Evidence map›Paper›PMID 25116391›Full record

ArticleVirus research2014

The SARS Coronavirus 3a protein binds calcium in its cytoplasmic domain.

Rinki Minakshi, Kartika Padhan, Safikur Rehman, Md Imtaiyaz Hassan, Faizan Ahmad

Open access · greenAbstract read
In one paragraph

Article in Virus research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact, top 88% 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

15 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Review
  3. Viroporins: Structure, function, and their role in the life cycle of SARS-CoV-2.The international journal of biochemistry & cell biology · 2022
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Computed optical spectra of SARS-CoV-2 proteins.Chemical physics letters · 2020
    Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Severe acute respiratory syndrome coronavirus ORF3a protein activates the NLRP3 inflammasome by promoting TRAF3-dependent ubiquitination of ASC.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    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 3 institutions in 2 countries.

Rinki MinakshiInternational Centre for Genetic Engineering and Biotechnology, New Delhi, India; Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India. Electronic address: rinki.minakshi@hotmail.com.
Kartika PadhanInternational Centre for Genetic Engineering and Biotechnology, New Delhi, India.
Safikur RehmanCentre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India.
Md Imtaiyaz HassanCentre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India.
Faizan AhmadCentre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India.
Jamia Millia Islamia · INInternational Centre for Genetic Engineering and Biotechnology · ITInternational Centre for Genetic Engineering and Biotechnology · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) is a positive stranded RNA virus with ∼30kb genome. Among all open reading frames (orfs) of this virus, the orf3a is the largest, and encodes a protein of 274 amino acids, named as 3a protein. Sequence analysis suggests that the orf3a aligned to one calcium pump present in Plasmodium falciparum and the enzyme glutamine synthetase found in Leptospira interrogans. This sequence similarity was found to be limited only to amino acid residues 209-264 which form the cytoplasmic domain of the orf3a. Furthermore, this region was predicted to be involved in the calcium binding. Owing to this hypothesis, we were driven to establish its calcium binding property in vitro. Here, we expressed and purified the cytoplasmic domain of the 3a protein, called Cyto3a, as a recombinant His-tagged protein in the E. coli. The calcium binding nature was established by performing various staining methods such as ruthenium red and stains-all. (45)Ca overlay method was also done to further support the data. Since the 3a protein forms ion channels, we were interested to see any conformational changes occurring in the Cyot3a upon calcium binding, using fluorescence spectroscopy and circular dichroism. These studies clearly indicate a significant change in the conformation of the Cyto3a protein after binding with calcium. Our results strongly suggest that the cytoplasmic domain of the 3a protein of SARS-CoV binds calcium in vitro, causing a change in protein conformation.

Indexed as

Amino Acid SequenceCalciumCytoplasmHumansMolecular Sequence DataProtein ConformationProtein Structure, TertiarySevere Acute Respiratory SyndromeSevere acute respiratory syndrome-related coronavirusViral Envelope ProteinsViral ProteinsViroporin Proteins3a protein, SARS-CoVCalciumViral Envelope ProteinsViral ProteinsViroporin ProteinsCalciumCyto3a proteinIon channelProtein conformationSARS-CoV

Identifiers

PMID25116391
PMCPMC7114474
OpenAlexW2070069376

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.