A library of mutated Maackia amurensis hemagglutinin distinguishes putative glycoforms of immunoglobulin A1 from IgA nephropathy patients

Keisuke Maenuma, Mijung Yim, Kunimitsu Komatsu, Mayumi Hoshino, Ayumi Tachiki-Fujioka, Kazuo Takahashi, Yoshiyuki Hiki, Nicolai Bovin, Tatsuro Irimura

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)

Abstract

Ten genetically modified Maackia amurensis hemagglutinin (MAH) clones at the carbohydrate-recognition loop were found to bind glycophorin A and a mucin mimetic with NeuAcα2-3Galβ1-3GalNAcα (monosialyl-T antigen) in different relative intensity. Binding profiles of these lectins to human serum IgA1 from healthy individuals and from IgA nephropathy patients were subjected to the cluster analysis. Two large groups, one with only healthy individuals and another with all IgA nephropathy patients, were generated. The results strongly suggest that the library of genetically modified MAH is a useful tool for serum diagnosis of IgA nephropathy.

Original languageEnglish
Pages (from-to)3617-3624
Number of pages8
JournalJournal of Proteome Research
Volume8
Issue number7
DOIs
Publication statusPublished - 06-07-2009

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • General Chemistry

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