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Peptidoglycan microarray as a novel tool to explore protein–ligand recognition
Author(s) -
Wang Ning,
Hirata Akiyoshi,
Nokihara Kiyoshi,
Fukase Koichi,
Fujimoto Yukari
Publication year - 2016
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22807
Subject(s) - peptidoglycan , cell wall , bacterial cell structure , chemistry , biochemistry , microbiology and biotechnology , biology , bacteria , genetics
ABSTRACT Peptidoglycan is a giant bag‐shaped molecule essential for bacterial cell shape and resistance to osmotic stresses. The activity of a large number of bacterial surface proteins involved in cell growth and division requires binding to this macromolecule. Recognition of peptidoglycan by immune effectors is also crucial for the establishment of the immune response against pathogens. The availability of pure and chemically defined peptidoglycan fragments is a major technical bottleneck that has precluded systematic studies of the mechanisms underpinning protein‐mediated peptidoglycan recognition. Here, we report a microarray strategy suitable to carry out comprehensive studies to characterize proteins–peptidoglycan interactions. We describe a method to introduce a functional group on peptidoglycan fragments allowing their stable immobilization on amorphous carbon chip plates to minimize nonspecific binding. Such peptidoglycan microarrays were used with a model peptidoglycan binding protein—the human peptidoglycan recognition protein‐S (hPGRP‐S). We propose that this strategy could be implemented to carry out high‐throughput analyses to study peptidoglycan binding proteins. © 2016 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 106: 422–429, 2016.