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Modification of N-Linked Glycan Sites in Viral Glycoproteins.

Authors :
Lennemann NJ
Corliss L
Maury W
Source :
Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2024; Vol. 2762, pp. 27-41.
Publication Year :
2024

Abstract

Post-translational modification of proteins by the addition of sugar chains, or glycans, is a functionally important hallmark of proteins trafficked through the secretory system. These proteins are termed glycoproteins. Glycans are known to be important for initiating signaling through binding of cell surface receptors, facilitating protein folding, and maintaining protein stability. For pathogens, glycans can also mask vulnerable protein regions from neutralizing antibodies. Thus, there is a need to develop methods to decipher the role of specific glycans attached to proteins in order to understand their biological role. Here, we describe established methods for identifying glycosylated residues and understanding their role in protein synthesis and function using viral glycoproteins as a model.<br /> (© 2024. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.)

Details

Language :
English
ISSN :
1940-6029
Volume :
2762
Database :
MEDLINE
Journal :
Methods in molecular biology (Clifton, N.J.)
Publication Type :
Academic Journal
Accession number :
38315358
Full Text :
https://doi.org/10.1007/978-1-0716-3666-4_3