Glycosylation Analysis Services for Virus Glyoprotein
Glycosylation of Virus Glycoprotein
Enveloped viruses, including SARS-CoV, Hepatitis C virus (HCV), HIV, Influenza virus, Ebola virus, and more, often cause a wide range of infections in humans, varying from mild to severe diseases. These viruses possess enveloped glycoproteins that are essential for viral infectivity, immune recognition, and immune evasion. Viral surface proteins undergo glycosylation during the cellular secretory pathway, resulting in heterogeneous glycan structures and differing numbers of glycosylation sites across different hosts and classes of viruses. Viral glycosylation is vital for maintaining the structural stability and functionality of viral glycoproteins and plays a critical role in virus biology, including viral attachment and entry, viral particle formation and release, immune recognition, and responses. Altering glycosylation sites or the presence or absence of glycans have significant impacts on viral lifecycle. Throughout viral evolution, glycosylation sites are frequently added or removed, increasing the diversity and complexity of viral glycoproteins in different hosts. Comprehensive analysis of the glycosylation patterns in viral envelope glycoproteins is fundamental for advancing viral biology research and the development of vaccines and antiviral treatments.
Fig.1 Roles of glycosylation in the biology of enveloped viruses.1
Technology Platforms for Viral Glycosylation Analysis at Creative Biolabs
The advancements in high-resolution tandem mass spectrometry have revolutionized the sensitive detection and thorough analysis of glycosylation on viral envelope glycoproteins. Creative Biolabs leverages these cutting-edge technologies to offer in-depth glycosylation analysis of virus glycoproteins across different classes of viruses and hosts. Our services encompass structural identification of glycans, site-specific glycan characterization, monitoring changes in glycan heterogeneity, site occupancy, and glycosylation site location.
Our use of MALDI TOF-TOF MS and fragmentation techniques like HCD and ETD allows us to simultaneously determine the peptide sequence and the specific attachment site of glycans, ensuring high confidence in glycosylation site localization. Additionally, the combination of MALDI-MS/MS with lectin microarray enhances the reliability of glycan structure characterization, as lectin binding profiles offer valuable information into glycosidic linkages. Through our MS-based detection and analysis, we deliver comprehensive insights into viral glycosylation.
Characterization of Viral Glycosylation at Creative Biolabs
Characterization of viral glycoproteins involves various levels of glycoprofiling, each providing critical insights into glycan patterns and their functional significance.
Released glycan profiles
Glycan profiling has been used to compare various N- and O-glycan patterns from different pathogenic viruses and different expression systems to explore potential implications for immune responses in vaccines.
Glycan site localization
Determination of specific glycosylation sites is crucial to identify glycan sites essential for protein function, especially for viral glycoproteins with numerous potential glycosylation sites, such as HIV-1 Env, and influenza HA.
Glycan site occupancy
Determining glycan site occupancy is vital for viral glycosylation analysis, especially for proteins with many glycosylation sites, some sites may remain unoccupied, potentially influencing protein function. High site occupancy rates (>90%) were reported in influenza HA.
Site-specific glycan profiles
Site-specific glycosylation analysis is particularly valuable for heavily glycosylated viral glycoproteins, providing detailed information on glycan patterns contributed to viral fitness, such as immune evasion or viral entry.
Glycosylation Analysis Services for Various Viruses
With advanced analytical platforms for viral glycosylation, Creative Biolabs offers comprehensive glycosylation analysis for glycoproteins from various classes of viruses, which includes:
Applications of Viral Glycosylation Analysis
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Viral structure and function studies
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Integrating glycosylation profiling with complementary techniques is a powerful approach to exploring the impact of specific glycans and glycosylation sites on viral structure and function. Structural analysis reveals the precise locations of glycosylation sites, while viral mutagenesis studies explore how particular glycosylation sites influence viral infectivity.
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Antiviral therapeutics development
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Viral glycosylation is a potential target for therapeutic intervention. Therapeutic approaches include using carbohydrate-binding agents and employing synthetic carbohydrate ligands to target viral glycans and block viral entry, such as some naturally occurring lectins. Host glycogenes have been identified as novel targets for antiviral drugs, such as the OST complex inhibitor.
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Vaccine design and development
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Crucial glycans for viral function are often conserved and can be targeted for intervention. Identifying conserved glycan patterns is a priority for vaccine development. Through mutation of specific conserved glycosylation sites, vaccines can be designed to enhance the neutralization of various viruses. Modifying glycan density on immunogens is a key strategy in vaccine design.
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Highlights
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Advanced MS-based technology for glycosylation analysis
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Comprehensive characterization of viral glycosylation
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Comparative analysis of glycosylation among different virus strains and subtypes
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Viral glycosylation analysis for various classes of viruses
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Analysis of viral glycoproteins produced from different host cells
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A professional team of experts specialized in viral glycosylation analysis
Thorough characterization of viral glycoproteins is crucial for advancing virus biology research and developing innovative strategies for antiviral therapeutics and vaccine design. Creative Biolabs is committed to delivering comprehensive glycosylation analysis services for a wide range of virus glycoproteins. If you require more information or wish to inquire further about our services, please don't hesitate to contact us.
Reference
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Bagdonaite, Ieva, and Hans H. Wandall. "Global aspects of viral glycosylation." Glycobiology 28.7 (2018): 443-467.
For Research Use Only.
Related Services:
- Glycoprotein Detection
- Glycoprotein Structure Analysis
- Glycoprotein Quantification
- High-throughput Glycan Screening
