Back to Search
Start Over
Terminal Epitope-Dependent Branch Preference of Siglecs Toward N-Glycans
- Source :
- Frontiers in Molecular Biosciences, Frontiers in Molecular Biosciences, Vol 8 (2021)
- Publication Year :
- 2021
- Publisher :
- Frontiers Media S.A., 2021.
-
Abstract
- Siglecs are sialic acid–binding immunoglobulin-like lectins that play vital roles in immune cell signaling. Siglecs help the immune system distinguish between self and nonself through the recognition of glycan ligands. While the primary binding specificities of Siglecs are known to be divergent, their specificities for complex glycans remain unclear. Herein, we determined N-glycan binding profiles of a set of Siglecs by using a complex asymmetric N-glycan microarray. Our results showed that Siglecs had unique terminal epitope-dependent branch preference when recognizing asymmetric N-glycans. Specifically, human Siglec-3, -9, and -10 prefer the α1-3 branch when Siaα2-6Galβ1-4GlcNAc terminal epitope serves as the binding ligand but prefer the opposite α1-6 branch when Siaα2-3Galβ1-4GlcNAc epitope serves as the ligand. Interestingly, Siglec-10 exhibited dramatic binding divergence toward a pair of Neu5Ac-containing asymmetric N-glycan isomers, as well as their Neu5Gc-containing counterparts. This new information on complex glycan recognition by Siglecs provides insights into their biological roles and applications.
- Subjects :
- 0301 basic medicine
Cell signaling
Glycan
QH301-705.5
Computational biology
Neu5Gc
010402 general chemistry
01 natural sciences
Biochemistry, Genetics and Molecular Biology (miscellaneous)
Biochemistry
Epitope
03 medical and health sciences
Molecular Biosciences
Biology (General)
Molecular Biology
Original Research
biology
Chemistry
Ligand
respiratory system
0104 chemical sciences
carbohydrates (lipids)
030104 developmental biology
Terminal (electronics)
Siglecs
Neu5Ac
biology.protein
asymmetric N-glycan
microarray
Subjects
Details
- Language :
- English
- ISSN :
- 2296889X
- Volume :
- 8
- Database :
- OpenAIRE
- Journal :
- Frontiers in Molecular Biosciences
- Accession number :
- edsair.doi.dedup.....aebe6acc596c1659ecbeffe0a1a88a7f