Evidence map›Paper›PMID 35312342›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

A tethered ligand assay to probe SARS-CoV-2:ACE2 interactions.

Magnus S Bauer, Sophia Gruber, Adina Hausch, Priscila S F C Gomes, Lukas F Milles, Thomas Nicolaus, Leonard C Schendel, Pilar López Navajas, Erik Procko, Daniel Lietha and 4 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
–field-weighted citation impact
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

30 citing papers in PubMed.

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  3. UltrastrongScience advances · 2025
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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

14 authors.

Magnus S BauerDepartment of Physics, LMU Munich, 80799 Munich, Germany.ORCID 0000-0003-1357-2852
Sophia GruberDepartment of Physics, LMU Munich, 80799 Munich, Germany.
Adina HauschDepartment of Physics, LMU Munich, 80799 Munich, Germany.
Priscila S F C GomesDepartment of Physics, Auburn University, Auburn, AL 36849.ORCID 0000-0001-7370-9596
Lukas F MillesDepartment of Biochemistry, University of Washington, Seattle, WA 98195.ORCID 0000-0001-8417-3205
Thomas NicolausDepartment of Physics, LMU Munich, 80799 Munich, Germany.
Leonard C SchendelDepartment of Physics, LMU Munich, 80799 Munich, Germany.ORCID 0000-0002-1986-2693
Pilar López NavajasCentro de Investigaciones Biológicas Margarita Salas, Spanish National Research Council, 28040 Madrid, Spain.
Erik ProckoDepartment of Biochemistry, University of Illinois, Urbana, IL 61801.ORCID 0000-0002-0028-490X
Daniel LiethaCentro de Investigaciones Biológicas Margarita Salas, Spanish National Research Council, 28040 Madrid, Spain.ORCID 0000-0002-6133-6486
Marcelo C R MeloDepartment of Physics, Auburn University, Auburn, AL 36849.ORCID 0000-0001-6901-1646
Rafael C BernardiDepartment of Physics, Auburn University, Auburn, AL 36849.ORCID 0000-0003-0758-2026
Hermann E GaubDepartment of Physics, LMU Munich, 80799 Munich, Germany.ORCID 0000-0002-4220-6088
Jan LipfertDepartment of Physics, LMU Munich, 80799 Munich, Germany.ORCID 0000-0003-3613-7896

Funding

Auburn University (AU)Cofunded by the European Regional Development Fund (FEDER)Deutsche Forschungsgemeinschaft (DFG) 111166240Deutsche Forschungsgemeinschaft (DFG) 386143268European Molecular Biology Organization (EMBO) ALTF 1047-2019Physics Department of the LMU MunichSpanish Ministry of Science, Innovation and Universities for the Spanish State Research Agency Retos Grant RTI2018-099318-B-I00
6 · The paper itself

Abstract

SignificanceIn the dynamic environment of the airways, where SARS-CoV-2 infections are initiated by binding to human host receptor ACE2, mechanical stability of the viral attachment is a crucial fitness advantage. Using single-molecule force spectroscopy techniques, we mimic the effect of coughing and sneezing, thereby testing the force stability of SARS-CoV-2 RBD:ACE2 interaction under physiological conditions. Our results reveal a higher force stability of SARS-CoV-2 binding to ACE2 compared to SARS-CoV-1, causing a possible fitness advantage. Our assay is sensitive to blocking agents preventing RBD:ACE2 bond formation. It will thus provide a powerful approach to investigate the modes of action of neutralizing antibodies and other agents designed to block RBD binding to ACE2 that are currently developed as potential COVID-19 therapeutics.

Indexed as

Host-Pathogen InteractionsAngiotensin-Converting Enzyme 2COVID-19Disease SusceptibilityHumansProtein BindingSARS-CoV-2Angiotensin-Converting Enzyme 2AFMforce spectroscopyhost–pathogen interactionsmagnetic tweezersSARS-CoV-2

Identifiers

PMID35312342
PMCPMC9168514

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.