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The Structure of HCV

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Hepatitis C Virus I

Abstract

According to nature’s functional aesthetics principles, hepatitis C virus (HCV) came to acquire a certain structure to serve a specific purpose. Structure explains mechanisms, reveals strategies. In viruses, optimization of the shape is dictated by the number of encoded structural proteins and constant pressure from the host immune system. The result is a durable particle, built to perfection. While perfection is often associated with symmetry, HCV shows how successful an irregular virus can be. This virus compromised its morphology, evolving to mask itself; a beautiful example of exploitation of the host to maintain a chronic infection. This chapter summarizes our current knowledge of the HCV virion and its peculiar properties that explain the challenges that we faced in isolating it and that we keep facing in trying to develop effective vaccine strategies.

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Abbreviations

Å:

Angstrom

aa:

Amino acid

AP2M1:

Adaptor-related protein complex 2 μ1 subunit

Apo:

Apolipoprotein

BVDV:

Bovine viral diarrhea virus

C:

Capsid protein

CE:

Cholesteryl esters

Chol:

Cholesterol (unesterified)

CM:

Chylomicrons

cryo-EM:

Cryo-electron microscopy

cryo-ET:

Cryo-electron tomography

CSFV:

Classical swine fever virus

DENV:

Dengue virus

DGAT1:

Diacylglycerol O-acetyltransferase 1

E:

Envelope glycoprotein

EM:

Electron microscopy

ER:

Endoplasmic reticulum

HA:

Hemagglutinin

HCV:

Hepatitis C virus

HCVcc:

Cell culture-derived HCV

HDL:

High-density lipoprotein

HSPGs:

Heparan sulfate proteoglycans

Huh:

Human hepatoma

HVR:

Hypervariable region

IDL:

Intermediate-density lipoprotein

iEM:

Immuno-EM

IFN:

Interferon

Ig:

Immunoglobulin

JFH:

Japanese fulminant hepatitis

Kb:

Kilobase

LD:

Lipid droplet

LDL:

Low-density lipoprotein

LDL-R:

LDL receptor

LPL:

Lipoprotein lipase

LVP:

Lipo-viro-particle

MTP:

Microsomal triglyceride transfer protein

NaBr:

Sodium bromide

NANBH:

Non-A non-B hepatitis

NDV:

Newcastle disease virus

NMR:

Nuclear magnetic resonance

NS:

Non-structural

PC:

Phosphatidylcholine

PE:

Phosphatidylethanolamine

PHH:

Primary human hepatocytes

PL:

Phospholipids

PS:

Phosphatidylserine

RIG-I:

Retinoic acid-inducible gene I

RNAi:

RNA interference

SCID:

Severe combined immunodeficiency

SM:

Sphingomyelin

SR-BI:

Scavenger receptor class B type I

TCID50 :

Tissue culture infectious dose50

TG:

Triglycerides

uPA:

Urokinase plasminogen activator

VLDL:

Very low-density lipoprotein

VLP:

Virus-like particles

WNV:

West Nile virus

YFV:

Yellow fever virus

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Acknowledgements

The authors would like to thank Dr. Matthew Miller (Rutgers University) for his assistance with the preparation of the figures.

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Authors and Affiliations

  1. Department of Chemistry and Chemical Biology, Rutgers, The State University of New Jersey, New Brunswick, NJ, USA

    Joseph Marcotrigiano

  2. Department of Infectious Diseases, King’s College London, London, UK

    Maria Teresa Catanese

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  1. Joseph Marcotrigiano
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  2. Maria Teresa Catanese
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Correspondence to Joseph Marcotrigiano or Maria Teresa Catanese .

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Editors and Affiliations

  1. National Institute of Infectious Diseases, Tokyo, Tokyo, Japan

    Tatsuo Miyamura

  2. Departments of Medicine and Microbiology & Immunology , The University of North Carolina, Chapel Hill, North Carolina, USA

    Stanley M. Lemon

  3. Center for Vaccines and Immunity, The Research Institute at Nationwide Children's Hospital, Columbus, Ohio, USA

    Christopher M. Walker

  4. National Institute of Infectious Diseases, Tokyo, Tokyo, Japan

    Takaji Wakita

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Marcotrigiano, J., Catanese, M.T. (2016). The Structure of HCV. In: Miyamura, T., Lemon, S., Walker, C., Wakita, T. (eds) Hepatitis C Virus I. Springer, Tokyo. https://doi.org/10.1007/978-4-431-56098-2_3

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