Evidence map›Paper›PMID 39714930›Full record

ArticleeLife2024

Virus adaptation to heparan sulfate comes with capsid stability tradeoff.

Han Kang Tee, Simon Crouzet, Arunima Muliyil, Gregory Mathez, Valeria Cagno, Matteo Dal Peraro, Aleksandar Antanasijevic, Sophie Clément, Caroline Tapparel

Abstract read
In one paragraph

Article in eLife, 2024. 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. Open questions in enterovirus uncoating.Journal of virology · 2026
    Review
  2. Serial passagingFrontiers in cellular and infection microbiology · 2026
    Article
  3. Article
  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

9 authors.

Han Kang TeeDepartment of Microbiology and Molecular Medicine, University of Geneva, Geneva, Switzerland.ORCID https://orcid.org/0000-0002-8975-0945
Simon CrouzetInterschool Institute of Bioengineering (SV), School of Life Sciences, École Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland.
Arunima MuliyilDepartment of Microbiology and Molecular Medicine, University of Geneva, Geneva, Switzerland.
Gregory MathezDepartment of Microbiology and Molecular Medicine, University of Geneva, Geneva, Switzerland.ORCID https://orcid.org/0000-0002-4453-7649
Valeria CagnoDepartment of Microbiology and Molecular Medicine, University of Geneva, Geneva, Switzerland.ORCID https://orcid.org/0000-0002-5597-334X
Matteo Dal PeraroInterschool Institute of Bioengineering (SV), School of Life Sciences, École Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland.
Aleksandar Antanasijevic *Global Health Institute, School of Life Sciences, École Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland.ORCID https://orcid.org/0000-0001-9452-8954
Sophie Clément *Department of Microbiology and Molecular Medicine, University of Geneva, Geneva, Switzerland.ORCID https://orcid.org/0000-0003-1348-4887
Caroline Tapparel *Department of Microbiology and Molecular Medicine, University of Geneva, Geneva, Switzerland.ORCID https://orcid.org/0000-0002-0411-6567

Funding

Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung 310030_184777Swiss national foundation Grant No 501100001711-10000300 and 501100001711-184777Swiss National Foundation 501100001711-10000300Swiss National Foundation 501100001711-184777
6 · The paper itself

Abstract

Because of high mutation rates, viruses constantly adapt to new environments. When propagated in cell lines, certain viruses acquire positively charged amino acids on their surface proteins, enabling them to utilize negatively charged heparan sulfate (HS) as an attachment receptor. In this study, we used enterovirus A71 (EV-A71) as the model and demonstrated that, unlike the parental MP4 variant, the cell-adapted strong HS-binder MP4-97R/167 G does not require acidification for uncoating and releases its genome in the neutral or weakly acidic environment of early endosomes. We experimentally confirmed that this pH-independent entry is not associated with the use of HS as an attachment receptor but rather with compromised capsid stability. We then extended these findings to another HS-dependent strain. In summary, our data indicate that the acquisition of capsid mutations conferring affinity for HS comes together with decreased capsid stability and allows EV-A71 to enter the cell via a pH-independent pathway. This pH-independent entry mechanism boosts viral replication in cell lines but may prove deleterious

Indexed as

CapsidHeparan SulfateAdaptation, PhysiologicalAnimalsCapsid ProteinsCell LineEnterovirusHumansHydrogen-Ion ConcentrationMutationProtein StabilityVirus InternalizationVirus ReplicationCapsid ProteinsHeparan SulfateEnterovirus A71heparan sulfateinfectious diseasemicrobiologyuncoatingvirus adaptationvirus capsid stabilityviruses

Identifiers

PMID39714930
PMCPMC11717363

What OpenQuestion holds

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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.