently, a variety of glycan-based microarrays emerged, allowing high-throughput profiling of a large repertoire of antibodies. As there are no direct approaches for comparison and evaluation of multi-glycan assays we compared three glycan-based immunoassays, namely printed glycan array (PGA), fluorescent microsphere-based suspension array (SA) and ELISA for their efficacy and selectivity in profiling anti-glycan antibodies in a cohort of 48 patients with and without ovarian cancer. The ABO blood group glycan antigens were selected as well recognized ligands for sensitivity and specificity assessments. As another ligand we selected P-1, a member of the P blood group system recently identified by PGA as a potential ovarian cancer biomarker. All three glyco-immunoassays reflected the known ABO blood groups with high performance. In contrast, anti-P-1 antibody binding profiles displayed much lower concordance. Whilst anti-P-1 antibody levels between benign controls and ovarian cancer patients were significantly discriminated using PGA (p = 0.004), we got only similar results using SA (p = 0.03) but not for ELISA. Our findings demonstrate that whilst assays were largely positively correlated, each presents unique characteristic features and should be validated by an independent patient cohort rather than another array technique. The variety between methods presumably reflects the differences in glycan presentation and the antigen/antibody ratio, assay conditions and detection technique. This indicates that the glycan-antibody interaction of interest has to guide the assay selection.

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