Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Failure of the lamivudine-resistant rtM204I hepatitis B virus mutants to efficiently support hepatitis delta virus secretion.

Journal of virology - 1 May 2005

Vietheer P T K, Netter H J, Sozzi T, Bartholomeusz A

Abstract excerpt

Hepatitis delta virus (HDV) is encapsidated by the envelope proteins of hepatitis B virus (HBV). The major HBV lamivudine (LMV)-resistant mutations in the polymerase gene within the reverse transcriptase (rt) region at rtM204V or rtM204I are associated with changes in the overlapping envelope gene products, in particular, the gene encoding small envelope protein (s) at sI195M or sW196L/S/Stop. We have...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Antigens, Viral
Share to Blotting, Northern
Share to Drug Resistance, Viral

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hepatitis B Surface Antigens

Share to Hepatitis B virus

Share to Hepatitis Delta Virus

Share to Lamivudine

Share to Reverse Transcriptase Inhibitors

Source

Open in PubMed Open full text

Identifiers

PMID: 15858045
DOI: 10.1128/JVI.79.10.6570-6573.2005
PMCID: PMC1091693

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Failure of the lamivudine-resistant rtM204I hepatitis B virus mutants to efficiently support hepatitis delta virus secretion.PMID 15858045Read ↗

Decreased infectivity of nucleoside analogs-resistant hepatitis B virus mutants.Semantic proximity Read ↗

Restoration of replication phenotype of lamivudine-resistant hepatitis B virus mutants by compensatory changes in the "fingers" subdomain of the viral polymerase selected as a consequence of mutations in the overlapping S gene.Semantic proximity Read ↗

Drug resistance mutations of hepatitis B virus (HBV) influence the yield of the virions of the human hepatitis delta virus (HDV) and their infectivity.Semantic proximity Read ↗

The antiviral drug selected hepatitis B virus rtA181T/sW172* mutant has a dominant negative secretion defect and alters the typical profile of viral rebound.Semantic proximity Read ↗

Variable influence of mutational patterns in reverse-transcriptase domain on replication capacity of hepatitis B virus isolates from antiviral-experienced patients.Semantic proximity Read ↗

The rtL229 substitutions in the reverse transcriptase region of hepatitis B virus (HBV) polymerase are potentially associated with lamivudine resistance as a compensatory mutationSemantic proximity Read ↗

Deficiency in virion secretion and decreased stability of the hepatitis B virus immune escape mutant G145R.Semantic proximity Read ↗

Lamivudine resistance and other mutations in the polymerase and surface antigen genes of hepatitis B virus associated with a fatal hepatic failure case.Semantic proximity Read ↗

The hepatitis B virus polymerase mutation rtV173L is selected during lamivudine therapy and enhances viral replication in vitro.Semantic proximity Read ↗

Selection of a secretion-incompetent mutant in the serum of a patient with severe hepatitis B.Semantic proximity Read ↗

High frequency of complex mutational patterns in lamivudine resistant hepatitis B virus isolates.Semantic proximity Read ↗

Comparison of replication competence of wild-type and lamivudine-resistant hepatitis B virus isolates from a chronic hepatitis B patient.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.