Hepatitis C Virus Structure: Defined by What It Is Not

Cold Spring Harb Perspect Med. 2020 Jan 2;10(1):a036822. doi: 10.1101/cshperspect.a036822.

Abstract

Hepatitis C virus (HCV) represents an important and growing public health problem, chronically infecting an estimated 70 million people worldwide. This blood-borne pathogen is generating a new wave of infections in the United States, associated with increasing intravenous drug use over the last decade. In most cases, HCV establishes a chronic infection, sometimes causing cirrhosis, end-stage liver disease, and hepatocellular carcinoma. Although a curative therapy exists, it is extremely expensive and provides no barrier to reinfection; therefore, a vaccine is urgently needed. The virion is asymmetric and heterogeneous with the buoyancy and protein content similar to low-density lipoparticles. Core protein is unstructured, and of the two envelope glycoproteins, E1 and E2, the function of E1 remains enigmatic. E2 is responsible for specifically binding host receptors CD81 and scavenger receptor class B type I (SR-BI). This review will focus on structural progress on HCV virion, core protein, envelope glycoproteins, and specific host receptors.

Publication types

  • Research Support, N.I.H., Intramural
  • Review

MeSH terms

  • Antibodies, Neutralizing / chemistry
  • Crystallography, X-Ray
  • Hepacivirus / chemistry*
  • Hepacivirus / immunology
  • Hepacivirus / metabolism
  • Humans
  • Protein Structure, Tertiary
  • Tetraspanin 28 / chemistry
  • Viral Envelope Proteins / chemistry*
  • Viral Envelope Proteins / immunology
  • Viral Hepatitis Vaccines / chemistry
  • Viral Hepatitis Vaccines / immunology
  • Virus Internalization

Substances

  • Antibodies, Neutralizing
  • CD81 protein, human
  • E1 protein, Hepatitis C virus
  • Tetraspanin 28
  • Viral Envelope Proteins
  • Viral Hepatitis Vaccines
  • glycoprotein E2, Hepatitis C virus