Glycosylation Analysis Service for Influenza Virus Glycoprotein

Roles of Viral Glycoproteins on Influenza Virus Evolution

Influenza viruses cause both seasonal epidemics and occasional pandemics in humans. The two main envelope glycoproteins on the surface of influenza viruses are hemagglutinin (HA) and neuraminidase (NA), both undergoing N-linked glycosylation. HA and NA glycoproteins play a crucial role in the recognition of host immune cells and are considered the primary antigenic determinants of the virus. Influenza A viruses, the greatest concern for public health, are categorized into various subtypes according to variations in their surface glycoproteins, specifically 18 HA (H1-H18) and 11 NA (N1-N11) subtypes. Glycosylation profile changes in viral glycoproteins, particularly HA, have a significant impact on the evolution of influenza A viruses. HA antigenic drift, which involves modifications in the number and location of glycosylation sites over time, can lead to alterations in various biological activities and the antigenic properties of the virus strain. This allows the novel virus subtypes to evade neutralizing antibodies and avoid immune recognition by host cells. Given the pivotal role of glycans in determining antigenicity, it is crucial to explore the glycosylation patterns of influenza viruses to improve the development of vaccines and antiviral drugs.

Fig.1 Structural models of the HA from different influenza A virus subtypes.¹

Glycosylation Analysis Services for Influenza Virus Glycoprotein at Creative Biolabs

The glycosylation patterns on these glycoproteins play a crucial role in the evolution of influenza viruses, understanding these glycosylation patterns is essential for improving influenza vaccines and antiviral strategies. Creative Biolabs has developed glycosylation analysis services for viral glycoproteins, specifically focusing on influenza virus glycoproteins.

Based on an in-house developed server, we provide sequence-specific prediction of potential glycosylation sites by analyzing adjacent primary sequences within the viral glycoproteins. For further confirmation, we utilize high-resolution HCD/CID-MS/MS tandem mass spectrometry to thoroughly analyze the glycosylation profiles of HA and NA glycoproteins from various influenza A virus subtypes, such as H1N1, H3N2, H5N1, H7N9. By combining predictive analysis with experimental validation, we ensure accurate and thorough glycosylation analysis for influenza virus glycoproteins, which provides valuable insights into how glycans and glycosylation patterns impact the biological activity of these glycoproteins and the evolution of influenza viruses.

In-depth Characterization of Viral Glycosylation at Creative Biolabs

Through comprehensive characterization, we provide essential glycosylation information on viral glycoproteins, including:

Identifying N-glycan structures and assessing glycan heterogeneity: We determine the specific types of N-glycan structures and analyze the diversity of glycan compositions attached to each glycosylation site. Research has indicated the presence of substantial glycan microheterogeneity in HA and NA glycoproteins. This microheterogeneity is closely linked to the biological activities and immune recognition of influenza viruses.
Evaluating glycosylation site localization and occupancy: We perform in-depth analyses of the changes in glycosylation site localization, site occupancy, and conserved sites among different influenza virus subtypes. It has been reported that HA possesses high glycosylation site occupancy and the number of potential glycosylation sites in both HA and NA of seasonal strains has increased throughout virus evolution. Distinct N-glycosylation sites and an increase in the number of glycosylation sites have been linked to immune evasion and attenuation.

Advantages of Our Services

High-resolution and accuracy detection of tandem mass spectrometry
Comprehensive analysis encompassing glycosylation sites and glycan structures
Glycosylation analysis for HA and NA glycoproteins from all influenza virus subtypes
Systematic comparison of glycosylation profiles among different virus subtypes
Professional team experienced in glycoprotein analysis

Published Data

Technology: MS-based N-glycosylation analysis

Journal: Human Vaccines & Immunotherapeutics

IF: 4.526

Published: 2018

Results: The researchers employed tandem mass spectrometry to analyze the site-specific glycosylation pattern of the HA glycoprotein in an egg-grown H1N1 strain (A/New Caledonia/20/1999). They found that eight sites on the stalk region (N28, N40, N304, and N498) and the globular head (N71, N104, N142, and N177) of the protein were glycosylated. The results also revealed a wide glycan microheterogeneity, indicating a diverse range of glycan compositions present at each glycosylation site.

Fig.2 Glycosylation sites on A/New Caledonia/20/1999 H1.²

Creative Biolabs has developed comprehensive glycosylation analysis services for influenza virus glycoproteins to investigate the impacts of glycosylation patterns of HA and NA glycoprotein on influenza virus evolution and advance the development of improved vaccines. For further details or specific inquiries about our influenza virus glycoprotein analysis services, please don't hesitate to contact us.

References

Tate, Michelle D., et al. "Playing hide and seek: how glycosylation of the influenza virus hemagglutinin can modulate the immune response to infection." Viruses 6.3 (2014): 1294-1316.
Cruz, Esteban, et al. "Site-specific glycosylation profile of influenza A (H1N1) hemagglutinin through tandem mass spectrometry." Human vaccines & immunotherapeutics 14.3 (2018): 508-517.

For Research Use Only.