Evidence map›Paper›PMID 36189721›Full record

ArticleActa crystallographica. Section F, Structural biology communications2022

Structure of the Monkeypox virus profilin-like protein A42R reveals potential functional differences from cellular profilins.

George Minasov, Nicole L Inniss, Ludmilla Shuvalova, Wayne F Anderson, Karla J F Satchell

Open access · hybridAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

16 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Exploring monkeypox virus proteins and rapid detection techniques.Frontiers in cellular and infection microbiology · 2024
    Review
  10. Article
  11. Identifying potential monkeypox virus inhibitors: anFrontiers in cellular and infection microbiology · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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

5 authors at 1 institution in 1 country.

George MinasovDepartment of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA.ORCID 0000-0001-5460-3462
Nicole L InnissDepartment of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA.
Ludmilla ShuvalovaCenter for Structural Genomics of Infectious Diseases, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA.ORCID 0000-0003-1702-6998
Wayne F AndersonCenter for Structural Genomics of Infectious Diseases, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA.
Karla J F SatchellDepartment of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA.
Northwestern University · US

Funding

TO PROVIDE SCIENTIFIC SUPPORT TO THE CENTERS FOR RESEARCH ON STRUCTURAL BIOLOGY OF INFECTIOUS DISEASES.75N93022C00035 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI SATCHELL, KARLA · 2022 to 2025
$20.7M
National Institute of Allergy and Infectious Diseases 75N9302200035NIAID NIH HHS 75N93022C00035
6 · The paper itself

Abstract

The infectious disease human monkeypox is spreading rapidly in 2022, causing a global health crisis. The genomics of Monkeypox virus (MPXV) have been extensively analyzed and reported, although little is known about the virus-encoded proteome. In particular, there are no reported experimental MPXV protein structures other than computational models. Here, a 1.52 Å resolution X-ray structure of the MPXV protein A42R, the first MPXV-encoded protein with a known structure, is reported. A42R shows structural similarity to profilins, which are cellular proteins that are known to function in the regulation of actin cytoskeletal assembly. However, structural comparison of A42R with known members of the profilin family reveals critical differences that support prior biochemical findings that A42R only weakly binds actin and does not bind poly(L-proline). In addition, the analysis suggests that A42R may make distinct interactions with phosphatidylinositol lipids. Overall, the data suggest that the role of A42R in the replication of orthopoxviruses may not be readily determined by comparison to cellular profilins. Furthermore, these findings support the need for increased efforts to determine high-resolution structures of other MPXV proteins to inform physiological studies of the poxvirus infection cycle and to reveal potential new strategies to combat human monkeypox should this emerging infectious disease with pandemic potential become more common in the future.

Indexed as

Mpox, MonkeypoxProfilinsActinsCrystallography, X-RayHumansMonkeypox virusPhosphatidylinositolsProteomeViral ProteinsActinsPhosphatidylinositolsProfilinsProteomeViral ProteinsactinCenter for Structural Genomics of Infectious Diseasesemerging infectious diseasesmonkeypoxpoxvirusesprofilinprofilin-like protein A42RX-ray structure

Identifiers

PMID36189721
PMCPMC9527652
OpenAlexW4297238507

What OpenQuestion holds

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LicenceCC BY
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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.