SARS-CoV-2 Glycosylation Profiling
The SARS-CoV-2 virus, the causative agent of COVID-19, is heavily glycosylated, with its spike protein in particular adorned with numerous N- and O-glycans. These intricate glycan modifications play a critical role in viral infectivity, immune evasion, and host-pathogen interactions. CD BioGlyco offers advanced SARS-CoV-2 glycosylation profiling services, providing comprehensive analysis of viral glycans to unravel their structural and functional significance. Our profiling services are designed to deliver detailed insights into the glycan landscape of SARS-CoV-2, supporting cutting-edge research.
Background
Coronavirus disease 2019 (COVID-19) pandemic, caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has dramatically impacted human health and the global economy. From the discovery of the virus in early January 2020 to November 2020, the virus has infected more than 60 million people worldwide and caused more than 1.4 million deaths. Understanding virus attachment patterns, entry, and replication has become a critical step in interventions has become a key step in interventions.
The scientific community is still making great efforts to understand the virus in many aspects and compile useful data. The virus uses the spike protein (S protein) to bind angiotensin-converting enzyme 2 (ACE-2) to cause infection. S protein is a highly glycosylated protein, containing 22 N-linked and 3 O-linked glycosylation sites, which is a key protein that affects virus infection and vaccine preparation. Therefore, it has become the focus of attention in academia and industry.
To better understand the variation of S protein and its potential impact on the host immune system, researchers are performing glycosylation profiling, characterizing its changes during the global spread and comparing it with the glycosylation characteristics of SARS-COV.
An In-depth Exploration of Glycosylation Modifications of SARS-CoV-2 Protein
Glycosylation Profiling
We provide the most comprehensive glycomics analysis platform to systematically analyze the coronavirus-related glycoproteins of interest to clients, including glycosylation profiling, comparative characterization (changes in the propagation process and the comparison with the glycosylation characteristics of SARS-COV, etc.), to provide the necessary basis for vaccine development.
- Global glycosylation profiling: Our company offers comprehensive analysis services for the entire N- and O-glycosome of SARS-CoV-2, providing clients with a holistic view of the viral glycosylation landscape.
- Site-specific glycosylation analysis: We provide detailed characterization of glycans attached to specific glycosylation sites on SARS-CoV-2 spike proteins or other viral proteins.
- Comparative glycosylation analysis: Our company provides analysis services for glycosylation patterns between different SARS-CoV-2 variants.
Glycoprotein-related Services
- We provide gene sequences of related proteins of SARS-CoV-2, including spike protein, nucleocapsid protein, papain-like protease, 3CL protease, as well as the related proteins such as various receptors in host cells.
- We have a variety of glycoengineered expression systems, including human embryonic kidney 293 cells (HEK293), Chinese hamster ovary cells (CHO), baby hamster kidney (BHK), Spodoptera frugiperda 21 (SF21), etc., to express SARS-CoV-2-related proteins according to clients' needs.
- We provide lectin-based development services to help clients identify and characterize glycoproteins in the viral envelope or changes in glycoproteins in host cells during viral infection.
Workflow
Our SARS-CoV-2 glycosylation profiling service follows a meticulously designed workflow to ensure comprehensive and reliable results. The main stages of our service process include:
Applications
- Our analysis of glycosylation changes in different SARS-CoV-2 variants helps to track viral evolution and understand its impact on transmissibility and immune escape.
- Our service can be used to study how the host immune system recognizes and responds to viral polysaccharides and how polysaccharides contribute to immune escape mechanisms.
- Our services can be used to analyze the glycosylation protection and immunogenicity of viral spiking proteoglycans, which is essential for designing more effective and broadly protective vaccines.
Advantages of Us
- Our team comprises highly experienced glycomic scientists with extensive knowledge in viral glycosylation and advanced analytical techniques. We leverage this expertise to provide precise and insightful data.
- Every step of our workflow is subject to stringent quality control measures, from sample preparation to data analysis, guaranteeing the accuracy and reproducibility of our results.
- We understand that each research project is unique. Our services are highly customizable to meet specific experimental designs and objectives, from routine profiling to complex structural elucidation.
Publication Data
Technology: Cryo-electron microscopy (cryo-EM)
Journal: Nature Communications
Published: 2020
IF: 14.7
Results: This paper utilizes single-particle cryo-electron microscopy to deeply analyze the structure of SARS-CoV spiking proteins after fusion, revealing the structure of the highly rotated HR1-HR2 six-helix bundle formed by the S2 subunit and its upstream tightly bound junction region. The study not only found that the structure of SARS-CoV S2 after fusion was significantly different from that before fusion and similar to that of class I viral fusion proteins such as mouse hepatitis virus, but also elucidated the structural rearrangement and conformational changes experienced by the S2 subunit during the fusion process, in particular the promotion of fusion peptide ejection by the extension of the HR1-CH helical region. In addition, the extensive structural rearrangement of the linker region during the fusion process and its critical role in the formation of the six-helix bundle, as well as the finding that glycosylation modifications in the S2 post-fusion structure may help the virus evade immune attack. These findings provide an important structural basis and potential targets for the development of vaccines and therapeutics against widespread SARS-like coronaviruses.
Fig.1 Structural and conformational changes in the SARS-CoV S glycoprotein from pre- to post-fusion. (Fan, et al., 2020)
Frequently Asked Questions
CD BioGlyco is committed to developing various technology platforms to help scientists around the world explore the coronavirus and promote the global vaccine development process. CD BioGlyco has professional teams and ultra-high-precision instruments. We are confident that we can provide customers with high-quality viral glycomics research.
Clients can reach our scientists directly via email or phone to receive prompt response. If you are interested in our services, please contact us for more detailed information.
Associated Services
Reference
- Fan, X.; et al. Cryo-EM analysis of the post-fusion structure of the SARS-CoV spike glycoprotein. Nature Communications. 2020, 11(1): 3618. (Open Access)
