Cross-comparison of protein recognition of sialic acid diversity on two novel sialoglycan microarrays.
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Cross-comparison of protein recognition of sialic acid diversity on two novel sialoglycan microarrays. / Padler-Karavani, Vered; Song, Xuezheng; Yu, Hai; Hurtado-Ziola, Nancy; Huang, Shengshu; Muthana, Saddam; Chokhawala, Harshal A; Cheng, Jiansong; Verhagen, Andrea; Langereis, Martijn A; Kleene, Ralf; Schachner, Melitta; Groot, de; Raoul, J; Lasanajak, Yi; Matsuda, Haruo; Schwab, Richard; Chen, Xi; Smith, David F; Cummings, Richard D; Varki, Ajit.
in: J BIOL CHEM, Jahrgang 287, Nr. 27, 27, 2012, S. 22593-22608.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Cross-comparison of protein recognition of sialic acid diversity on two novel sialoglycan microarrays.
AU - Padler-Karavani, Vered
AU - Song, Xuezheng
AU - Yu, Hai
AU - Hurtado-Ziola, Nancy
AU - Huang, Shengshu
AU - Muthana, Saddam
AU - Chokhawala, Harshal A
AU - Cheng, Jiansong
AU - Verhagen, Andrea
AU - Langereis, Martijn A
AU - Kleene, Ralf
AU - Schachner, Melitta
AU - Groot, de
AU - Raoul, J
AU - Lasanajak, Yi
AU - Matsuda, Haruo
AU - Schwab, Richard
AU - Chen, Xi
AU - Smith, David F
AU - Cummings, Richard D
AU - Varki, Ajit
PY - 2012
Y1 - 2012
N2 - DNA and protein arrays are commonly accepted as powerful exploratory tools in research. This has mainly been achieved by the establishment of proper guidelines for quality control, allowing cross-comparison between different array platforms. As a natural extension, glycan microarrays were subsequently developed, and recent advances using such arrays have greatly enhanced our understanding of protein-glycan recognition in nature. However, although it is assumed that biologically significant protein-glycan binding is robustly detected by glycan microarrays, there are wide variations in the methods used to produce, present, couple, and detect glycans, and systematic cross-comparisons are lacking. We address these issues by comparing two arrays that together represent the marked diversity of sialic acid modifications, linkages, and underlying glycans in nature, including some identical motifs. We compare and contrast binding interactions with various known and novel plant, vertebrate, and viral sialic acid-recognizing proteins and present a technical advance for assessing specificity using mild periodate oxidation of the sialic acid chain. These data demonstrate both the diversity of sialic acids and the analytical power of glycan arrays, showing that different presentations in different formats provide useful and complementary interpretations of glycan-binding protein specificity. They also highlight important challenges and questions for the future of glycan array technology and suggest that glycan arrays with similar glycan structures cannot be simply assumed to give similar results.
AB - DNA and protein arrays are commonly accepted as powerful exploratory tools in research. This has mainly been achieved by the establishment of proper guidelines for quality control, allowing cross-comparison between different array platforms. As a natural extension, glycan microarrays were subsequently developed, and recent advances using such arrays have greatly enhanced our understanding of protein-glycan recognition in nature. However, although it is assumed that biologically significant protein-glycan binding is robustly detected by glycan microarrays, there are wide variations in the methods used to produce, present, couple, and detect glycans, and systematic cross-comparisons are lacking. We address these issues by comparing two arrays that together represent the marked diversity of sialic acid modifications, linkages, and underlying glycans in nature, including some identical motifs. We compare and contrast binding interactions with various known and novel plant, vertebrate, and viral sialic acid-recognizing proteins and present a technical advance for assessing specificity using mild periodate oxidation of the sialic acid chain. These data demonstrate both the diversity of sialic acids and the analytical power of glycan arrays, showing that different presentations in different formats provide useful and complementary interpretations of glycan-binding protein specificity. They also highlight important challenges and questions for the future of glycan array technology and suggest that glycan arrays with similar glycan structures cannot be simply assumed to give similar results.
KW - Reproducibility of Results
KW - Antigens, CD/metabolism
KW - Cell Adhesion Molecules/metabolism
KW - Antibody Specificity
KW - Oxidation-Reduction
KW - Lectins/metabolism
KW - Acetylation
KW - Antibodies/immunology
KW - Glycolipids/immunology/metabolism
KW - Glycomics/instrumentation/methods/standards
KW - N-Acetylneuraminic Acid/immunology/metabolism
KW - Periodic Acid/metabolism
KW - Plant Lectins/metabolism
KW - Polysaccharides/immunology/metabolism
KW - Protein Array Analysis/instrumentation/methods/standards
KW - Reproducibility of Results
KW - Antigens, CD/metabolism
KW - Cell Adhesion Molecules/metabolism
KW - Antibody Specificity
KW - Oxidation-Reduction
KW - Lectins/metabolism
KW - Acetylation
KW - Antibodies/immunology
KW - Glycolipids/immunology/metabolism
KW - Glycomics/instrumentation/methods/standards
KW - N-Acetylneuraminic Acid/immunology/metabolism
KW - Periodic Acid/metabolism
KW - Plant Lectins/metabolism
KW - Polysaccharides/immunology/metabolism
KW - Protein Array Analysis/instrumentation/methods/standards
M3 - SCORING: Journal article
VL - 287
SP - 22593
EP - 22608
JO - J BIOL CHEM
JF - J BIOL CHEM
SN - 0021-9258
IS - 27
M1 - 27
ER -
