Book chapter
Modification of N-Linked Glycan Sites in Viral Glycoproteins
Recombinant Glycoproteins, pp.27-41
Methods in molecular biology (Clifton, N.J.), v. 2762, Humana
2024
DOI: 10.1007/978-1-0716-3666-4_3
PMID: 38315358
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.
Details
- Title: Subtitle
- Modification of N-Linked Glycan Sites in Viral Glycoproteins
- Creators
- Nicholas J Lennemann - University of Alabama at BirminghamLochlain Corliss - University of Alabama at BirminghamWendy Maury - University of Iowa
- Resource Type
- Book chapter
- Publication Details
- Recombinant Glycoproteins, pp.27-41
- Publisher
- Humana; New York, NY
- Series
- Methods in molecular biology (Clifton, N.J.); v. 2762
- DOI
- 10.1007/978-1-0716-3666-4_3
- PMID
- 38315358
- eISBN
- 1071636669; 9781071636664
- ISSN
- 1064-3745
- eISSN
- 1940-6029
- Language
- English
- Date published
- 2024
- Academic Unit
- Microbiology and Immunology
- Record Identifier
- 9984557946302771
Metrics
4 Record Views