Aetiological Agent of Enterically Transmitted Non-A, Non-B Hepatitis

Bradley, Daniel W.; Andjaparidze, A. G.; Cook, E. H.; McCaustland, Karen A.; Balayan, M. S.; Stetler, Harrison C.; Velazquez, Oscar; Robertson, Betty H.; Humphrey, Charles D.; Kane, Mark; Weisfuse, Isaac B.

doi:10.1099/0022-1317-69-3-731

Cited by 140 publications

(76 citation statements)

References 19 publications

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“…It contains a protein of about 76K on S D S -P A G E and Western blotting. All these biophysical characteristics suggest that HEV is similar to caliciviruses, as other investigators have suggested (Arankalle et al, 1988;Bradley et al, 1988). Reyes et al (1990) have recently reported that HEV might be a new virus of the Caliciviridae family, and Tam et al (1991) suggested that HEV represents either the prototype member of an as yet unclassified novel virus family or perhaps a separate genus within the Caliciviridae.…”

Section: Discussionmentioning

confidence: 55%

Isolation and identification of hepatitis E virus in Xinjiang, China

Huang

Wei

et al. 1992

Journal of General Virology

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Section: Discussionmentioning

confidence: 55%

Isolation and identification of hepatitis E virus in Xinjiang, China

Huang

Wei

et al. 1992

Journal of General Virology

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“…The virus cannot be propagated efficiently in vitro. HEV isolated from patients is a small, non-enveloped, single positive-stranded RNA virus with an isosahedral capsid of average 30-nm diameter (4). The viral genome of 7.5 kilobases is organized as three open reading frames; open reading frame 1 maps to the 5Ј terminus and encodes a non-structural protein, open reading frame 2 maps to the 3Ј terminus and encodes for a major structural protein, and open reading frame 3 overlaps both and encodes a thus far unknown function (5).…”

Section: Hepatitis E Virus (Hev)mentioning

confidence: 99%

Mutational Analysis of Essential Interactions Involved in the Assembly of Hepatitis E Virus Capsid

Zhang

et al. 2005

Journal of Biological Chemistry

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The hepatitis E virus (HEV) capsid consists of a single structural protein, a portion of which is engaged in isosahedral contact to form a basal shell, and another portion in dimeric contact to form the homodimers protruding from the shell. Previous studies revealed that homodimers of the truncated HEV capsid proteins, E2 (amino acids 394 -606) and p239 (amino acids 368 -606), model dominant antigenic determinants of HEV. Immunization with these proteins protected rhesus monkeys against the virus, and three monoclonal antibodies against the homodimers could neutralize HEV infectivity and/or immune-capture of the virus. Furthermore, homodimers of p239 further interact to form particles of 23 nm diameter, rendering it an efficacious candidate vaccine. In light of this we postulate that the interactions involved in the formation of the homodimers and particles might be similar to those involved in assembly of the virus capsid. Presently, mutational analysis was carried out to identify these sites of interactions. The site of dimeric interactions was located to a cluster of six hydrophobic amino acids residues, Ala 597 , Val 598 , Ala 599 , Leu 601 , and Ala 602 ; furthermore, the site involved in particle formation was located at amino acids 368 -394. The possibility that these sites are also involved in assembly of the virus capsid is supported by the fact that they are located at two major and highly conserved hydrophobic regions of the HEV structural protein.

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“…Hepatitis E virus (HEV) is a small, non-enveloped, single positive-stranded RNA virus with an icosahedral capsid of approximately 30 nm diameter (Bradley et al, 1988). The viral genome of 7.5 kb is organized as three open reading frames (ORFs).…”

Section: Introductionmentioning

confidence: 99%

Role of heat-shock protein 90 in hepatitis E virus capsid trafficking

Zheng

Jiang

Zhao

et al. 2010

Journal of General Virology

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p239 is a virus-like particle constituted from hepatitis E virus (HEV) recombinant proteins. It can be used as a surrogate for HEV and as an investigative tool to study cellular interactions because of its ability to adsorb to and penetrate HepG2 cellular membranes. Our objective was to use p239 to define the role of HEV capsid proteins during the early stages of infection. Pull-down and MALDI-TOF MS experiments identified three host-cell proteins, Grp 78/Bip, a-tubulin and heatshock protein 90 (HSP90), and the latter was investigated further. Antibodies to p239 alone or HSP90 alone could detect p239 or HSP90, suggesting the formation of a complex between p239 and HSP90. In the HepG2 cell, geldanamycin (GA), an HSP90-specific inhibitor, blocked intracellular transportation of p239, but had no effect on the binding and cellular entry of p239, suggesting that HSP90 was important for HEV capsid intracellular transportation. RT-PCR results showed that the efficiency of wild-type HEV infection was inhibited significantly by GA treatment, suggesting the importance of HSP90 in virus infectivity. It was concluded that HSP90 plays a crucial role in the intracellular transportation of viral capsids in the early stage of HEV infection.

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Aetiological Agent of Enterically Transmitted Non-A, Non-B Hepatitis

Cited by 140 publications

References 19 publications

Isolation and identification of hepatitis E virus in Xinjiang, China

Isolation and identification of hepatitis E virus in Xinjiang, China

Mutational Analysis of Essential Interactions Involved in the Assembly of Hepatitis E Virus Capsid

Role of heat-shock protein 90 in hepatitis E virus capsid trafficking

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