Immunological and Morphological Properties of HBeAg Subtypes (HBeAg/1 and HBeAg/2) in Hepatitis B Virus Core Particles

Ohori, Hitoshi; Shimizu, Norio; Yamada, Erika; Onodera, Satoshi; Ishida, Nakao

doi:10.1099/0022-1317-65-2-405

Cited by 22 publications

(20 citation statements)

References 24 publications

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“…As reported in other papers (Ohori et al 1980a(Ohori et al , 1984Mackey et al 1981), HBcAg particles display their antigenic conversion from HBcAg to HBeAg accompanying with their morphological disintegration.…”

Section: Discussionsupporting

confidence: 68%

Establishment of passive hemagglutination assay (PHA) system for anti-HBc in plasma.

Uemura

Fukuyama

Nishida

et al. 1986

Tohoku J. Exp. Med.

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A sensitive and specific assay system for anti-HBc, the passive hemagglutination (PHA) method, has been established. The reactivity of PHA cells prepared by conjugating purified recombinant HBcAg-particles with fixed sheep blood cells (SRBC) was highly specific to monoclonal-and polyclonal anti-HBc IgGs. The sensitivity of PHA method was higher than that of radioimmunoassay (RIA). However, uncertainty for the positivity of anti-HBc still remained in plasma with the PHA titers lower than 25. A relatively high ratio (19%, 37 of 196) of anti-HBc-positive plasma, which had been confirmed to be HBsAg negative, was demonstrated in blood donors whose bloods have been considered suitable for transfusion. The hazards of anti-HBcpositive bloods and the importance of anti-HBc detection in plasma are discussed in this paper.

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Section: Discussionsupporting

confidence: 68%

Establishment of passive hemagglutination assay (PHA) system for anti-HBc in plasma.

Uemura

Fukuyama

Nishida

et al. 1986

Tohoku J. Exp. Med.

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“…Indeed, HBcAg was reported to be relatively stable at temperature as high as 65 8C[32,35]. Ohori et al[36] have demonstrated that the antigenicity of HBcAg was still active after 4 h incubation at 56 8C. Meanwhile, Naito et al…”

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confidence: 96%

The release of hepatitis B core antigen from Escherichia coli by batch mode bead milling

Tan

Kamarudin

et al. 2008

Process Biochemistry

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The performance of a batch model bead mill on the release of hepatitis B core antigen (HBcAg) from Escherichia coli was investigated in this study. The operating parameters examined were impeller tip speed (8-14 m/s), biomass concentration [5-20% (w/v)] and bead loading [65-80% (v/v)]. The highest yield (24.3 mg/g cell) and rate constant (0.471 l/min) of HBcAg release were achieved at impeller tip speed of 14 m/s. However, the high-shear stress under these operating conditions caused damage of the HBcAg. The highest yield (22.7 mg/g cell) and rate constant (0.344 l/ min) of HBcAg release were observed at biomass concentration of 20% (w/v). There was no significant effect of bead loading on the performance of bead milling being observed. In conclusion, the optimal operating condition for the release of HBcAg was at bead loading of 75% (v/v), biomass concentration of 20% (w/v) and impeller tip speed of 10 m/s.

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“…Thus, a plausible hypothesis is that the HBV core antigen binds to the regulatory region of the interferon gene and prevents transcription of the gene. However, another HBV antigen, the e antigen, is also encoded by the core antigen gene region (34) and hence is another potential candidate as the inhibitory factor.…”

Section: Discussionmentioning

confidence: 99%

Hepatitis B virus suppresses expression of human beta-interferon.

Twu

Lee

Lin

et al. 1988

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

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To determine whether hepatitis B virus (HBV) regulates the expression of the human fl-interferon gene, a series of recombinant bovine papilloma virus plasmids containing the human interferon gene and various fragments of the HBV genome were constructed and used to transform C127 cells, a murine fibroblast line. Analysis of the DNA from transformed C127 cells indicated that the interferon gene was intact and that the plasmids replicated as stable multicopy elements. The 1828-base-pair BamHI HBV DNA fragment containing the core antigen gene, but not the 2755-base-pairBgl II HBV DNA fragment encoding both the surface antigen and the X antigen, suppressed the production of human fl-interferon. No effect by any of the recombinant plasmids on the synthesis of murine interferon was detected. The suppression of human f-interferon by HBV occurs via a trans-acting factor.A frameshift mutation within the HBV core gene alleviates the inhibitory activity; thus we infer that the core protein is this factor or is crucially associated with this activity. was cloned into the same BamHI site of the plasmid pdBPV-1, which had one of the two BamHI sites destroyed (19). The resulting plasmids, pBHC and pBHS (Fig. 1), were used in further plasmid constructions. The plasmid pIFR containing the human Pinterferon gene as a 1.6-kilobase (kb) EcoRI-HindIII fragment (20) was linearized by digestion with EcoRI and the EcoRI ends were converted to HindIII ends. Following digestion with HindIII, the resulting 1.6-kb HindIII fragment containing the human 8-interferon gene was isolated and inserted into the HindIII site of (i) pdBPV-1, (it) pBHS, and (iii) pBHC, resulting in the formation of pBI, pBHSI, and pBHCI, respectively (Fig. 1).An insertion mutation at the Taq I site (mp 2014) that is within the HBV core antigen gene was created by digesting circularized 1828-bp BamHI HBV DNA fragments with Taq I. The linearized fragment was filled-in, ligated, and then cleaved with BamHI. The resulting BamHI HBV DNA fragment then was cloned into the BamHI site of pBI, yielding pBIHCdTaqI. The insertion mutation resulted in the destruction ofthe Taq I site in the HBV core antigen gene and in a shift in the open reading frame.Cell Cultures and DNA Transfections. Murine C127 fibroblasts were grown as described (20). One day before transfection, 8 x 104 cells were plated in each well of a 24-well plate; the cells were refed with fresh medium 4 hr before transfection. C127 cells were transfected by the calcium phosphate precipitation technique (21) with 0.2 Ag of total plasmid DNA that included 50 ng of a plasmid containing the neomycin-resistance gene. Eight hours after transfection, cells were diluted and G418 (600 ,ug/ml) was added. After 14-21 days, well-separated foci were picked and stable transformants were grown to confluence in the presence of G418.Interferon Induction and Assay. Induction of interferon by poly(I)-poly(C) in C127 cells that had been confluent for 4 days was performed as described (20). Uninduced cells were treated in t...

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Immunological and Morphological Properties of HBeAg Subtypes (HBeAg/1 and HBeAg/2) in Hepatitis B Virus Core Particles

Cited by 22 publications

References 24 publications

Establishment of passive hemagglutination assay (PHA) system for anti-HBc in plasma.

Establishment of passive hemagglutination assay (PHA) system for anti-HBc in plasma.

The release of hepatitis B core antigen from Escherichia coli by batch mode bead milling

Hepatitis B virus suppresses expression of human beta-interferon.

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