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Glycoconj J. 2011 Dec;28(8-9):501-5. doi: 10.1007/s10719-011-9355-0. Epub 2011 Nov 8.

Profiling of serum antibodies with printed glycan array: room for data misinterpretation.

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Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10, 117997 Moscow, Russia.


Using an example of Galβ1-3GlcNAc (Le(C)) related glycans, we here demonstrate a risk of data misinterpretation when polyclonal antibodies are probed for their glycan-binding specificities with help of a printed glycan array (PGA). Affinity isolation of antibodies from human serum using Le(C)-Sepharose or 3'-O-SuLe(C)-Sepharose in conditions of excess of the adsorbents generated identical material regardless of the affinity ligand, with the antibodies equally capable of binding to Le(C) and to 3'-O-SuLe(C) disaccharides, as well as to 3'-O-SiaLe(C) trisaccharide. More detailed profiling has shown that the isolated antibodies bind to the inner part of Galβ1-3GlcNAc disaccharide. We therefore conclude that serum does not contain different subsets of antibodies specific either to Le(C) or to 3'-O-SuLe(C), despite their visibly different binding signals to these glycans on PGA.

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