Interaction of hepatitis C virus F protein with prefoldin 2 perturbs tubulin cytoskeleton organization

Tsao, Mei-Ling; Chao, Chung-Hao; Yeh, Chau‐Ting

doi:10.1016/j.bbrc.2006.07.062

Cited by 37 publications

(28 citation statements)

References 31 publications

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“…Therefore, interruption of normal microtubule formation likely results in decreased HCV replication. Tsao et al (29) found that F protein interacts with a cellular protein named prefoldin 2. Functional prefoldin delivers nascent actin and tubulin proteins to the eukaryotic cytosolic chaperonin for facilitated folding.…”

Section: Discussionmentioning

confidence: 99%

Hepatitis C virus F protein: A double-edged sword in the potential contribution of chronic inflammation to carcinogenesis

Kong

Deng²,

Wang³

et al. 2009

Mol Med Rep

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Section: Discussionmentioning

confidence: 99%

Hepatitis C virus F protein: A double-edged sword in the potential contribution of chronic inflammation to carcinogenesis

Kong

Deng²,

Wang³

et al. 2009

Mol Med Rep

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“…This might be due to the functional constraints of the F protein in natural infection, even though its function remains unclear. To date, no homologous function of the F protein has been identified except for an interaction with prefoldin (PFD) 2, a subunit of the PFD complex, resulting in some disturbance of the tubulin cytoskeleton organization (Tsao et al, 2006). It has also been suggested that the F protein could serve as a modulator to prevent cytolysis of the host cells.…”

Section: Discussionmentioning

confidence: 99%

Differential reactivity of putative genotype 2 hepatitis C virus F protein between chronic and recovered infections

Chuang

Allain

2008

Journal of General Virology

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To date, all studies regarding hepatitis C virus (HCV) F protein have been based on expression in vitro/in vivo of recombinant protein or monoclonal antibodies derived from genotype 1a or 1b sequences, but not from other genotypes. The objective of this study was to prepare a putative genotype 2 recombinant F protein and evaluate its reactivity in plasma from individuals with chronic HCV infection or who had recovered from infection. One genotype 2 strain was selected for F protein (F-2) and core expression in bacterial culture. An ELISA was developed and applied to samples from patients with chronic infection or recovered infection of various genotypes. The anti-F-2 response in 117 samples showed a significantly higher reactivity in chronic than in recovered HCV-infected blood donors (P<0.001), but no difference was found among genotypes. However, the correlation between anti-F and anti-core was more significant in genotypes 1 and 2 than in genotype 3. Anti-F-2 titres were also significantly higher in chronic than in recovered individuals (P<0.0001). Antibody titres to recombinant genotype 2 core protein or to genotype 1 multiple proteins used in commercial anti-HCV assays paralleled the anti-F-2 end-point antibody titre. This study thus demonstrated the antigenicity of genotype 2 HCV F protein, although the exact location of the natural frameshift position remains unknown. The difference in anti-F-2 response between chronic and recovered infection, the cross-reactivity irrespective of genotype and the correlation of antibody response with structural and non-structural antigens suggest that the immune response to F protein is an integral part of the natural HCV infection.

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“…This pressure may reflect immune-driven selective pressure and/or the adaptation of F protein to the cellular environment. 52 In this respect, F protein has recently been described as potentially interacting with the cytoskeleton. 52 Thus, by demonstrating F variants that cluster in HCC, this study will make it possible to test whether or not different F protein mutants display distinct biological activities.…”

Section: Discussionmentioning

confidence: 99%

Distinct hepatitis C virus core and F protein quasispecies in tumoral and nontumoral hepatocytes isolated via microdissection

et al. 2007

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Hepatitis C virus (HCV) genetic variability may be involved in liver carcinogenesis. We investigated HCV core and corresponding putative F protein genetic variability in hepatocellular carcinoma (HCC) and cirrhotic nodules. Hepatocyte clusters from 7 patients with HCC and HCV1b-related cirrhosis were isolated via microdissection of HCC tissues and 2 nontumoral cirrhotic nodules. The HCV core complementary DNA was cloned and sequenced from each liver compartment and from the serum of 2 patients. Nucleotide diversity and synonymous and nonsynonymous substitutions were analyzed within and between compartments via phylogenetic analysis and Mantel's test. Liver HCV RNA accumulation was lower in HCC. Increased quasispecies diversity and complexity was observed with HCC in 6 of 7 patients. Mantel's test demonstrated marked compartmentalization of quasispecies between HCC and cirrhotic nodules in all 7 patients and also between the 2 nontumoral nodules in 5 of them. Synonymousnonsynonymous substitution analysis indicated low selection against tumoral core quasispecies in all patients and a more selective pressure against F protein quasispecies in all compartments. In the 2 subjects analyzed, HCC and nontumoral hepatocyte quasispecies were only minor or undetected in serum. Conclusion: In tumoral hepatocytes, low-replicating hepatitis C quasispecies are compartmentalized and more diversified and are subjected to low selective pressure. Our study supports the importance of core genetic variability in hepatocellular carcinogenesis.

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Interaction of hepatitis C virus F protein with prefoldin 2 perturbs tubulin cytoskeleton organization

Cited by 37 publications

References 31 publications

Hepatitis C virus F protein: A double-edged sword in the potential contribution of chronic inflammation to carcinogenesis

Hepatitis C virus F protein: A double-edged sword in the potential contribution of chronic inflammation to carcinogenesis

Differential reactivity of putative genotype 2 hepatitis C virus F protein between chronic and recovered infections

Distinct hepatitis C virus core and F protein quasispecies in tumoral and nontumoral hepatocytes isolated via microdissection

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