Glycosylation Analysis Service for Measles Virus Glycoprotein

Measles Virus Glycoprotein

Measles virus (MeV) belongs to the Morbillivirus genus, Paramyxoviridae family, characterized as a negative-sense single-stranded RNA virus. It possesses two envelope glycoproteins: hemagglutinin (H) and fusion (F) proteins, which play crucial roles in the virus's lifecycle, particularly during viral entry to host cells. The H protein mediates the viral attachment to host cells by interacting with cellular receptors containing sialic acid. Two known receptors for the H protein are CD46 and SLAM. The H protein also triggers host immune responses. This glycoprotein undergoes N-linked glycosylation, typically featuring five potential N-linked glycosylation sites, specifically Asn 168, 187, 200, 215, and 238. The F protein is categorized as a class I fusion protein and is responsible for initiating membrane fusion. The oligomerization of the H and F proteins is a key initiating step in this cellular entry process. N-linked glycosylation plays a crucial role in maintaining the proper conformation and stability of glycoproteins and influences the binding affinity to cell receptors and the interaction with cell membranes, thereby impacting viral attachment to host cells.

Fig.1 Measles virion and genome.¹

Glycosylation Analysis Services for MeV Glycoprotein at Creative Biolabs

Creative Biolabs offers advanced glycosylation analysis services for MeV glycoproteins, aiming to understand the role of N-linked glycosylation in the viral entry and infection process. We utilize high-resolution tandem mass spectrometry techniques, including MALDI-TOF/TOF MS, to provide comprehensive analyses of the N-linked glycosylation patterns of MeV glycoprotein. Our team adheres to rigorous protocols in sample handling and analysis, ensuring the utmost precision and reliability of results.

We offer detailed information on glycan composition and structures, and the identification of specific glycosylation sites within MeV H and F glycoproteins, including assessing the occupancy status and structural diversity at each site. This information is vital for understanding glycan patterns, glycosylation sequons related to cell receptor binding, and the formation of F/H hetero-oligomerization. It offers valuable insights into the role of MeV glycoproteins in viral entry processes.

Benefits of Our Services

• Specialized protocols for sample handling and analysis: We follow stringent Standard Operating Procedures (SOP) for every stage of viral glycosylation analysis from sample preparation to MS detection and data analysis, ensuring the accuracy and consistency of our processes.
• Advanced detection techniques and methodologies: We employ cutting-edge tandem mass spectrometry techniques and are equipped with state-of-the-art equipment and analysis methods, with MALDI-TOF/TOF MS being a particularly common and effective choice for glycan analysis.
• Comprehensive characterization of glycosylation profiles: Our analysis encompasses a thorough characterization of glycan composition and structures, specific glycosylation sites, site occupancy assessment, and comparison of glycan heterogeneity, providing a holistic view of viral glycosylation.
• Specific analysis of glycosylation patterns involved in viral entry: We specialize in tailoring our analysis to the complex of viral glycoprotein and cell receptors. We identify critical glycosylation patterns involved in receptor binding, offering valuable structural and functional insights into viral entry and infection mechanisms.
• Professional team of experts: Our team consists of seasoned experts with a wealth of experience in glycoprotein analysis, ensuring the highest level of competence and reliability.

Creative Biolabs offers cutting-edge MS-based analysis platforms customized for MeV glycoproteins. Our services enable in-depth N-glycan profiling, contributing to a deeper understanding of MeV glycoprotein structure and function, particularly in the context of viral entry and infection.

Please feel free to contact us for detailed information or send an inquiry directly. Our dedicated team offers expert guidance and support for your research endeavors.

Reference

1. Bankamp, Bettina, et al. "Genetic characterization of measles vaccine strains." The Journal of Infectious Diseases 204.suppl_1 (2011): S533-S548.

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