| A sialylated glycan microarray reveals novel interactions of modified sialic acids with proteins and viruses. | |
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MedLine Citation:
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PMID: 21757734 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Many glycan-binding proteins in animals and pathogens recognize sialic acid or its modified forms, but their molecular recognition is poorly understood. Here we describe studies on sialic acid recognition using a novel sialylated glycan microarray containing modified sialic acids presented on different glycan backbones. Glycans terminating in beta-linked galactose at the non-reducing end and with an alkylamine-containing fluorophore at the reducing end were sialylated by a one-pot-three-enzyme system to generate alpha2-3- and alpha2-6-linked sialyl glycans with 16 modified sialic acids. The resulting 77 sialyl glycans were purified and quantified, characterized by mass spectrometry, covalently printed on activated slides, and interrogated with a number of key sialic acid binding proteins and viruses. Sialic acid recognition by the sialic acid-binding lectins SNA and MAL-I, which are routinely used for detecting alpha2-6- and alpha2-3-linked sialic acids, is affected by sialic acid modifications and both lectins bind glycans terminating with Kdn and Kdn derivatives stronger than the derivatives of more common Neu5Ac and Neu5Gc. Three human parainfluenza viruses bind to glycans terminating with Neu5Ac or Neu5Gc and some of their derivatives, but not to Kdn and its derivatives. Influenza A virus also does not bind glycans terminating in Kdn or Kdn derivatives. An especially novel aspect of human influenza A virus binding is its ability to equivalently recognize glycans terminated with either alpha2-6-linked Neu5Ac9Lt or alpha2-6-linked Neu5Ac. Our results demonstrate the utility of this sialylated glycan microarray to investigate the biological importance of modified sialic acids in protein-glycan interactions. |
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Authors:
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Xuezheng Song; Hai Yu; Xi Chen; Yi Lasanajak; Mary M Tappert; Gillian M Air; Vinod K Tiwari; Hongzhi Cao; Harshal A Chokhawala; Haojie Zheng; Richard D Cummings; David F Smith |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-7-12 |
Journal Detail:
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Title: The Journal of biological chemistry Volume: - ISSN: 1083-351X ISO Abbreviation: - Publication Date: 2011 Jul |
Date Detail:
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Created Date: 2011-7-15 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Emory University, United States; |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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