Evidence map›Paper›PMID 8709225›Full record

ArticleJournal of virology1996

Characterization of a 120-Kilodalton pre-S-binding protein as a candidate duck hepatitis B virus receptor.

J S Li, S P Tong, J R Wands

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.8field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 37 citations in OpenAlex.

  1. Primary Duck Hepatocyte Culture and Duck Hepatitis B Virus Infection Model.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  2. Review
  3. Review
  4. Virus entry mediated by hepatitis B virus envelope proteins.World journal of gastroenterology · 2013
    Review
  5. Article
  6. Article
  7. Hepatitis B virus-cell interactions and pathogenesis.Journal of cellular physiology · 2008
    Review
  8. Article
  9. Review
  10. Molecular characterization of duck hepatitis B virus isolated from Hubei brown ducks.Journal of Huazhong University of Science and Technology. Medical sciences = Hua zhong ke ji da xue xue bao. Yi xue Ying De wen ban = Huazhong keji daxue xuebao. Yixue Yingdewen ban · 2006
    Article
  11. Article
  12. Article
  13. Study of the early steps of the Hepatitis B Virus life cycle.International journal of medical sciences · 2004
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

J S LiMolecular Hepatology Laboratory, Massachusetts General Hospital Cancer Center, Charlestown, Massachusetts 02129, USA.
S P Tong
J R Wands
Massachusetts General Hospital · US

Funding

STUDY OF HBV AND/OR VARIANTS IN ALCOHOLICSR01AA008169 · NIAAA · RHODE ISLAND HOSPITAL (PROVIDENCE, RI) · PI WANDS, JACK R · 1989 to 2011
$3.9M
PATHOGENESIS, IMMUNODIAGNOSIS AND THERAPY OF HCCR37CA035711 · NCI · RHODE ISLAND HOSPITAL (PROVIDENCE, RI) · PI WANDS, JACK R · 2000 to 2008
$2.9M
PATHOGENESIS, IMMUNODIAGNOSIS, AND THERAPY OF HCCR01CA035711 · NCI · RHODE ISLAND HOSPITAL (PROVIDENCE, RI) · PI WANDS, JACK R · 1985 to 1999
–
NCI NIH HHS CA-35711NIAAA NIH HHS AA-08169
6 · The paper itself

Abstract

Infection by human and animal hepadnaviruses displays remarkable host and tissue tropism. The infection cycle probably initiates with binding of the pre-S domain of viral envelope protein to surface receptors present on the hepatocyte. Three types of neutralizing monoclonal antibodies against duck hepatitis B virus (DHBV) have their binding sites clustered within residues 83 to 107 of the pre-S protein, suggesting that this region may constitute a major receptor binding site. A 170- or 180-kDa duck protein (p170 or gp180) which binds DHBV particles through this part of the pre-S sequence has been identified recently. Although the p170 binding protein is host (duck) specific, its distribution is not restricted to DHBV-infectible tissues. Using the pre-S protein fused to glutathione S-transferase and immobilized on Sepharose beads, we have now identified an additional binding protein with a size of 120 kDa (p120). p120 expression is restricted to the liver, kidney, and pancreas, the three major organs of DHBV replication. While optimal p170 binding requires an intact pre-S protein, binding to p120 occurs much more efficiently with a few N- or C-terminally truncated forms. The p120 binding site was mapped to residues 98 to 102 of the pre-S region, which overlaps with a cluster of known virus-neutralizing epitopes. Site-directed mutagenesis revealed residues 100 to 102 (Phe-Arg-Arg) as the critical p120 contact site; nonconservative substitution in any of the three positions abolished p120 binding. Double mutations at positions 100 to 102 markedly reduced DHBV infectivity in cell culture. Short pre-S peptides covering the clustered neutralizing epitopes (also p170 and p120 binding sites) reduced DHBV infectivity in primary duck hepatocyte cultures. Thus, p120 represents a candidate component of the DHBV receptor complex.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCells, CulturedDucksEpitopesGene Products, envHepatitis B Virus, DuckHumansKidneyLiverMolecular Sequence DataMolecular WeightMutagenesis, Site-DirectedOrgan SpecificityPancreasEpitopesGene Products, envReceptors, VirusRecombinant Fusion Proteins

Identifiers

PMID8709225
PMCPMC190623
OpenAlexW2139676754

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.