English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Noncovalent microarrays from synthetic amino-terminating glycans : implications in expanding glycan microarray diversity and platform comparison

Li, C., Palma, A. S., Zhang, P., Zhang, Y., Gao, C., Silva, L. M., et al. (2021). Noncovalent microarrays from synthetic amino-terminating glycans: implications in expanding glycan microarray diversity and platform comparison. Glycobiology, 31(8), 931-946. doi:10.1093/glycob/cwab037.

Item is

Basic

show hide
Genre: Journal Article

Files

show Files
hide Files
:
Article.pdf (Publisher version), 2MB
Name:
Article.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-

Locators

show

Creators

show
hide
 Creators:
Li, Chunxia, Author
Palma, Angelina S., Author
Zhang, Pengtao, Author
Zhang, Yibing, Author
Gao, Chao, Author
Silva, Lisete M., Author
Li, Zhen, Author
Trovão, Filipa, Author
Weishaupt, Markus W.1, Author              
Seeberger, Peter H.1, Author              
Likhosherstov, Leonid M., Author
Piskarev, Vladimir, Author
Yu, Jin, Author
Westerlind, Ulrika, Author
Chai, Wengang, Author
Affiliations:
1Peter H. Seeberger - Automated Systems, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863306              

Content

show
hide
Free keywords: neoglycolipid; glycan microarray, oligosaccharide microarray, Dectin-1, rotavirus
 Abstract: Glycan microarrays have played important roles in detection and specificity assignment of glycan-recognition by proteins. However, the size and diversity of glycan libraries in current microarray systems are small compared to estimated glycomes, and these may lead to missed detection or incomplete assignment. For microarray construction, covalent and non-covalent immobilization are the two types of methods used, but a direct comparison of results from the two platforms is required. Here we develop a chemical strategy to prepare lipid-linked probes from both naturally-derived aldehyde-terminating and synthetic amino-terminating glycans that addresses the two aspects: expansion of sequence-defined glycan libraries and comparison of the two platforms. We demonstrate the specific recognition by plant and mammalian lectins, carbohydrate-binding modules and antibodies, and the overall similarities from the two platforms. Our results provide new knowledge on unique glycan-binding specificities for the immune-receptor Dectin-1 towards β-glucans and the interaction of rotavirus P[19] adhesive protein with mucin O-glycan cores.

Details

show
hide
Language(s): eng - English
 Dates: 2021-05-082021
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1093/glycob/cwab037
BibTex Citekey: 10.1093/glycob/cwab037
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Glycobiology
  Other : Glycobiology
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Oxford : Oxford University Press
Pages: - Volume / Issue: 31 (8) Sequence Number: - Start / End Page: 931 - 946 Identifier: ISSN: 0959-6658