Evidence map›Paper›PMID 31315999›Full record

ArticleJournal of virology2019

Membrane Protein of Human Coronavirus NL63 Is Responsible for Interaction with the Adhesion Receptor.

Antonina Naskalska, Agnieszka Dabrowska, Artur Szczepanski, Aleksandra Milewska, Krzysztof Piotr Jasik, Krzysztof Pyrc

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
8.8field-weighted citation impact, top 1% 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

40 citing papers in PubMed, 80 citations in OpenAlex.

  1. Review
  2. Review
  3. Structural proteins of human coronaviruses: what makes them different?Frontiers in cellular and infection microbiology · 2024
    Review
  4. Article
  5. Article
  6. Cell surface nucleocapsid protein expression: A betacoronavirus immunomodulatory strategy.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Structure and dynamics of membrane protein in SARS-CoV-2.Journal of biomolecular structure & dynamics · 2022
    Article
  12. Review
  13. Is heparan sulfate a target for inhibition of RNA virus infection?American journal of physiology. Cell physiology · 2022
    Review
  14. Article
  15. Article
  16. Glycosylation of SARS-CoV-2: structural and functional insights.Analytical and bioanalytical chemistry · 2021
    Review
  17. TheEmerging microbes & infections · 2021
    Article
  18. Article
  19. Review
  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

6 authors at 2 institutions in 1 country.

Antonina NaskalskaVirogenetics Laboratory of Virology, Malopolska Centre of Biotechnology, Jagiellonian University, Krakow, Poland antonina.naskalska@uj.edu.pl k.a.pyrc@uj.edu.pl.ORCID 0000-0002-5868-1000
Agnieszka DabrowskaVirogenetics Laboratory of Virology, Malopolska Centre of Biotechnology, Jagiellonian University, Krakow, Poland.
Artur SzczepanskiVirogenetics Laboratory of Virology, Malopolska Centre of Biotechnology, Jagiellonian University, Krakow, Poland.
Aleksandra MilewskaVirogenetics Laboratory of Virology, Malopolska Centre of Biotechnology, Jagiellonian University, Krakow, Poland.
Krzysztof Piotr JasikSchool of Pharmacy, Division of Laboratory Medicine, Medical University of Silesia in Katowice, Sosnowiec, Poland.ORCID 0000-0003-3974-6507
Krzysztof PyrcVirogenetics Laboratory of Virology, Malopolska Centre of Biotechnology, Jagiellonian University, Krakow, Poland antonina.naskalska@uj.edu.pl k.a.pyrc@uj.edu.pl.ORCID 0000-0002-3867-7688
Jagiellonian University · PLMedical University of Silesia · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human coronavirus NL63 (HCoV-NL63) is a common respiratory virus that causes moderately severe infections. We have previously shown that the virus uses heparan sulfate proteoglycans (HSPGs) as the initial attachment factors, facilitating viral entry into the cell. In the present study, we show that the membrane protein (M) of HCoV-NL63 mediates this attachment. Using viruslike particles lacking the spike (S) protein, we demonstrate that binding to the cell is not S protein dependent. Furthermore, we mapped the M protein site responsible for the interaction with HSPG and confirmed its relevance using a viable virus. Importantly,

Indexed as

Virus AttachmentAnimalsCell LineCoronavirus NL63, HumanHeparan Sulfate ProteoglycansPlatelet Glycoprotein GPIb-IX ComplexViral Matrix Proteinsadhesion receptorHeparan Sulfate ProteoglycansPlatelet Glycoprotein GPIb-IX ComplexViral Matrix ProteinsattachmentHCoV-NL63heparan sulfate proteoglycansmembrane proteinviruslike particles

Identifiers

PMID31315999
PMCPMC6744225
OpenAlexW2963084573

What OpenQuestion holds

Textmetadata
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.