Evidence map›Paper›PMID 30274351›Full record

ArticleViruses2018

Respiratory Syncytial Virus Matrix (M) Protein Interacts with Actin In Vitro and in Cell Culture.

Shadi Shahriari, Ke-Jun Wei, Reena Ghildyal

Open access · goldAbstract read
In one paragraph

Article in Viruses, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed, 1 pooled it
2.6field-weighted citation impact, top 10% 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

31 citing papers in PubMed, 1 synthesis or guideline pooled it, 47 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Journal of virology · 2022
    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

3 authors at 1 institution in 1 country.

Shadi ShahriariCentre for Research in Therapeutic Solutions, Faculty of Science and Technology, University of Canberra, Canberra ACT 2617, Australia. shadi.shahriari@canberra.edu.au.
Ke-Jun WeiCentre for Research in Therapeutic Solutions, Faculty of Science and Technology, University of Canberra, Canberra ACT 2617, Australia. kejunw2000@yahoo.com.
Reena GhildyalCentre for Research in Therapeutic Solutions, Faculty of Science and Technology, University of Canberra, Canberra ACT 2617, Australia. Reena.Ghildyal@canberra.edu.au.
University of Canberra · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The virus⁻host protein interactions that underlie respiratory syncytial virus (RSV) assembly are still not completely defined, despite almost 60 years of research. RSV buds from the apical surface of infected cells, once virion components have been transported to the budding sites. Association of RSV matrix (M) protein with the actin cytoskeleton may play a role in facilitating this transport. We have investigated the interaction of M with actin in vitro and cell culture. Purified wildtype RSV M protein was found to bind directly to polymerized actin in vitro. Vero cells were transfected to express full-length M (1⁻256) as a green fluorescent protein-(GFP) tagged protein, followed by treatment with the microfilament destabilizer, cytochalasin D. Destabilization of the microfilament network resulted in mislocalization of full-length M, from mostly cytoplasmic to diffused across both cytoplasm and nucleus, suggesting that M interacts with microfilaments in this system. Importantly, treatment of RSV-infected cells with cytochalasin D results in lower infectious virus titers, as well as mislocalization of M to the nucleus. Finally, using deletion mutants of M in a transfected cell system, we show that both the N- and C-terminus of the protein are required for the interaction. Together, our data suggest a possible role for M⁻actin interaction in transporting virion components in the infected cell.

Indexed as

ActinsAnimalsBiological TransportCell LineCell NucleusChlorocebus aethiopsCytochalasin DCytoplasmGene DeletionHumansProtein BindingRespiratory Syncytial Virus, HumanRespiratory Syncytial Virus InfectionsViral Matrix ProteinsVirionVirus AssemblyActinsCytochalasin DViral Matrix Proteinsactin cytoskeletonmatrix proteinrespiratory syncytial virusvirus transport

Identifiers

PMID30274351
PMCPMC6213044
OpenAlexW2894614613

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.