Evidence map›Paper›PMID 28573087›Full record

ArticleWorld journal of virology2017

Structural and nucleic acid binding properties of hepatitis delta virus small antigen.

Carolina Alves, Hong Cheng, João Paulo Tavanez, Ana Casaca, Severin Gudima, Heinrich Roder, Celso Cunha

Abstract read
In one paragraph

Article in World journal of virology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Structure and nucleic acid interactions of the SProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Review
  4. 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

7 authors.

Carolina AlvesCarolina Alves, João Paulo Tavanez, Ana Casaca, Celso Cunha, Global Health and Tropical Medicine, GHTM, Instituto de Higiene e Medicina Tropical, IHMT, Universidade Nova de Lisboa, 1349-008 Lisboa, Portugal.
Hong ChengCarolina Alves, João Paulo Tavanez, Ana Casaca, Celso Cunha, Global Health and Tropical Medicine, GHTM, Instituto de Higiene e Medicina Tropical, IHMT, Universidade Nova de Lisboa, 1349-008 Lisboa, Portugal.
João Paulo TavanezCarolina Alves, João Paulo Tavanez, Ana Casaca, Celso Cunha, Global Health and Tropical Medicine, GHTM, Instituto de Higiene e Medicina Tropical, IHMT, Universidade Nova de Lisboa, 1349-008 Lisboa, Portugal.
Ana CasacaCarolina Alves, João Paulo Tavanez, Ana Casaca, Celso Cunha, Global Health and Tropical Medicine, GHTM, Instituto de Higiene e Medicina Tropical, IHMT, Universidade Nova de Lisboa, 1349-008 Lisboa, Portugal.
Severin GudimaCarolina Alves, João Paulo Tavanez, Ana Casaca, Celso Cunha, Global Health and Tropical Medicine, GHTM, Instituto de Higiene e Medicina Tropical, IHMT, Universidade Nova de Lisboa, 1349-008 Lisboa, Portugal.
Heinrich RoderCarolina Alves, João Paulo Tavanez, Ana Casaca, Celso Cunha, Global Health and Tropical Medicine, GHTM, Instituto de Higiene e Medicina Tropical, IHMT, Universidade Nova de Lisboa, 1349-008 Lisboa, Portugal.
Celso CunhaCarolina Alves, João Paulo Tavanez, Ana Casaca, Celso Cunha, Global Health and Tropical Medicine, GHTM, Instituto de Higiene e Medicina Tropical, IHMT, Universidade Nova de Lisboa, 1349-008 Lisboa, Portugal.

Funding

Super-infection and virus spread during chronic hepadnaviral infectionR01CA166213 · NCI · UNIVERSITY OF KANSAS MEDICAL CENTER · PI GUDIMA, SEVERIN O, MENNE, STEPHAN · 2012 to 2016
$1.6M
NCI NIH HHS R01 CA166213
6 · The paper itself

Abstract

aimTo further characterize the structure and nucleic acid binding properties of the 195 amino acid small delta antigen, S-HDAg, a study was made of a truncated form of S-HDAg, comprising amino acids 61-195 (∆60HDAg), thus lacking the domain considered necessary for dimerization and higher order multimerization.

methodsCircular dichroism, and nuclear magnetic resonance experiments were used to assess the structure of ∆60HDAg. Nucleic acid binding properties were investigated by gel retardation assays.

resultsResults showed that the truncated ∆60HDAg protein is intrinsically disordered but compact, whereas the RNA binding domain, comprising residues 94-146, adopts a dynamic helical conformation. We also found that ∆60HDAg fails to multimerize but still contains nucleic acid binding activity, indicating that multimerization is not essential for nucleic acid binding. Moreover, in agreement with what has been previously reported for full-length protein, no apparent specificity was found for the truncated protein regarding nucleic acid binding.

conclusionTaken together these results allowed concluding that ∆60HDAg is intrinsically disordered but compact; ∆60HDAg is not a multimer but is still capable of nucleic acid binding albeit without apparent specificity.

Indexed as

Circular dichroismDelta antigenHepatitis delta virusIntrinsically disordered proteinNuclear magnetic resonance

Identifiers

PMID28573087
PMCPMC5437381

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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.