Multiplex profiling of glycoproteins using a novel bead-based lectin array

Authors

  • Hong Wang,

    1. Department of Chemistry, Fudan University, Shanghai, China
    2. Institutes of Biomedical Sciences, Fudan University, Shanghai, China
    3. Shanghai Institute for food and drug control, Shanghai, China
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    • These authors contributed equally to this work.

  • Hong Li,

    1. Department of Chemistry, Fudan University, Shanghai, China
    2. Institutes of Biomedical Sciences, Fudan University, Shanghai, China
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    • These authors contributed equally to this work.

  • Wei Zhang,

    1. Department of Chemistry, Fudan University, Shanghai, China
    2. Institutes of Biomedical Sciences, Fudan University, Shanghai, China
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  • Liming Wei,

    1. Institutes of Biomedical Sciences, Fudan University, Shanghai, China
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  • Hongxiu Yu,

    Corresponding author
    1. Institutes of Biomedical Sciences, Fudan University, Shanghai, China
    • Correspondence: Dr. Hongxiu Yu, Institutes of Biomedical Sciences, Fudan University, 138 Yi Xueyuan Road, Shanghai, 200032, China

      E-mail: hongxiuyu@fudan.edu.cn

      Fax: +86 21 5423-7961

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  • Pengyuan Yang

    1. Department of Chemistry, Fudan University, Shanghai, China
    2. Institutes of Biomedical Sciences, Fudan University, Shanghai, China
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  • Colour Online: See the article online to view Figs. 1 and 4 in colour

Abstract

Lectin array is becoming important in profiling targeted glycan/glycoprotein, but weak interaction between lectin and glycan causes low sensitivity of the approach. This study aims to develop a bead-based lectin array for improving the sensitivity of glycosylation profiling. Lectins are chemically coupled to fluorescent dye coated microbeads, and glycan-lectin recognition is carried out three dimensionally. The performance of this platform was evaluated, and the LOD of lectin Ricinus communis agglutinin 120 (RCA120) was 50 pg/mL (1 pM) of asialofetuin, providing the bead-based lectin microarray with the highest sensitivity among the reported lectin microarrays. Furthermore, multiplexed assay was performed, which allowed the simultaneous detection of multiple carbohydrate epitopes in a single reaction vessel. The glycosylation patterns of hepatocellular carcinoma associated immunoglobulin G were analyzed, and increased (α-1,6) core fucosylation and (α-2,6) sialylation patterns were observed, which may provide significant clinical evidence for disease diagnosis.

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