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Related Concept Videos

Hepatitis01:25

Hepatitis

Hepatitis is an inflammatory condition of the liver most commonly caused by hepatotropic viruses (A–E), though non-infectious causes such as alcohol and drugs also exist.Hepatitis AHepatitis A virus (HAV) is a non-enveloped RNA virus of the Picornaviridae family. It is primarily transmitted via the fecal-oral route, typically through ingestion of contaminated food or water. After ingestion, HAV enters the bloodstream through the oropharynx or intestinal epithelium and reaches the liver. The...
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Coronavirus

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Related Experiment Video

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Engineering Antiviral Agents via Surface Plasmon Resonance
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Hepatitis C virus envelope glycoprotein E2 glycans modulate entry, CD81 binding, and neutralization.

Emilia Falkowska1, Francis Kajumo, Edie Garcia

  • 1Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.

Journal of Virology
|May 18, 2007
PubMed
Summary

N- and O-linked glycans on Hepatitis C virus (HCV) envelope protein E2 are critical for viral entry. Removing these glycans enhances antibody neutralization, suggesting a new strategy for developing effective HCV vaccines.

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A Protocol for Analyzing Hepatitis C Virus Replication
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A Protocol for Analyzing Hepatitis C Virus Replication

Published on: June 26, 2014

Area of Science:

  • Virology
  • Immunology
  • Glycobiology

Background:

  • Hepatitis C virus (HCV) causes significant liver disease, including cirrhosis and cancer.
  • HCV entry into hepatocytes relies on envelope glycoproteins E1 and E2 interacting with cellular receptors.
  • Glycans on viral envelopes can shield functional domains and reduce immune system recognition.

Purpose of the Study:

  • To investigate the role of N- and O-linked glycans on the HCV E2 envelope glycoprotein.
  • To determine how these glycans influence viral entry and antibody-mediated neutralization.
  • To explore the impact of glycans on E2 binding to cellular receptors like CD81.

Main Methods:

  • Analysis of N- and O-linked glycans on the HCV E2 protein.
  • Assessment of glycan impact on viral entry into target cells.
  • Evaluation of serum neutralization efficacy against HCV with modified glycans.
  • Investigation of E2 binding to the CD81 receptor.

Main Results:

  • Several N- and O-linked glycans on E2 were identified as critical for HCV viral entry.
  • Removal of specific glycans significantly enhanced the neutralization of viral entry by sera from HCV-positive individuals.
  • Only a subset of the identified glycans affected both viral entry/neutralization and CD81 binding.

Conclusions:

  • HCV envelope glycans play a vital role in masking functionally important regions of the E2 protein.
  • These glycans contribute to immune evasion by reducing viral immunogenicity.
  • Targeting these glycans presents a potential new strategy for developing highly neutralizing antibodies and effective HCV vaccines.