How Stable Is the Hepatitis C Virus (HCV)? Environmental Stability of HCV and Its Susceptibility to Chemical Biocides

Ciesek, Sandra; Friesland, Martina; Steinmann, Jörg; Becker, Benedikt; Wedemeyer, Heiner; Manns, Michael P.; Steinmann, J.; Pietschmann, Thomas; Steinmann, Eike

doi:10.1086/652803

Cited by 76 publications

(68 citation statements)

References 35 publications

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“…Importantly, fusion in all these systems depends on a transient acidification, consistent with HCV entry dependence on endosomal acidification [146,147]. Yet, HCVcc are pH resistant [78,178], indicating that a first trigger may be needed to render the glycoprotein fusogenic. Consistent with this, cell-to-cell and cell-surface fusion assays depend on a 37°C incubation period with the target cells prior to the acidic treatment.…”

Section: Endocytosis and Fusion Of Hcvmentioning

confidence: 66%

“…Data on HCVcc storage are sparser. Briefly, we found that HCVcc (Jc1 or Luc-Jc1 virus) has a half-life of 6 hours at 37°C, 3.5 days at room temperature and 11 days at 4°C [178]. Other teams reported JFH-1 virus stability at 4°C for up to 4 or 6 weeks [6,190], a difference that might be imputable to the different virus strains and titers.…”

Section: Preparation Concentration and Storage Of Hcvccmentioning

confidence: 84%

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Entry and replication of recombinant hepatitis C viruses in cell culture

Vièyres

Pietschmann

2013

Methods

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Section: Endocytosis and Fusion Of Hcvmentioning

confidence: 66%

Section: Preparation Concentration and Storage Of Hcvccmentioning

confidence: 84%

Entry and replication of recombinant hepatitis C viruses in cell culture

Vièyres

Pietschmann

2013

Methods

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“…Whereas HCV contained in culture supernatant retains full infectivity when stored for 1 week at 4°C, for example (70), infectivity of captured virus samples is reduced by up to 100-fold within 16 h at 4°C. Therefore, analyses of infectious virions after capture by using density gradient centrifugation were difficult as infectivity was FIGURE 6.…”

Section: Discussionmentioning

confidence: 99%

Biochemical and Morphological Properties of Hepatitis C Virus Particles and Determination of Their Lipidome

Merz

Long

Hiet

et al. 2011

Journal of Biological Chemistry

314

355

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A hallmark of hepatitis C virus (HCV) particles is their association with host cell lipids, most notably lipoprotein components. It is thought that this property accounts for the low density of virus particles and their large heterogeneity. However, the composition of infectious virions and their biochemical and morphological properties are largely unknown. We developed a system in which the envelope glycoprotein E2 was Nterminally tagged with a FLAG epitope. This virus, designated Jc1E2 FLAG , produced infectivity titers to wild type levels and allowed affinity purification of virus particles that were analyzed for their protein and lipid composition. By using mass spectrometry, we found the lipid composition of Jc1E2 FLAG particles to resemble the one very low-and low density-lipoprotein with cholesteryl esters accounting for almost half of the total HCV lipids. Thus, HCV particles possess a unique lipid composition that is very distinct from all other viruses analyzed so far and from the human liver cells in which HCV was produced. By electron microscopy (EM), we found purified Jc1E2 FLAG particles to be heterogeneous, mostly spherical structures, with an average diameter of about 73 nm. Importantly, the majority of E2-containing particles also contained apoE on their surface as assessed by immuno-EM. Taken together, we describe a rapid and efficient system for the production of large quantities of affinity-purified HCV allowing a comprehensive analysis of the infectious virion, including the determination of its lipid composition.

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“…2). Furthermore, poor stability of virions makes the purification process extremely time-sensitive, limiting the number of purification steps that can be undertaken before most of the infectivity is lost (11). Finally, propensity to forming aggregates has been observed, preventing tandem affinity purification approaches (Fig.…”

Section: Discussionmentioning

confidence: 99%

Proteomics of HCV virions reveals an essential role for the nucleoporin Nup98 in virus morphogenesis

Lussignol

Kopp

Molloy

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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Hepatitis C virus (HCV) is a unique enveloped virus that assembles as a hybrid lipoviral particle by tightly interacting with host lipoproteins. As a result, HCV virions display a characteristic low buoyant density and a deceiving coat, with host-derived apolipoproteins masking viral epitopes. We previously described methods to produce high-titer preparations of HCV particles with tagged envelope glycoproteins that enabled ultrastructural analysis of affinity-purified virions. Here, we performed proteomics studies of HCV isolated from culture media of infected hepatoma cells to define viral and host-encoded proteins associated with mature virions. Using two different affinity purification protocols, we detected four viral and 46 human cellular proteins specifically copurifying with extracellular HCV virions. We determined the C terminus of the mature capsid protein and reproducibly detected low levels of the viral nonstructural protein, NS3. Functional characterization of virion-associated host factors by RNAi identified cellular proteins with either proviral or antiviral roles. In particular, we discovered a novel interaction between HCV capsid protein and the nucleoporin Nup98 at cytosolic lipid droplets that is important for HCV propagation. These results provide the first comprehensive view to our knowledge of the protein composition of HCV and new insights into the complex virushost interactions underlying HCV infection. Hepatitis C virus (HCV) is a positive-sense ssRNA virus of the Flaviviridae family. This bloodborne pathogen causes chronic liver infection that develops into cirrhosis and hepatocellular carcinoma and is the leading indication for liver transplantation. Over 185 million people are chronically infected with HCV (2). Despite great advances in the ability to study this virus in vitro, significant gaps remain in our understanding of the infectious particle and the virus-host interactions required for HCV propagation.The protein composition of HCV is not known. Although the capsid protein, Core, and the E1 and E2 envelope glycoproteins are thought to be the major constituents of the virion, it remains to be determined if nonstructural viral proteins are packaged as well. A growing body of literature suggests that cellular proteins are important components of HCV. Indeed, this virus closely associates with LDL and very-LDL components, forming a chimeric lipoviral particle (LVP). Biochemical and ultrastructural studies demonstrated that infectious HCV particles are coated with endogenous apolipoproteins that play key roles in viral attachment and entry, explaining the higher infectivity of lipoprotein-associated HCV (2).The heterogeneous size and appearance of extracellular HCV, ranging from 40 to >100 nm in diameter, suggests that the set of associated proteins (both viral and cellular), as well as their stoichiometry, might vary across the virion population. Additionally, the specific infectivity of HCV changes according to the cell system/host that the virus is produced in, highlighting a stro...

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How Stable Is the Hepatitis C Virus (HCV)? Environmental Stability of HCV and Its Susceptibility to Chemical Biocides

Abstract: This study assessed the environmental stability and susceptibility to chemical biocides of HCV. The results should be useful in defining rigorous disinfection protocols to prevent nosocomial transmission of HCV.

Cited by 76 publications

References 35 publications

Entry and replication of recombinant hepatitis C viruses in cell culture

Entry and replication of recombinant hepatitis C viruses in cell culture

Biochemical and Morphological Properties of Hepatitis C Virus Particles and Determination of Their Lipidome

Proteomics of HCV virions reveals an essential role for the nucleoporin Nup98 in virus morphogenesis

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