AI Article Synopsis
- * The study utilized a new sequencing algorithm called StrucGP to analyze the glycosylation of the S protein at specific sites, revealing both common and uncommon glycan structures.
- * A total of 20 glycosites in the S protein were identified, providing deeper insight into the structural and functional role of glycosylation in the COVID-19 virus.
Article Abstract
The spike (S) protein plays a key role in COVID-19 (SARS-CoV-2) infection and host-cell entry. Previous studies have systematically analyzed site-specific glycan compositions as well as many important structural motifs of the S protein. Here, we further provide structural-clear glycosylation of the S protein at a site-specific level by using our recently developed structural- and site-specific glycoproteomics sequencing algorithm, StrucGP. In addition to the common glycans as detected in previous studies, many uncommon glycosylation structures such as LacdiNAc structures, Lewis structures, Mannose 6-phosphate (M6P) residues, and bisected core structures were unambiguously mapped at a total of 20 glycosites in the S protein trimer and protomer. These data further support the glycosylation structural-functional investigations of the COVID-19 virus spike.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1021/acs.analchem.2c02265 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!