Interaction of the UV-damaged DNA-binding protein with hepatitis B virus X protein is conserved among mammalian hepadnaviruses and restricted to transactivation-proficient X-insertion mutants

Sitterlin, Delphine; Lee, Teh-Hsiu; Prigent, Sylvie; Tiollais, Pierre; Butel, Janet S.; Transy, Catherine

doi:10.1128/jvi.71.8.6194-6199.1997

Cited by 104 publications

(43 citation statements)

References 38 publications

(42 reference statements)

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“…In the present study, this method, combined with mass spectrometric analysis, was introduced to search for the HBx‐binding molecules in Huh‐7 hepatoma cells, and a total of five proteins were identified. Among these, DDB1 [Sitterlin et al, 1997; Leupin et al, 2005] and HSP70 [Zhang et al, 2005] were also reported previously to interact with HBx, which validated the present methods. However, the results also showed that there was much non‐specific binding of non‐FLAG tagged proteins from the Huh‐7 lysate.…”

Section: Discussionsupporting

confidence: 82%

Hepatitis B virus X protein blocks filamentous actin bundles by interaction with eukaryotic translation elongat ion factor 1 alpha 1

Lin

Jiao

et al. 2012

Journal of Medical Virology

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Hepatitis B virus (HBV)‐encoded X protein (HBx protein) is a multi‐functional regulatory protein. It functions by protein–protein interaction and plays a pivotal role in the pathogenesis of HBV‐related diseases. However, the partners in hepatocytes interacting with HBx protein are far from understood fully. In this study, immunoprecipitation was employed to screen for binding partners for the HBx protein from huh‐7 hepatoma cells infected with recombinant adenovirus expressing HBx protein, and five cellular proteins including eukaryotic translation elongation factor 1 alpha 1 (eEF1A1), were identified. The interaction between HBx protein and eEF1A1 was confirmed further using a GST pull‐down assay and co‐immunoprecipitation, respectively. In Huh‐7 hepatoma cells, the HBx protein inhibits dimer formation of eEF1A1, hence blocks filamentous actin bundling. These findings provide new insights into the molecular mechanisms involved in the functions of the HBx protein. J. Med. Virol. 84:871–877, 2012. © 2012 Wiley Periodicals, Inc.

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Section: Discussionsupporting

confidence: 82%

Hepatitis B virus X protein blocks filamentous actin bundles by interaction with eukaryotic translation elongat ion factor 1 alpha 1

Lin

Jiao

et al. 2012

Journal of Medical Virology

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“…Viral load has been shown to be one of many clinical variables that impact the therapeutic outcomes and natural history of chronic HBV infection [4,15]. As with most infectious agents, both host and viral factors have been shown to affect the risk of chronic infection and the severity of clinical disease [16][17][18][19][20][21][22][23]. As an effective statistical tool with which to accurately assess HBV DNA measurements, MMM is able to provide clinicians with statistically normalized viral load determinations, which can allow one to focus on the host and viral factors in the design and monitoring of individualized therapy.…”

Section: Discussionmentioning

confidence: 99%

Multi‐measurement method comparison of three commercial hepatitis B virus DNA quantification assays

Krajden

Minor²,

Cork

et al. 1998

Journal of Viral Hepatitis

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Serum specimens (327) from patients with chronic hepatitis B were evaluated for hepatitis B virus (HBV) DNA using three commercial assays--Chiron Quantiplex (CA), Digene Hybrid Capture (DA) and Abbott HBV DNA assay (AA). The HBV DNA values obtained following evaluation were used to compare the linearity, responsiveness and precision of each assay and to determine the conversion between the three different assay values. The comparison was accomplished using a new statistical approach termed the multi-measurement method (MMM). MMM is a minimal bias, non-linear regression technique that allows simultaneous multiassay performance evaluation as well as assay value interconversion. MMM analysis demonstrated that the CA was more sensitive and responsive than either the DA or the AA. Both the CA and DA were more precise than the AA. Validation of the MMM results was performed using two additional data sets of 551 and 100 specimens, respectively. MMM is a novel statistical tool that has a broad application for the generation of statistically normalized laboratory data and for interassay standardization.

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“…Thus, interaction of wtHBx with DDB1 may affect the integrity of the genome by modulating CDT1 degradation. wtHBx also interacts with single stranded DNA and a series of DNA repair proteins, resulting in inefficient repair of damaged cellular DNA . By blocking DNA repair, wtHBx may facilitate the fixation of mutations and play a role in hepatocarcinogenesis.…”

Section: Hbx: a Viral Proto‐oncogene Evolving In The Course Of Multismentioning

confidence: 99%

Wild type HBx and truncated HBx: Pleiotropic regulators driving sequential genetic and epigenetic steps of hepatocarcinogenesis and progression of HBV‐associated neoplasms

Niller

Bánáti³

et al. 2015

Reviews in Medical Virology

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Hepatitis B virus (HBV) is one of the causative agents of hepatocellular carcinoma. The molecular mechanisms of tumorigenesis are complex. One of the host factors involved is apparently the long-lasting inflammatory reaction which accompanies chronic HBV infection. Although HBV lacks a typical viral oncogene, the HBx gene encoding a pleiotropic regulatory protein emerged as a major player in liver carcinogenesis. Here we review the tumorigenic functions of HBx with an emphasis on wild type and truncated HBx variants, and their role in the transcriptional dysregulation and epigenetic reprogramming of the host cell genome. We suggest that HBx acquired by the HBV genome during evolution acts like a cellular proto-onc gene that is activated by deletion during hepatocarcinogenesis. The resulting viral oncogene (v-onc gene) codes for a truncated HBx protein that facilitates tumor progression. Copyright © 2015 John Wiley & Sons, Ltd.

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Interaction of the UV-damaged DNA-binding protein with hepatitis B virus X protein is conserved among mammalian hepadnaviruses and restricted to transactivation-proficient X-insertion mutants

Cited by 104 publications

References 38 publications

Hepatitis B virus X protein blocks filamentous actin bundles by interaction with eukaryotic translation elongat ion factor 1 alpha 1

Hepatitis B virus X protein blocks filamentous actin bundles by interaction with eukaryotic translation elongat ion factor 1 alpha 1

Multi‐measurement method comparison of three commercial hepatitis B virus DNA quantification assays

Wild type HBx and truncated HBx: Pleiotropic regulators driving sequential genetic and epigenetic steps of hepatocarcinogenesis and progression of HBV‐associated neoplasms

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