Evidence map›Paper›PMID 26418008›Full record

ArticlePloS one2015

Structure and Sialyllactose Binding of the Carboxy-Terminal Head Domain of the Fibre from a Siadenovirus, Turkey Adenovirus 3.

Abhimanyu K Singh, M Álvaro Berbís, Mónika Z Ballmann, Michelle Kilcoyne, Margarita Menéndez, Thanh H Nguyen, Lokesh Joshi, F Javier Cañada, Jesús Jiménez-Barbero, Mária Benkő and 2 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed, 1 pooled it
2.7field-weighted citation impact, top 9% 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, 1 synthesis or guideline pooled it, 31 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Adenovirus Structure: What Is New?International journal of molecular sciences · 2021
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Polysialic acid is a cellular receptor for human adenovirus 52.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  15. Article
  16. Article
  17. Article
  18. Review
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

12 authors at 7 institutions in 3 countries.

Abhimanyu K SinghDepartamento de Estructura de Macromoléculas, Centro Nacional de Biotecnología (CNB-CSIC), Madrid, Spain.
M Álvaro BerbísDepartamento de Biología Física-Química, Centro de Investigaciones Biológicas (CIB-CSIC), Madrid, Spain.
Mónika Z BallmannInstitute for Veterinary Medical Research, Centre for Agricultural Research, Hungarian Academy of Sciences, Budapest, Hungary.
Michelle KilcoyneGlycoscience Group, National Centre for Biomedical Engineering Science, National University of Ireland Galway, Galway, Ireland; Microbiology, School of Natural Sciences, National University of Ireland Galway, Galway, Ireland.
Margarita MenéndezDepartamento de Química Física-Biológica, Instituto de Química Física Rocasolano (IQFR-CSIC) and CIBER de Enfermedades Respiratorias (CIBERES), calle Serrano 119, E-28006 Madrid, Spain.
Thanh H NguyenDepartamento de Estructura de Macromoléculas, Centro Nacional de Biotecnología (CNB-CSIC), Madrid, Spain.
Lokesh JoshiGlycoscience Group, National Centre for Biomedical Engineering Science, National University of Ireland Galway, Galway, Ireland.
F Javier CañadaDepartamento de Biología Física-Química, Centro de Investigaciones Biológicas (CIB-CSIC), Madrid, Spain.
Jesús Jiménez-BarberoDepartamento de Biología Física-Química, Centro de Investigaciones Biológicas (CIB-CSIC), Madrid, Spain; Centro de Investigación Cooperativa en Biociencias (CIC bioGUNE), Parque Tecnológico de Bizkaia, Derio, Spain; Ikerbasque, Basque Foundation for Science, Bilbao, Spain.
Mária BenkőInstitute for Veterinary Medical Research, Centre for Agricultural Research, Hungarian Academy of Sciences, Budapest, Hungary.
Balázs HarrachInstitute for Veterinary Medical Research, Centre for Agricultural Research, Hungarian Academy of Sciences, Budapest, Hungary.
Mark J van RaaijDepartamento de Estructura de Macromoléculas, Centro Nacional de Biotecnología (CNB-CSIC), Madrid, Spain.
Centro Nacional de Biotecnología · ESCentre for Agricultural Research · HUCentro de Investigaciones Biológicas Margarita Salas · ESOllscoil na Gaillimhe – University of Galway · IECentro de Investigación Biomédica en Red de Enfermedades Respiratorias · ESCIC bioGUNE · ESHUN-REN Veterinary Medical Research Institute · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The virulent form of turkey adenovirus 3 (TAdV-3), also known as turkey hemorrhagic enteritis virus (THEV), is an economically important poultry pathogen, while the avirulent form is used as a vaccine. TAdV-3 belongs to the genus Siadenovirus. The carboxy-terminal region of its fibre does not have significant sequence similarity to any other adenovirus fibre heads of known structure. Two amino acid sequence differences between virulent and avirulent TAdV-3 map on the fibre head: where virulent TAdV-3 contains Ile354 and Thr376, avirulent TAdV-3 contains Met354 and Met376. We determined the crystal structures of the trimeric virulent and avirulent TAdV-3 fibre head domains at 2.2 Å resolution. Each monomer contains a beta-sandwich, which, surprisingly, resembles reovirus fibre head more than other adenovirus fibres, although the ABCJ-GHID topology is conserved in all. A beta-hairpin insertion in the C-strand of each trimer subunit embraces its neighbouring monomer. The avirulent and virulent TAdV-3 fibre heads are identical apart from the exact orientation of the beta-hairpin insertion. In vitro, sialyllactose was identified as a ligand by glycan microarray analysis, nuclear magnetic resonance spectroscopy, and crystallography. Its dissociation constant was measured to be in the mM range by isothermal titration calorimetry. The ligand binds to the side of the fibre head, involving amino acids Glu392, Thr419, Val420, Lys421, Asn422, and Gly423 binding to the sialic acid group. It binds slightly more strongly to the avirulent form. We propose that, in vivo, the TAdV-3 fibre may bind a sialic acid-containing cell surface component.

Indexed as

Protein Structure, TertiaryAmino Acid SequenceBinding SitesCalorimetryCarbohydrate ConformationCarbohydrate SequenceCrystallography, X-RayLactoseMagnetic Resonance SpectroscopyModels, MolecularMolecular Sequence DataMutationPolysaccharidesProtein BindingSiadenovirusSialic AcidsLactoseN-acetylneuraminoyllactosePolysaccharidesSialic AcidsViral Proteins

Identifiers

PMID26418008
PMCPMC4587935
OpenAlexW2272469972

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.