Unique Binding Specificities of Proteins toward Isomeric Asparagine-Linked Glycans.

Abstract:

:The glycan ligands recognized by Siglecs, influenza viruses, and galectins, as well as many plant lectins, are not well defined. To explore their binding to asparagine (Asn)-linked N-glycans, we synthesized a library of isomeric multiantennary N-glycans that vary in terminal non-reducing sialic acid, galactose, and N-acetylglucosamine residues, as well as core fucose. We identified specific recognition of N-glycans by several plant lectins, human galectins, influenza viruses, and Siglecs, and explored the influence of sialic acid linkages and branching of the N-glycans. These results show the unique recognition of complex-type N-glycans by a wide variety of glycan-binding proteins and their abilities to distinguish isomeric structures, which provides new insights into the biological roles of these proteins and the uses of lectins in biological applications to identify glycans.

journal_name

Cell Chem Biol

journal_title

Cell chemical biology

authors

Gao C,Hanes MS,Byrd-Leotis LA,Wei M,Jia N,Kardish RJ,McKitrick TR,Steinhauer DA,Cummings RD

doi

10.1016/j.chembiol.2019.01.002

subject

Has Abstract

pub_date

2019-04-18 00:00:00

pages

535-547.e4

issue

4

eissn

2451-9456

issn

2451-9448

pii

S2451-9456(19)30002-9

journal_volume

26

pub_type

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