Hepatitis C Virus Infection Protein Network

Chassey, Benoı̂t de; Tafforeau, Lionel; André, Patrice; Rabourdin–Combe, Chantal; Lotteau, Vincent

doi:10.1016/j.ijid.2008.05.437

Cited by 96 publications

(170 citation statements)

References 65 publications

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“…2 against the HCV core protein. HCV core has been reported to bind to more than 45 human proteins (22), but did not interact with any of the human proteins from Fig. 2 in our yeast two-hybrid screens.…”

Section: Mapping the Denv-human Protein Interactionmentioning

confidence: 67%

“…High-throughput yeast twohybrid assays and co-affinity purification plus mass spectrometry allowed protein-protein interactions to be identified on a large-scale. These high throughput technologies enabled the identification of virus-host cell interactions and the development of human protein interaction networks that provide a larger context to understand virus-host cell interactions (21)(22)(23)(24)(25)(26)(27)(28). The two approaches to identify cellular cofactors of virus infection are complementary: RNAi screens provide a list of host factors that can affect virus replication either directly or indirectly, and virus-host protein interaction networks elucidate the direct interface between the virus and the host cell.…”

mentioning

confidence: 99%

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A Physical Interaction Network of Dengue Virus and Human Proteins

Khadka

Vangeloff

Zhang

et al. 2011

Molecular & Cellular Proteomics

153

148

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Dengue virus (DENV), an emerging mosquito-transmitted pathogen capable of causing severe disease in humans, interacts with host cell factors to create a more favorable environment for replication. However, few interactions between DENV and human proteins have been reported to date. To identify DENV-human protein interactions, we used high-throughput yeast two-hybrid assays to screen the 10 DENV proteins against a human liver activation domain library. From 45 DNA-binding domain clones containing either full-length viral genes or partially overlapping gene fragments, we identified 139 interactions between DENV and human proteins, the vast majority of which are novel. These interactions involved 105 human proteins, including six previously implicated in DENV infection and 45 linked to the replication of other viruses. Human proteins with functions related to the complement and coagulation cascade, the centrosome, and the cytoskeleton were enriched among the DENV interaction partners. To determine if the cellular proteins were required for DENV infection, we used small interfering RNAs to inhibit their expression. Six of 12 proteins targeted (CALR, DDX3X, ERC1, GOLGA2, TRIP11, and UBE2I) caused a significant decrease in the replication of a DENV replicon. We further showed that calreticulin colocalized with viral dsRNA and with the viral NS3 and NS5 proteins in DENV-infected cells, consistent with a direct role for calreticulin in DENV replication. Human proteins that interacted with DENV had significantly higher average degree and betweenness than expected by chance, which provides additional support for the hypothesis that viruses preferentially target cellular proteins that occupy central position in the human protein interaction network. This study provides a valuable starting point for additional investigations into the roles of human proteins in

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Section: Mapping the Denv-human Protein Interactionmentioning

confidence: 67%

mentioning

confidence: 99%

A Physical Interaction Network of Dengue Virus and Human Proteins

Khadka

Vangeloff

Zhang

et al. 2011

Molecular & Cellular Proteomics

153

148

View full text Add to dashboard Cite

show abstract

“…The protein is involved in several steps of the HCV life cycle and interacts with almost all other non-structural proteins and with numerous host factors (48,49). NS5A is anchored at the cytoplasmic side of the endoplasmic reticulum membrane via an N-terminal helix (50) and comprises 3 cytosolic domains (D1, D2, and D3).…”

Section: Hepatitis C Virus (Hcv)mentioning

confidence: 99%

Hepatitis C Virus NS5B and Host Cyclophilin A Share a Common Binding Site on NS5A

Rosnoblet¹,

Fritzinger²,

Legrand

et al. 2012

Journal of Biological Chemistry

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Background: HCV replication requires the interaction of the viral polymerase NS5B with both viral and host proteins. Results: We performed the molecular characterization of the interactions between HCV NS5B, NS5A, and host CypA. Conclusion: HCV NS5B and host CypA share a binding site on HCV NS5A. Significance: The NS5A-D2 site, which interacts with both the HCV polymerase NS5B and the host CypA, might regulate the HCV replication.

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“…1) that were recently developed to generate the HCV infection map (4). For this interactome approach, 27 HCV ORFs (encoding full-length proteins or domains) were used as baits to screen 2 human cDNA libraries and generate a virus-host cell interaction map composed of 314 virushost protein interactions.…”

mentioning

confidence: 99%

Virus–Human Cell Interactomes

Tafforeau¹,

Rabourdin–Combe²,

Lotteau³

2011

Methods in Molecular Biology

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Using global approaches and high-throughput technologies in virology brings a new vision of the infections physiology and allows the identification of cellular factors, mandatory for viral life cycle, that could be targeted by original therapeutic agents. It opens perspectives for the treatment of viral infections by acting on cellular pathways that the virus must use for its own replication. Combining these new molecules with classical antiviral drugs and immunomodulators diversifies and enlarges the antiviral arsenal and contributes to fight drug resistance.Our laboratory and others are constructing virus-human interactomes to propose a comprehensive analysis of viral infection at the cellular level. Studying these infection maps, where the viral infection can be visualized as perturbation of the human protein-protein interaction network, and identifying the biological functions that are impaired by these perturbations may lead to discovery of new therapeutic targets. These virus-human interaction maps are constructed in a stringent yeast two-hybrid system by screening human cDNA libraries with viral proteins as bait and integrating interactions mined from literature and public databases. Key words:Yeast two-hybrid screen, Mating, Yeast two-hybrid array, Protein-protein interactionThe rapidly growing knowledge of protein-protein interaction networks (interactomes) for model organisms and human provides a network-based model to understand molecular and cellular biology. Recently, virus-host relationships also began to be studied at the proteome level by identifying interactions between viral and host-cell proteins (1-5), as reviewed in ref. 6. These virus-host interactomes compose a repertoire of interactions between viral and human proteins that can be analyzed in a network approach. By this mean, viral infections can be viewed as the expression of new constraints imposed by the virus on the cellular interactome.

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Hepatitis C Virus Infection Protein Network

Cited by 96 publications

References 65 publications

A Physical Interaction Network of Dengue Virus and Human Proteins

A Physical Interaction Network of Dengue Virus and Human Proteins

Hepatitis C Virus NS5B and Host Cyclophilin A Share a Common Binding Site on NS5A

Virus–Human Cell Interactomes

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