Glycosylation Analysis Service for Marburg Virus Glycoprotein
Marburg Virus Glycoprotein
Marburg virus (MARV), a member of the Filoviridae family, is responsible for causing the severe and often fatal MARV disease (MVD) in humans. It is characterized by an enveloped, negative-sense, single-stranded RNA genome encoding seven main proteins including the glycoprotein (GP). GP is the only surface protein that forms homotrimeric spikes on the viral envelope and plays pivotal roles in host cell attachment, viral entry, immune evasion, and the elicitation of host immune responses. It comprises two subunits, GP1 and GP2, with GP1 being responsible for receptor binding and GP2 facilitating membrane fusion during viral entry. GP is heavily glycosylated with complex and high mannose-type N-linked glycans and mucin-type O-linked glycans, contributing significantly to its molecular weight. Its extensive glycosylation patterns are essential for its role in viral entry and immune responses. Understanding these glycosylation patterns is crucial for advancing research on MARV and developing potential therapeutic interventions.
Fig.1 Virion structure and genome organization of MARV.1, 2
Glycosylation Analysis Services for MARV Glycoprotein at Creative Biolabs
In-depth characterization of glycosylation patterns not only enhances our understanding of viral biology but also opens doors to novel treatment and vaccination approaches. Creative Biolabs leverages extensive expertise and state-of-the-art glycosylation analysis technologies to provide a comprehensive range of services dedicated to characterizing the glycosylation patterns of MARV GP. We have successfully developed MS-based viral glycoproteomic platforms, complemented by lectin microarray techniques to boost confidence in structure assignment. Our advanced MS methods, including MALDI-TOF MS/MS, enable us to profile glycan composition and structures meticulously and determine glycosylation site occupancy. Our further analysis of glycopeptides offers site-specific heterogeneity profiles for each glycosylation site. This encompasses the analysis of complex and high mannose-type N-linked glycans, as well as mucin-type O-linked glycans attached to MARV GP.
Glycosylation Analysis for MARV Vaccine Development
Glycosylation analysis of MARV GP is crucial for the development of effective vaccines. Virus-like particle (VLP)-based vaccines are considered a promising approach for protecting against MARV. These vaccines contain viral proteins, including GP. Using viral vectors, such as adenovirus or vesicular stomatitis virus (VSV), to express the GP subunit is another approach to MARV vaccines.
Our glycosylation analysis of MARV GP helps in characterizing specific glycan structures and glycosylation sites responsible for receptor binding and immune evasion, allowing modulation of glycosylation patterns for enhanced immune recognition and immune responses, ultimately contributing to the development of MARV vaccines with safety and efficacy.
Highlights of Our Services
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Advanced detection techniques and methodologies
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In-depth characterization for viral N- and O- glycosylation
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Comprehensive profiles for site-specific heterogeneity
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Identifying critical glycosylation patterns involved in viral infection
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Providing valuable insights into MARV vaccine development
Creative Biolabs is your trusted partner in the field of viral glycoprotein analysis. Based on cutting-edge glycosylation analysis techniques and a team of experts, we aim to unravel the role of glycosylation in shaping viral infectivity, immunogenicity, and pathogenicity. For any specific requirements related to research on MARV glycoprotein, please contact us directly or submit an inquiry.
Reference
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Abir, Mehedy Hasan, et al. "Pathogenicity and virulence of Marburg virus." Virulence 13.1 (2022): 609-633.
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Under Open Access license CC BY 4.0, without modification.
For Research Use Only.
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