Evidence map›Paper›PMID 25994880›Full record

ArticleVirology journal2015

Crystal structure of the fibre head domain of bovine adenovirus 4, a ruminant atadenovirus.

Thanh H Nguyen, Márton Z Vidovszky, Mónika Z Ballmann, Marta Sanz-Gaitero, Abhimanyu K Singh, Balázs Harrach, Mária Benkő, Mark J van Raaij

Open access · goldAbstract read
In one paragraph

Article in Virology journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.7field-weighted citation impact, top 23% 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

5 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
  2. Review
  3. Adenovirus Structure: What Is New?International journal of molecular sciences · 2021
    Review
  4. Article
  5. 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

8 authors at 2 institutions in 3 countries.

Thanh H NguyenDepartamento de Estructura de Macromoleculas, Centro Nacional de Biotecnologia (CNB-CSIC), calle Darwin 3, 28049, Madrid, Spain. th.nguyen@cnb.csic.es.
Márton Z VidovszkyInstitute for Veterinary Medical Research, Centre for Agricultural Research, Hungarian Academy of Sciences, Budapest, Hungary. kisvido@googlemail.com.
Mónika Z BallmannInstitute for Veterinary Medical Research, Centre for Agricultural Research, Hungarian Academy of Sciences, Budapest, Hungary. sibilatrix@gmail.com.
Marta Sanz-GaiteroDepartamento de Estructura de Macromoleculas, Centro Nacional de Biotecnologia (CNB-CSIC), calle Darwin 3, 28049, Madrid, Spain. msanz@cnb.csic.es.
Abhimanyu K SinghDepartamento de Estructura de Macromoleculas, Centro Nacional de Biotecnologia (CNB-CSIC), calle Darwin 3, 28049, Madrid, Spain. A.K.Singh@kent.ac.uk.
Balázs HarrachInstitute for Veterinary Medical Research, Centre for Agricultural Research, Hungarian Academy of Sciences, Budapest, Hungary. harrach@vmri.hu.
Mária BenkőInstitute for Veterinary Medical Research, Centre for Agricultural Research, Hungarian Academy of Sciences, Budapest, Hungary. benko@vmri.hu.
Mark J van RaaijDepartamento de Estructura de Macromoleculas, Centro Nacional de Biotecnologia (CNB-CSIC), calle Darwin 3, 28049, Madrid, Spain. mjvanraaij@cnb.csic.es.
Centro Nacional de Biotecnología · ESConsejo Superior de Investigaciones Científicas · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundIn adenoviruses, primary host cell recognition is generally performed by the head domains of their homo-trimeric fibre proteins. This first interaction is reversible. A secondary, irreversible interaction subsequently takes place via other adenovirus capsid proteins and leads to a productive infection. Although many fibre head structures are known for human mastadenoviruses, not many animal adenovirus fibre head structures have been determined, especially not from those belonging to adenovirus genera other than Mastadenovirus.

methodsWe constructed an expression vector for the fibre head domain from a ruminant atadenovirus, bovine adenovirus 4 (BAdV-4), consisting of amino acids 414-535, expressed the protein in Escherichia coli, purified it by metal affinity and cation exchange chromatography and crystallized it. The structure was solved using single isomorphous replacement plus anomalous dispersion of a mercury derivative and refined against native data that extended to 1.2 Å resolution.

resultsLike in other adenoviruses, the BAdV-4 fibre head monomer contains a beta-sandwich consisting of ABCJ and GHID sheets. The topology is identical to the fibre head of the other studied atadenovirus, snake adenovirus 1 (SnAdV-1), including the alpha-helix in the DG-loop, despite of them having a sequence identity of only 15 %. There are also differences which may have implications for ligand binding. Beta-strands G and H are longer and differences in several surface-loops and surface charge are observed.

conclusionsChimeric adenovirus fibres have been used to retarget adenovirus-based anti-cancer and gene therapy vectors. Ovine adenovirus 7 (OAdV-7), another ruminant atadenovirus, is intensively tested as a basis for such a vector. Here, we present the high-resolution atomic structure of the BAdV-4 fibre head domain, the second atadenovirus fibre head structure known and the first of an atadenovirus that infects a mammalian host. Future research should focus on the receptor-binding properties of these fibre head domains.

Indexed as

AnimalsAtadenovirusCapsid ProteinsCattleCrystallography, X-RayModels, MolecularProtein ConformationCapsid Proteinshexon capsid protein, Adenovirus

Identifiers

PMID25994880
PMCPMC4451742
OpenAlexW1884369410

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.