Evidence map›Paper›PMID 42225430›Full record

ArticleACS applied materials & interfaces2026

Unveiling the Structural and Mechanical Diversity of SARS-CoV-2 Variants Using Atomic Force Microscopy.

Dominik Sziklai, Bálint Budavári, Bálint Kiss, Levente Herényi, Zoltán Kis, Bernadett Pályi, Miklós Kellermayer

Abstract read
In one paragraph

Article in ACS applied materials & interfaces, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

7 authors.

Dominik SziklaiDepartment of Biophysics and Radiation Biology, Semmelweis University, Budapest, Pest county1094, Hungary.ORCID 0000-0003-3590-7449
Bálint BudaváriDepartment of Biophysics and Radiation Biology, Semmelweis University, Budapest, Pest county1094, Hungary.
Bálint KissDepartment of Biophysics and Radiation Biology, Semmelweis University, Budapest, Pest county1094, Hungary.ORCID 0000-0002-1595-0426
Levente HerényiDepartment of Biophysics and Radiation Biology, Semmelweis University, Budapest, Pest county1094, Hungary.
Zoltán KisNational Biosafety Laboratory, National Center for Public Health and Pharmacy, Budapest, Pest county1097, Hungary.
Bernadett PályiNational Biosafety Laboratory, National Center for Public Health and Pharmacy, Budapest, Pest county1097, Hungary.
Miklós KellermayerDepartment of Biophysics and Radiation Biology, Semmelweis University, Budapest, Pest county1094, Hungary.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Understanding the structure and virion-host interaction of SARS-CoV-2 is crucial for elucidating the fundamental mechanisms of its assembly, stability, and transmission. These insights not only improve antiviral strategies but also contribute to a broader understanding of the nanoscale biological systems. Most studies of coronavirus focus primarily on viral genetics and on the structure and receptor affinity of the spike protein but overlook the broader mechanical and structural properties of the virion as a whole. Several studies have already suggested structural variability among coronavirus virions, and our work aims to provide more evidence of this matter. Here, we studied chemically fixed SARS-CoV-2 variants, focusing on wild-type, alpha, and delta variants. We used atomic force microscopy to acquire high-resolution topographic information. To estimate physically plausible virion envelope shapes, we utilized the Helfrich vesicle model as part of the analysis pipeline. We estimated viral geometry and adhesional compliance through reduced volume and its relationship with other geometrical parameters. We revealed consistent differences in apparent virion geometry across the three variants with alpha and delta displaying smaller fitted envelopes and lower reduced-volume estimates than wild-type under identical capture, fixation, and imaging conditions. Geometry-derived contact metrics also differed systematically among variants, consistent with differences in apparent deformation and compliance in this assay. Together, these descriptors establish a comparative framework for assessing the variant-dependent virion geometry and apparent deformation behavior.

Indexed as

COVID-19Microscopy, Atomic ForceSARS-CoV-2VirionHumansSpike Glycoprotein, CoronavirusSpike Glycoprotein, Coronavirusbending rigiditycoronavirusmembrane vesiclenanomechanicsnanoscale biophysicsstructural biologyvirion geometry

Identifiers

PMID42225430
PMCPMC13288390

What Socratic 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 Socratic graph.