Changes in hepatitis B virus DNA‐polymerase activity in patients with chronic infection

Alberti, Alfredo; Pontisso, Patrizia; Realdi, Giuseppe

doi:10.1002/jmv.1890080402

Cited by 23 publications

(7 citation statements)

References 15 publications

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“…The IgG for conjugation was prepared from the serum of healthy HBsAg carrier by ionexchange chromatography and was positive for anti-HBc HBsAg, anti-HBc, HBeAg and anti-HBe were detected by commercially available RIA kits (Abbott Laboratories, Ltd., North Chicago, Ill.). HBV DNA polymerase levels in serum were measured by the method previously described (11).…”

Section: Methodsmentioning

confidence: 99%

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Differential Distribution of Hepatitis B Core and E Antigens in Hepatocytes: Analysis by Monoclonal Antibodies

et al. 1986

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Current knowledge on the expression of HBeAg in hepatocytes is incomplete because of difficulties in obtaining monospecific antisera devoid of anti-HBc reactivity. In this study, we have examined by immunofluorescence the expression of HBcAg and HBeAg in cryostat liver sections from 25 chronic carriers of HBsAg using monoclonal antibodies. Although virtually all liver biopsies displayed concordance for HBeAg and HBcAg expression, the pattern of fluorescence differed markedly. Thus, monoclonal anti-HBc gave nuclear staining in all 13 reactive biopsies, while cytoplasmic staining was observed in only two of these. In contrast, monoclonal anti-HBe showed cytoplasmic reactivity coexisting with nuclear reactivity in 10 of 13 reactive biopsies. Hepatitis B virus DNA polymerase activity in the serum appeared to correlate better with the presence of HBcAg in hepatocytes rather than HBeAg. These results provide further evidence that HBeAg is expressed both in the nuclei and in the cytoplasm of infected hepatocytes. The observation that the number of cells expressing HBeAg exceeds those expressing HBcAg in carriers with active virus replication would suggest that assembly of core particles occurs in only a proportion of infected hepatocytes expressing HBeAg.

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Section: Methodsmentioning

confidence: 99%

“…HBsAg, anti-HBc, HBeAg and anti-HBe were detected by commercially available RIA kits (Abbott Laboratories, Ltd., North Chicago, Ill.). HBV DNA polymerase levels in serum were measured by the method previously described (11).…”

Section: Monoclonal Anti-€€be and Anti-€€bementioning

confidence: 99%

Differential Distribution of Hepatitis B Core and E Antigens in Hepatocytes: Analysis by Monoclonal Antibodies

et al. 1986

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“…HBsAg titer was measured by RPHA (Hepatest, Wellcome). HBV-DNAP activity was measured by the method of Kaplan et al (18), recently modified in our laboratory (19).…”

Section: Hbv Markersmentioning

confidence: 99%

An Antibody Which Precipitates Dane Particles in Acute Hepatitis Type B: Relation to Receptor Sites Which Bind Polymerized Human Serum Albumin on Virus Particles

et al. 1984

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An antibody, which is distinct from the HBsAg- reacts with antigenic sites on Dane particles- HBcAg and HBeAg, was studied by radioimmunoprecipitation of radioactive intact hepatitis B virions in sera obtained early in the course of acute hepatitis type B. The antibody, previously termed anti-Dane particle (anti-DP) antibody, was reactive with Dane particles and HBsAg particles obtained from HBeAg-positive sera but not with HBsAg particles from anti-HBe containing sera. The expression on virus particles of the evoking antigen correlated with levels of binding sites for polymerized human serum albumin (pHSA) as detected by solid-phase radioimmunoassay. In acute hepatitis B sera, levels of anti-DP antibody activity showed inverse correlation with expression of pHSA receptors on circulating virus particles, although the two reactivities were not mutually exclusive. In inhibition experiments, pHSA blocked precipitation of Dane particles by anti-DP positive sera, while native human albumin and polymerized bovine albumin had no effect. The inhibition by pHSA of the anti-DP reaction appeared specific since identical concentrations of pHSA did not interfere with precipitation of virus particles by anti-HBs. Affinity chromatography studies with anti-DP insolubilized on Sepharose 4B columns showed selective binding to the gel of radioactive Dane particles; 125I-HBsAg was not reactive. The binding of Dane particles to anti-DP columns was completely inhibited when virus particles were applied to the gel in pHSA; pretreatment of the column with pHSA did not affect the reaction.(ABSTRACT TRUNCATED AT 250 WORDS)

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“…HBsAg activity was determined by a RIA test involving rabbit polyclonal IgG to serum HBsAg both in the solid phase as catcher and radiolabelled as tracer. HBV-associated endogenous DNA polymerase activity was analysed by the method described by Alberti et al (1981). HBV DNA was determined by hybridization according to Scotto et al (1983).…”

Section: Methodsmentioning

confidence: 99%

Antigenic Mapping of the Surface Proteins of Infectious Hepatitis B Virus Particles

Petit

Capel²,

Riottot³

et al. 1987

Journal of General Virology

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SUMMARYTo identify further the surface proteins of the native virus, hepatitis B virus (HBV) particles purified from HBe antigen (Ag)-positive human sera were used as immunogens to produce murine monoclonal antibody (MAb)-secreting hybridomas. The specific binding of antibodies to the HBV envelope (env) proteins was determined in indirect radioimmunoassay and by Western blot analysis. Six MAbs directed against major hepatitis B surface antigen (HBsAg) recognized conformational epitopes on S proteins (P24~/GP27~). Three preS2-specific MAbs reacted with the middle env proteins (GP33s/GP36 s) in the 22 nm HBsAg spherical particles. One MAb, F222, was found to react specifically with the two very large (VL) HBV surface proteins with Mr 54K and 66K. The epitope recognized by F222 was located on the protruding N terminus which, in the assembled virus particles, was readily split off by trypsin or V8 protease treatment. The presence of these VL proteins appeared to correspond to the presence of the large env proteins (P39s/GP429. The data described here indicate that F222 probably recognized an assembled topographic site which could be involved in virus entry into hepatocytes. Moreover, our results suggest that the preS-coded part of the HBV env proteins, which is sensitive to proteases in vitro, could be unstable in vivo and stabilized by immunoglobulins.

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Changes in hepatitis B virus DNA‐polymerase activity in patients with chronic infection

Cited by 23 publications

References 15 publications

Differential Distribution of Hepatitis B Core and E Antigens in Hepatocytes: Analysis by Monoclonal Antibodies

Differential Distribution of Hepatitis B Core and E Antigens in Hepatocytes: Analysis by Monoclonal Antibodies

An Antibody Which Precipitates Dane Particles in Acute Hepatitis Type B: Relation to Receptor Sites Which Bind Polymerized Human Serum Albumin on Virus Particles

Antigenic Mapping of the Surface Proteins of Infectious Hepatitis B Virus Particles

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