Evidence map›Paper›PMID 31220181›Full record

ArticlePLoS pathogens2019

Vaccinia viral A26 protein is a fusion suppressor of mature virus and triggers membrane fusion through conformational change at low pH.

Hung-Wei Chang, Cheng-Han Yang, Yu-Chun Luo, Bo-Gang Su, Huei-Yin Cheng, Shu-Yun Tung, Kathleen Joyce D Carillo, Yi-Ting Liao, Der-Lii M Tzou, Hao-Ching Wang and 1 more

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

23 citing papers in PubMed, 39 citations in OpenAlex.

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  9. Methods to Study Poxvirus Structures by Cryo-EM Imaging Modalities.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
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  11. Article
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  13. Article
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  15. Article
  16. The Art of Viral Membrane Fusion and Penetration.Sub-cellular biochemistry · 2023
    Article
  17. Article
  18. Article
  19. Article
  20. 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

11 authors at 4 institutions in 1 country.

Hung-Wei ChangInstitute of Molecular Biology, Academia Sinica, Taipei, Taiwan.
Cheng-Han YangInstitute of Molecular Biology, Academia Sinica, Taipei, Taiwan.
Yu-Chun LuoInstitute of Molecular Biology, Academia Sinica, Taipei, Taiwan.
Bo-Gang SuInstitute of Molecular Biology, Academia Sinica, Taipei, Taiwan.
Huei-Yin ChengInstitute of Molecular Biology, Academia Sinica, Taipei, Taiwan.
Shu-Yun TungInstitute of Molecular Biology, Academia Sinica, Taipei, Taiwan.
Kathleen Joyce D CarilloSustainable Chemical Science and Technology Program, Taiwan International Graduate Program, Academia Sinica, Taipei, Taiwan.
Yi-Ting LiaoThe Ph.D. Program for Translational Medicine, College of Medical Science and Technology, Taipei Medical University and Academia Sinica, Taipei, Taiwan.
Der-Lii M TzouSustainable Chemical Science and Technology Program, Taiwan International Graduate Program, Academia Sinica, Taipei, Taiwan.
Hao-Ching WangThe Ph.D. Program for Translational Medicine, College of Medical Science and Technology, Taipei Medical University and Academia Sinica, Taipei, Taiwan.ORCID 0000-0003-2396-717X
Wen ChangInstitute of Molecular Biology, Academia Sinica, Taipei, Taiwan.ORCID 0000-0003-3369-083X
Institute of Molecular Biology, Academia Sinica · TWTaipei Medical University · TWNational Chiayi University · TWNational Yang Ming Chiao Tung University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vaccinia mature virus requires A26 envelope protein to mediate acid-dependent endocytosis into HeLa cells in which we hypothesized that A26 protein functions as an acid-sensitive membrane fusion suppressor. Here, we provide evidence showing that N-terminal domain (aa1-75) of A26 protein is an acid-sensitive region that regulates membrane fusion. Crystal structure of A26 protein revealed that His48 and His53 are in close contact with Lys47, Arg57, His314 and Arg312, suggesting that at low pH these His-cation pairs could initiate conformational changes through protonation of His48 and His53 and subsequent electrostatic repulsion. All the A26 mutant mature viruses that interrupted His-cation pair interactions of His48 and His 53 indeed have lost virion infectivity. Isolation of revertant viruses revealed that second site mutations caused frame shifts and premature termination of A26 protein such that reverent viruses regained cell entry through plasma membrane fusion. Together, we conclude that viral A26 protein functions as an acid-sensitive fusion suppressor during vaccinia mature virus endocytosis.

Indexed as

EndocytosisMembrane FusionVirus InternalizationAnimalsChlorocebus aethiopsHeLa CellsHumansHydrogen-Ion ConcentrationMiceVaccinia virusViral ProteinsViral Proteins

Identifiers

PMID31220181
PMCPMC6605681
OpenAlexW2952688132

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.