Glycosylation Analysis Service for Hepatitis C Virus Glycoprotein

Hepatitis C Virus Glycoprotein

The Hepatitis C virus (HCV) is responsible for causing both acute and chronic liver diseases in humans, including chronic hepatitis, cirrhosis, and hepatocellular carcinoma. HCV is a positive-strand RNA virus with a genome comprised of 10 different proteins, including core proteins, envelope proteins E1 and E2, p7, and nonstructural proteins. The envelope proteins E1 and E2 play a critical role in the interaction between the virus and host cells, including processes such as receptor binding and internalization, which are vital for various biological functions. Notably, both HCV E1 and E2 are extensively glycosylated in their N-terminal ectodomains, featuring up to 5 and 11 N-linked glycosylation sites in E1 and E2, respectively. Glycans serve essential functions in the proper folding of these proteins, receptor binding, and facilitating HCV cell entry. Additionally, glycan shielding has emerged as a potential mechanism by which HCV conceals broadly neutralizing epitopes on its viral glycoproteins, thereby evading host immune responses. Studies of the glycan structures attached to the HCV envelope glycoproteins provide valuable insights into various aspects of viral biology.

Fig.1 HCV structure and genome organization.¹

Glycosylation Analysis Services for HCV Glycoprotein at Creative Biolabs

The HCV glycosylation analysis services offered by Creative Biolabs are designed to provide comprehensive insights into the glycosylation patterns of HCV envelope proteins, particularly E1 and E2. Our approach combines high-throughput glycomic technology with advanced analytical techniques to comprehensively map the precise glycopatterns of HCV envelope glycoproteins. Here's an overview of our methods:

1. Lectin microarray: We utilize lectin microarray technology to investigate the glycan landscape of HCV envelope proteins. This technique enables us to gain insights into glycosidic linkages, specific glycan motifs, interactions, and partial glycan structures.
2. LC-MS/MS: Our glycosylation analysis includes LC-MS/MS using MALDI or ESI combined with ETD/HCD fragmentation methods. This powerful analytical tool allows us to determine the composition of glycans with precision.
   Through our glycosylation analysis services, we can provide valuable information including glycosylation site occupancy and mapping, N-linked oligosaccharide profile, and glycan structural characterization.

Applications of HCV Glycosylation Analysis

1. Molecular mechanisms of viral entry
   Analyzing the glycan structures on HCV E1 and E2 proteins can decipher how the virus interacts with host cells during the entry process and help identify key glycan-dependent interactions that are crucial for viral entry.
2. Vaccine development
   Glycosylation patterns on viral envelope proteins play a significant role in immune recognition. Characterizing these patterns can aid in the design of effective vaccines by identifying glycan epitopes that elicit neutralizing antibodies or immune responses.
3. Therapeutic development
   Glycans on viral glycoproteins serve as targets for therapeutic intervention. Understanding the glycan structures can lead to the development of innovative therapeutics, such as entry inhibitors or glycan-targeting antibodies, which may disrupt viral entry or neutralize the virus.
4. Immune evasion strategies
   HCV employs glycan shielding as a mechanism to hide critical epitopes from the host immune system. Analyzing glycan shielding strategies can provide insights into how the virus evades immune surveillance.

Published Data

Technology: N-glycosylation analysis

Journal: Pathogens

IF: 4.531

Published: 2021

Results: This review emphasizes the significance of glycosylation in HCV infection and highlights the importance of ongoing research to uncover novel therapeutic and vaccine targets. Notably, the N-glycosylation sites on HCV E1 and E2 exhibit a high degree of conservation across most genotypes, and these conserved sites are typically occupied. By elucidating the roles of viral and cellular glycans in HCV pathogenesis, we can advance our efforts to develop novel strategies for therapeutics or vaccines.

Fig.2 N-glycosylation of HCV glycoproteins.²

Our team at Creative Biolabs is committed to delivering high-quality glycosylation analysis services to support your research endeavors in the field of HCV and virology. By leveraging our HCV glycosylation analysis service, researchers can gain valuable insights into the role of glycosylation in HCV infection, immune evasion, and potential therapeutic targets. Please don't hesitate to contact us for more details or send an inquiry directly.

References

1. Roe, Barbara, and William W. Hall. "Cellular and molecular interactions in coinfection with hepatitis C virus and human immunodeficiency virus." Expert reviews in molecular medicine 10 (2008): e30.
2. LeBlanc, Emmanuelle V., et al. "Hepatitis C virus glycan-dependent interactions and the potential for novel preventative strategies." Pathogens 10.6 (2021): 685.

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