Evidence map›Paper›PMID 29968781›Full record

ArticleScientific reports2018

Enteric Species F Human Adenoviruses use Laminin-Binding Integrins as Co-Receptors for Infection of Ht-29 Cells.

Anandi Rajan, B David Persson, Lars Frängsmyr, Annelie Olofsson, Linda Sandblad, Jyrki Heino, Yoshikazu Takada, A Paul Mould, Lynn M Schnapp, Jason Gall and 1 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.9field-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

20 citing papers in PubMed, 34 citations in OpenAlex.

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  11. Adenovirus Structure: What Is New?International journal of molecular sciences · 2021
    Review
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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

11 authors at 5 institutions in 4 countries.

Anandi RajanDepartment of Clinical Microbiology/Virology, and, the Laboratory for Molecular Infection Medicine Sweden, Umeå University, Umeå, Sweden.
B David PerssonDepartment of Clinical Microbiology/Virology, and, the Laboratory for Molecular Infection Medicine Sweden, Umeå University, Umeå, Sweden.
Lars FrängsmyrDepartment of Clinical Microbiology/Virology, and, the Laboratory for Molecular Infection Medicine Sweden, Umeå University, Umeå, Sweden.
Annelie OlofssonDepartment of Molecular Biology, Umeå University, Umeå, Sweden.
Linda SandbladDepartment of Molecular Biology, Umeå University, Umeå, Sweden.
Jyrki HeinoDepartment of Biochemistry, University of Turku, Turku, Finland.
Yoshikazu TakadaDepartment of Dermatology, Biochemistry and Molecular Medicine, UC Davis School of Medicine, California, USA.
A Paul MouldBiomolecular Analysis Core Facility, Faculty of Biology, Medicine and Health, University of Manchester, Manchester, United Kingdom.
Lynn M SchnappDivision of Pulmonary, Critical Care, Allergy and Sleep Medicine, Medical University of South Carolina, Charleston, USA.
Jason GallVaccine Research Center (VRC), NIAID, NIH, Bethesda, USA.
Niklas ArnbergDepartment of Clinical Microbiology/Virology, and, the Laboratory for Molecular Infection Medicine Sweden, Umeå University, Umeå, Sweden. niklas.arnberg@umu.se.ORCID 0000-0002-7069-6678
Umeå University · SEMedical University of South Carolina · USUniversity of California, Davis · USUniversity of Manchester · GBUniversity of Turku · FI

Funding

Staff InvestigatorsP30CA093373 · NCI · UNIVERSITY OF CALIFORNIA DAVIS · PI Laura Marcu · 2002 to 2026
$84.9M
European Commission (EC) 290002NCI NIH HHS P30 CA093373
6 · The paper itself

Abstract

The enteric species F human adenovirus types 40 and 41 (HAdV-40 and -41) are the third most common cause of infantile gastroenteritis in the world. Knowledge about HAdV-40 and -41 cellular infection is assumed to be fundamentally different from that of other HAdVs since HAdV-40 and -41 penton bases lack the αV-integrin-interacting RGD motif. This motif is used by other HAdVs mainly for internalization and endosomal escape. We hypothesised that the penton bases of HAdV-40 and -41 interact with integrins independently of the RGD motif. HAdV-41 transduction of a library of rodent cells expressing specific human integrin subunits pointed to the use of laminin-binding α2-, α3- and α6-containing integrins as well as other integrins as candidate co-receptors. Specific laminins prevented internalisation and infection, and recombinant, soluble HAdV-41 penton base proteins prevented infection of human intestinal HT-29 cells. Surface plasmon resonance analysis demonstrated that HAdV-40 and -41 penton base proteins bind to α6-containing integrins with an affinity similar to that of previously characterised penton base:integrin interactions. With these results, we propose that laminin-binding integrins are co-receptors for HAdV-40 and -41.

Indexed as

Virus AttachmentAdenoviruses, HumanAnimalsCell LineCHO CellsCricetulusHT29 CellsHumansIntegrin alpha6Integrin alpha6beta4LamininReceptors, VirusSurface Plasmon ResonanceIntegrin alpha6Integrin alpha6beta4LamininReceptors, Virus

Identifiers

PMID29968781
PMCPMC6030200
OpenAlexW2810574893

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.