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Receptor binding and priming of the spike protein of SARS-CoV-2 for membrane fusion

Overview of attention for article published in Nature, September 2020
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About this Attention Score

  • In the top 5% of all research outputs scored by Altmetric
  • High Attention Score compared to outputs of the same age (98th percentile)
  • Above-average Attention Score compared to outputs of the same age and source (61st percentile)

Mentioned by

news
16 news outlets
twitter
176 tweeters
facebook
2 Facebook pages
reddit
3 Redditors

Citations

dimensions_citation
49 Dimensions

Readers on

mendeley
178 Mendeley
Title
Receptor binding and priming of the spike protein of SARS-CoV-2 for membrane fusion
Published in
Nature, September 2020
DOI 10.1038/s41586-020-2772-0
Pubmed ID
Authors

Donald J. Benton, Antoni G. Wrobel, Pengqi Xu, Chloë Roustan, Stephen R. Martin, Peter B. Rosenthal, John J. Skehel, Steven J. Gamblin

Abstract

SARS-CoV-2 infection is initiated by virus binding to ACE2 cell surface receptors1-4, followed by fusion of virus and cell membranes to release the virus genome into the cell. Both receptor binding and membrane fusion activities are mediated by the virus Spike glycoprotein, S5-7. As with other class I membrane fusion proteins, S is post-translationally cleaved, in this case by furin, into S1 and S2 components that remain associated following cleavage8-10. Fusion activation following receptor binding is proposed to involve the exposure of a second proteolytic site (S2'), cleavage of which is required for the fusion peptide release11,12. We have investigated the binding of ACE2 to the furin-cleaved form of SARS-CoV-2 S by cryoEM. We classify ten different molecular species including the unbound, closed spike trimer, the fully open ACE2-bound trimer, and dissociated monomeric S1 bound to ACE2. The ten structures describe ACE2 binding events which destabilise the spike trimer, progressively opening up, and out, the individual S1 components. The opening process reduces S1 contacts and un-shields the trimeric S2 core, priming fusion activation and dissociation of ACE2-bound S1 monomers. The structures also reveal refolding of an S1 subdomain following ACE2 binding, that disrupts interactions with S2, notably involving Asp61413-15, leading to destabilisation of the structure of S2 proximal to the secondary (S2') cleavage site.

Twitter Demographics

The data shown below were collected from the profiles of 176 tweeters who shared this research output. Click here to find out more about how the information was compiled.

Mendeley readers

The data shown below were compiled from readership statistics for 178 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 178 100%

Demographic breakdown

Readers by professional status Count As %
Researcher 34 19%
Student > Ph. D. Student 28 16%
Student > Bachelor 22 12%
Student > Master 12 7%
Professor 9 5%
Other 36 20%
Unknown 37 21%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 45 25%
Chemistry 17 10%
Agricultural and Biological Sciences 16 9%
Immunology and Microbiology 14 8%
Medicine and Dentistry 10 6%
Other 33 19%
Unknown 43 24%

Attention Score in Context

This research output has an Altmetric Attention Score of 216. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 20 January 2021.
All research outputs
#89,413
of 16,663,134 outputs
Outputs from Nature
#7,859
of 77,518 outputs
Outputs of similar age
#3,603
of 314,694 outputs
Outputs of similar age from Nature
#270
of 700 outputs
Altmetric has tracked 16,663,134 research outputs across all sources so far. Compared to these this one has done particularly well and is in the 99th percentile: it's in the top 5% of all research outputs ever tracked by Altmetric.
So far Altmetric has tracked 77,518 research outputs from this source. They typically receive a lot more attention than average, with a mean Attention Score of 88.7. This one has done well, scoring higher than 89% of its peers.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 314,694 tracked outputs that were published within six weeks on either side of this one in any source. This one has done particularly well, scoring higher than 98% of its contemporaries.
We're also able to compare this research output to 700 others from the same source and published within six weeks on either side of this one. This one has gotten more attention than average, scoring higher than 61% of its contemporaries.