Comprehensive N-glycosylation profiling of recombinant spike S1 protein from the wild-type SARS-CoV-2 and its variants.

ABSTRACT:

Introduction

By 2024, COVID-19 has become endemic, with new variants contributing to its continued spread. The Spike protein forms trimers that bind to the ACE2 receptor on host cells, with the S1 subunit being a primary target for vaccines and antiviral treatments.

Methods

Herein, we performed an in-depth analysis of the N-glycosylation of the recombinant Spike S1 protein (S1 protein) across the wild-type (WT) virus and its 5 variants, including Alpha, Beta, Gamma, Delta, and Lambda, by integrating ultrahigh-performance liquid chromatography coupled with quadrupole-time-of-flight mass spectrometry (UHPLC-Q-TOF MS) and unique TiO₂-PGC chip-based LC/MS techniques.

Results

A total of 332 glycan structures arising from 180 compositions on the S1 and RBD regions were iden

SUBMITTER: Peng Y 

PROVIDER: S-EPMC12314560 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature