Evidence map›Paper›PMID 26487711›Full record

ArticleProtein engineering, design & selection : PEDS2015

Reconstitution of the receptor-binding motif of the SARS coronavirus.

Natalia T Freund, Anna Roitburd-Berman, Jianhua Sui, Wayne A Marasco, Jonathan M Gershoni

Open access · bronzeAbstract read
In one paragraph

Article in Protein engineering, design & selection : PEDS, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.2field-weighted citation impact, top 42% 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

12 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. [Comparative analysis of structural characteristics and epitopes in S proteins between SARS-CoV-2 and SARS-CoV].Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2020
    Article
  9. The 2019 coronavirus: Learning curves, lessons, and the weakest link.International journal of clinical practice · 2020
    Article
  10. Article
  11. B-cell restriction - an alternative piece to the puzzle.Human vaccines & immunotherapeutics · 2019
    Article
  12. Review
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 3 countries.

Natalia T FreundDepartment of Cell Research and Immunology, The George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel Present address: Laboratory of Molecular Immunology, The Rockefeller University, New York, NY 10065, USA.
Anna Roitburd-BermanDepartment of Cell Research and Immunology, The George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel.
Jianhua SuiDepartment of Cancer Immunology and AIDS, Dana Farber Cancer Institute Department of Medicine, Harvard Medical School, Boston, MA 02115, USA Present address: National Institute of Biological Sciences, Beijing 102206, China.
Wayne A MarascoDepartment of Cancer Immunology and AIDS, Dana Farber Cancer Institute Department of Medicine, Harvard Medical School, Boston, MA 02115, USA.
Jonathan M GershoniDepartment of Cell Research and Immunology, The George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel gershoni@tauex.tau.ac.il.
Tel Aviv University · ILDana-Farber Cancer Institute · USNational Institute of Biological Sciences, Beijing · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The severe acute respiratory syndrome (SARS) coronavirus (CoV) identified in 2003 has infected ∼8000 people worldwide, killing nearly 10% of them. The infection of target cells by the SARS CoV is mediated through the interaction of the viral Spike (S) protein (1255 amino acids) and its cellular receptor, angiotensin-converting enzyme 2 (ACE2). The SARS CoV receptor-binding domain (amino acids N318-T509 of S protein) harbors an extended excursion along its periphery that contacts ACE2 and is designated the receptor-binding motif (RBM, amino acids S432-T486). In addition, the RBM is a major antigenic determinant, able to elicit production of neutralizing antibodies. Hence, the role of the RBM is a bi-functional bioactive surface that can be demonstrated by antibodies such as the neutralizing human anti-SARS monoclonal antibody (mAb) 80R which targets the RBM and competes with the ACE2 receptor for binding. Here, we employ phage-display peptide-libraries to reconstitute a functional RBM. This is achieved by generating a vast collection of candidate RBM peptides that present a diversity of conformations. Screening such 'Conformer Libraries' with corresponding ligands has produced short RBM constructs (ca. 40 amino acids) that can bind both the ACE2 receptor and the neutralizing mAb 80R.

Indexed as

Peptide LibraryAmino Acid MotifsAmino Acid SequenceAngiotensin-Converting Enzyme 2Binding SitesHumansModels, MolecularMolecular Sequence DataPeptide FragmentsPeptidyl-Dipeptidase ASevere acute respiratory syndrome-related coronavirusSpike Glycoprotein, CoronavirusACE2 protein, humanAngiotensin-Converting Enzyme 2Peptide FragmentsPeptide LibraryPeptidyl-Dipeptidase ASpike Glycoprotein, Coronavirusbioactive peptideconformational libraryphage-displayvirus spike

Identifiers

PMID26487711
PMCPMC7107155
OpenAlexW2279048742

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.