Lipochitin Oligosaccharides Immobilized through Oximes in Glycan Microarrays Bind LysM Proteins

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  • Nicolai Nareth Maolanon, LUKKET: 2012 Nanobiovidenskab, Denmark
  • Mickael Blaise, Denmark
  • Kasper K Sørensen, Department of Chemistry, Faculty of Science, University of Copenhagen, Denmark
  • Mikkel B Thygesen, Department of Chemistry, Faculty of Science, University of Copenhagen, Denmark
  • Emiliano Cló, Department of Chemistry, Faculty of Science, University of Copenhagen, Denmark
  • John T Sullivan, Department of Microbiology and Immunology, University of Otago, New Zealand
  • Clive W Ronson, Department of Microbiology and Immunology, University of Otago, New Zealand
  • Jens Stougaard
  • Klas Ola Blixt, Department of Chemistry, Faculty of Science, University of Copenhagen, Denmark
  • Knud J Jensen, Department of Chemistry, Faculty of Science, University of Copenhagen, Denmark
Glycan microarrays have emerged as novel tools to study carbohydrate-protein interactions. Here we describe the preparation of a covalent microarray with lipochitin oligosaccharides and its use in studying proteins containing LysM domains. The glycan microarray was assembled from glycoconjugates that were synthesized by using recently developed bifunctional chemoselective aminooxy reagents without the need for transient carbohydrate protecting groups. We describe for the first time the preparation of a covalent microarray with lipochitin oligosaccharides and its use for studying proteins containing LysM domains. Lipochitin oligosaccharides (also referred to as Nod factors) were isolated from bacterial strains or chemoenzymatically synthesized. The glycan microarray also included peptidoglycan-related compounds, as well as chitin oligosaccharides of different lengths. In total, 30 ligands were treated with the aminooxy linker molecule. The identity of the glycoconjugates was verified by mass spectrometry, and they were then immobilized on the array. The presence of the glycoconjugates on the array surface was confirmed by use of lectins and human sera (IgG binding). The functionality of our array was tested with a bacterial LysM domain-containing protein, autolysin p60, which is known to act on the bacterial cell wall peptidoglycan. P60 showed specific binding to Nod factors and to chitin oligosaccharides. Increasing affinity was observed with increasing chitin oligomer length.
Original languageEnglish
JournalChemBioChem
Volume15
Issue3
Pages (from-to)425-434
Number of pages10
ISSN1439-4227
DOIs
Publication statusPublished - 10 Feb 2014

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