Evidence map›Paper›PMID 34791819›Full record

ArticleChemistryOpen2021

Zn-Induced Interactions Between SARS-CoV-2 orf7a and BST2/Tetherin.

Maria Petrosino, Francesco Stellato, Roberta Chiaraluce, Valerio Consalvi, Giovanni La Penna, Alessandra Pasquo, Olivier Proux, Giancarlo Rossi, Silvia Morante

Open access · goldAbstract read
In one paragraph

Article in ChemistryOpen, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

14 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. The zinc proteome of SARS-CoV-2.Metallomics : integrated biometal science · 2022
    Article
  12. Multi-functional BST2/tetherin against HIV-1, other viruses and LINE-1.Frontiers in cellular and infection microbiology · 2022
    Review
  13. Article
  14. 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 at 5 institutions in 2 countries.

Maria PetrosinoDipartimento di Scienze Biochimiche "A. Rossi Fanelli", Sapienza Università di Roma, Piazzale Aldo Moro 5, 00185, Roma, Italy.ORCID http://orcid.org/0000-0001-7875-5954
Francesco StellatoDipartimento di Fisica, Università di Roma Tor Vergata and INFN, Via della Ricerca Scientifica, 1, 00133, Roma, Italy.ORCID http://orcid.org/0000-0001-8102-7982
Roberta ChiaraluceDipartimento di Scienze Biochimiche "A. Rossi Fanelli", Sapienza Università di Roma, Piazzale Aldo Moro 5, 00185, Roma, Italy.ORCID http://orcid.org/0000-0001-7748-2237
Valerio ConsalviDipartimento di Scienze Biochimiche "A. Rossi Fanelli", Sapienza Università di Roma, Piazzale Aldo Moro 5, 00185, Roma, Italy.ORCID http://orcid.org/0000-0003-2110-9630
Giovanni La PennaINFN - Sezione di Roma Tor Vergata, Via della Ricerca Scientifica, 1, 00133, Roma, Italy.ORCID http://orcid.org/0000-0002-8619-4867
Alessandra PasquoENEA CR Frascati, Diagnostics and Metrology Laboratory FSN-TECFIS-DIM, Via Enrico Fermi, 45, 00044, Frascati, RM.ORCID http://orcid.org/0000-0003-1808-6394
Olivier ProuxObservatoire des Sciences de l'Univers de Grenoble, UAR 832 CNRS, Universitè Grenoble Alpes, 38041, Grenoble, France.ORCID http://orcid.org/0000-0003-0385-1815
Giancarlo RossiDipartimento di Fisica, Università di Roma Tor Vergata and INFN, Via della Ricerca Scientifica, 1, 00133, Roma, Italy.ORCID http://orcid.org/0000-0001-9688-9454
Silvia MoranteDipartimento di Fisica, Università di Roma Tor Vergata and INFN, Via della Ricerca Scientifica, 1, 00133, Roma, Italy.ORCID http://orcid.org/0000-0002-3913-5733
Sapienza University of Rome · ITUniversity of Rome Tor Vergata · ITCentre National de la Recherche Scientifique · FRIstituto Nazionale di Fisica Nucleare, Roma Tor Vergata · ITNational Agency for New Technologies, Energy and Sustainable Economic Development · IT

Funding

BIOPHYS initiative (INFN (Italy)) MIUR-PRIN-201744NR8S
6 · The paper itself

Abstract

We present in this work a first X-ray Absorption Spectroscopy study of the interactions of Zn with human BST2/tetherin and SARS-CoV-2 orf7a proteins as well as with some of their complexes. The analysis of the XANES region of the measured spectra shows that Zn binds to BST2, as well as to orf7a, thus resulting in the formation of BST2-orf7a complexes. This structural information confirms the the conjecture, recently put forward by some of the present Authors, according to which the accessory orf7a (and possibly also orf8) viral protein are capable of interfering with the BST2 antiviral activity. Our explanation for this behavior is that, when BST2 gets in contact with Zn bound to the orf7a Cys

Indexed as

Antigens, CDBone Marrow Stromal Antigen 2CysteineGPI-Linked ProteinsHistidineHumansMolecular Dynamics SimulationProtein BindingSARS-CoV-2Viral ProteinsX-Ray Absorption SpectroscopyZincAntigens, CDBone Marrow Stromal Antigen 2BST2 protein, humanCysteineGPI-Linked ProteinsHistidineORF7a protein, SARS-CoV-2Viral ProteinsZincorf7a proteinSARS-CoV-2Tetherin/BST2XANESZn speciation

Identifiers

PMID34791819
PMCPMC8600262
OpenAlexW3214148112

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.