Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 114, Issue 27, Pages 6954-6959Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1701785114
Keywords
chemoenzymatic synthesis; glycosyltransferases; protein-glycan interactions; human milk oligosaccharides
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Funding
- National Institute of General Medical Sciences [R01GM090269, P01GM107012, P41GM103390]
- National Heart, Lung, and Blood Institute [P01HL107150]
- National Cancer Institute [F31CA180478]
- US National Institutes of Health (NIH)
- NIH [S10RR027097]
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Despite mammalian glycans typically having highly complex asymmetrical multiantennary architectures, chemical and chemo-enzymatic synthesis has almost exclusively focused on the preparation of simpler symmetrical structures. This deficiency hampers investigations into the biology of glycan-binding proteins, which in turn complicates the biomedical use of this class of biomolecules. Herein, we describe an enzymatic strategy, using a limited number of human glycosyltransferases, to access a collection of 60 asymmetric, multiantennary human milk oligosaccharides (HMOs), which were used to develop a glycan microarray. Probing the array with several glycan-binding proteins uncovered that not only terminal glycoepitopes but also complex architectures of glycans can influence binding selectivity in unanticipated manners. N- and O-linked glycans express structural elements of HMOs, and thus, the reported synthetic principles will find broad applicability.
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