Evidence map›Paper›PMID 29674446›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Polysialic acid is a cellular receptor for human adenovirus 52.

Annasara Lenman, A Manuel Liaci, Yan Liu, Lars Frängsmyr, Martin Frank, Bärbel S Blaum, Wengang Chai, Iva I Podgorski, Balázs Harrach, Mária Benkő and 3 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
9.9field-weighted citation impact, top 2% 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

57 citing papers in PubMed, 91 citations in OpenAlex.

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  14. Construction and application of adenoviral vectors.Molecular therapy. Nucleic acids · 2023
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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

13 authors at 6 institutions in 6 countries.

Annasara LenmanDivision of Virology, Department of Clinical Microbiology, and Laboratory for Molecular Infection Medicine Sweden, Umeå University, SE-90185 Umeå, Sweden; annasara.lenman@umu.se thilo.stehle@uni-tuebingen.de.
A Manuel LiaciInterfaculty Institute of Biochemistry, University of Tübingen, D-72076 Tübingen, Germany.
Yan LiuGlycosciences Laboratory, Department of Medicine, Imperial College London, W12 0NN London, United Kingdom.
Lars FrängsmyrDivision of Virology, Department of Clinical Microbiology, and Laboratory for Molecular Infection Medicine Sweden, Umeå University, SE-90185 Umeå, Sweden.
Martin FrankBiognos AB, SE-40274 Gothenburg, Sweden.
Bärbel S BlaumInterfaculty Institute of Biochemistry, University of Tübingen, D-72076 Tübingen, Germany.
Wengang ChaiGlycosciences Laboratory, Department of Medicine, Imperial College London, W12 0NN London, United Kingdom.
Iva I PodgorskiInstitute for Veterinary Medical Research, Centre for Agricultural Research, Hungarian Academy of Sciences, H-1143 Budapest, Hungary.
Balázs HarrachInstitute for Veterinary Medical Research, Centre for Agricultural Research, Hungarian Academy of Sciences, H-1143 Budapest, Hungary.
Mária BenkőInstitute for Veterinary Medical Research, Centre for Agricultural Research, Hungarian Academy of Sciences, H-1143 Budapest, Hungary.
Ten FeiziGlycosciences Laboratory, Department of Medicine, Imperial College London, W12 0NN London, United Kingdom.
Thilo StehleInterfaculty Institute of Biochemistry, University of Tübingen, D-72076 Tübingen, Germany; annasara.lenman@umu.se thilo.stehle@uni-tuebingen.de.
Niklas ArnbergDivision of Virology, Department of Clinical Microbiology, and Laboratory for Molecular Infection Medicine Sweden, Umeå University, SE-90185 Umeå, Sweden.ORCID 0000-0002-7069-6678
Clovis Oncology (United Kingdom) · GBHUN-REN Veterinary Medical Research Institute · HUUmeå University · SEUniversity of Tübingen · DEBiognos (Sweden) · SEVanderbilt University · US

Funding

Wellcome Trust WT093378MA/Z/10/ZWellcome Trust WT099197/Z/12/Z
6 · The paper itself

Abstract

Human adenovirus 52 (HAdV-52) is one of only three known HAdVs equipped with both a long and a short fiber protein. While the long fiber binds to the coxsackie and adenovirus receptor, the function of the short fiber in the virus life cycle is poorly understood. Here, we show, by glycan microarray analysis and cellular studies, that the short fiber knob (SFK) of HAdV-52 recognizes long chains of α-2,8-linked polysialic acid (polySia), a large posttranslational modification of selected carrier proteins, and that HAdV-52 can use polySia as a receptor on target cells. X-ray crystallography, NMR, molecular dynamics simulation, and structure-guided mutagenesis of the SFK reveal that the nonreducing, terminal sialic acid of polySia engages the protein with direct contacts, and that specificity for polySia is achieved through subtle, transient electrostatic interactions with additional sialic acid residues. In this study, we present a previously unrecognized role for polySia as a cellular receptor for a human viral pathogen. Our detailed analysis of the determinants of specificity for this interaction has general implications for protein-carbohydrate interactions, particularly concerning highly charged glycan structures, and provides interesting dimensions on the biology and evolution of members of

Indexed as

Molecular Dynamics SimulationAdenoviruses, HumanCell Line, TumorHumansSialic Acidspolysialic acidSialic Acidsglycan microarrayglycan receptorhuman adenoviruspolysialic acidshort fiber

Identifiers

PMID29674446
PMCPMC5939068
OpenAlexW2800567031

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.