Basic-liver, pancreas, and biliary tractMapping of the Hepatitis B Virus Attachment Site by Use of Infection-Inhibiting preS1 Lipopeptides and Tupaia Hepatocytes
Section snippets
Isolation and Purification of Hepatitis B Virus Virions and Subviral Particles From Plasma of Hepatitis B Virus–Infected Patients
HBV and natural HBs antigen (HBsAg; genotype D; HBsAg subtype ayw2) were isolated from hepatitis B early antigen (HBeAg)-positive plasma of 2 asymptomatic chronic HBV carriers with normal transaminase levels in serum. One carrier (ID304) had 1.6 × 109 HBV genomes per milliliter and 55 μg/mL HBsAg, and the second (ID259) had 2 × 109 HBV genomes per milliliter and 10 μg/mL HBsAg.
The purification was performed as previously described,19 with some modifications: HBV and subviral particles from 350
Inhibition of Hepatitis B Virus Infection of Primary Tupaia Hepatocytes by Myristoylated Peptides
For HBV infection of tupaia hepatocytes, we used highly purified plasma-derived HBV particles that contained less than 10% subviral HBsAg particles. We determined HBeAg secretion of infected cells as a marker of an established infection, because HBeAg is a nonstructural viral protein and therefore not present in the purified viral input. The amount of secreted HBeAg is approximately proportional to the amount of infectious HBV in the inoculum.10
We have shown previously that infection of primary
Discussion
Our previous study10 suggested that both the preS1 and S-domains of the HBs protein could be involved in the attachment and uptake of HBV by primary tupaia hepatocyte cultures because certain MAbs against both the preS1 and the S-domain inhibited the infection process very efficiently. The data of this study fully support the importance of the preS1 domain for the infection process at the level of attachment. Surprisingly, a role of the SHBs or the HBsAg epitopes in the S-domain for the
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Supported by Grants SFB 535/A2 (to W.H.G.) and UR72/4-1/4-2 (to S.U.) from the Deutsche Forschungsgemeinschaft and European Union Grant QLK2-2000-01476 (to K.S. and W.H.G.).
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D.G. and S.U. contributed equally to this work.