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

Pochechueva, Tatiana ; Jacob, Francis ; Goldstein, Darlene ; Huflejt, Margaret ; Chinarev, Alexander ; Caduff, Rosemarie ; Fink, Daniel ; Hacker, Neville ; Bovin, Nicolai ; Heinzelmann-Schwarz, Viola

In: Glycoconjugate Journal, 2011, vol. 28, no. 8-9, p. 507-517

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    Titre
    • Comparison of printed glycan array, suspension array and ELISA in the detection of human anti-glycan antibodies
    Auteur
    • Pochechueva, Tatiana. Translational Research Group, University Hospital Zurich, Zurich, Switzerland
    • Jacob, Francis. Translational Research Group, University Hospital Zurich, Zurich, Switzerland
    • Goldstein, Darlene. Institut de Mathématiques, Ecole Polytéchnique Fédérale, Lausanne, Switzerland
    • Huflejt, Margaret. Department of Cardiothoracic Surgery, Division of Thoracic Surgery and Thoracic Oncology, New York University School of Medicine, New York, NY, USA
    • Chinarev, Alexander. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russian Federation
    • Caduff, Rosemarie. Institute of Clinical Pathology, University Hospital Zurich, Zurich, Switzerland
    • Fink, Daniel. Department of Gynecology, University Hospital Zurich, Zurich, Switzerland
    • Hacker, Neville. Gynecological Cancer Centre, Royal Hospital for Women and School of Women's and Children's Health, Sydney, Australia
    • Bovin, Nicolai. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russian Federation
    • Heinzelmann-Schwarz, Viola. Translational Research Group, University Hospital Zurich, Zurich, Switzerland
    Type de document
    • Postprint
    Langue
    • Anglais
    Publié dans
    • Glycoconjugate Journal, 2011, vol. 28, no. 8-9, p. 507-517. Springer US; http://www.springer-ny.com
    Autre version électronique
    Identifiant OAI-PMH
    • oai:doc.rero.ch:320287
    Summary
    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 P1, 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-P1 antibody binding profiles displayed much lower concordance. Whilst anti-P1 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