Evidence map›Paper›PMID 41064641›Full record

ArticleFrontiers in cellular and infection microbiology2025

Vitamin D-inducible antimicrobial peptide LL-37 binds SARS-CoV-2 Spike and accessory proteins ORF7a and ORF8.

Annika Roth, Steffen Lütke, Matthias Mörgelin, Denise Meinberger, Gabriele Hermes, Gerhard Sengle, Manuel Koch, Marco Drexelius, Jan Gebauer, Ines Neundorf and 4 more

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In one paragraph

Article in Frontiers in cellular and infection microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

14 authors.

Annika Roth *Institute for Clinical Chemistry, Medical Faculty and University Hospital Cologne, University of Cologne, Cologne, Germany.
Steffen Lütke *Department of Pediatrics and Adolescent Medicine, Faculty of Medicine and University Hospital Cologne, University of Cologne, Cologne, Germany.
Matthias MörgelinDivision of Infection Medicine, Department of Clinical Sciences, Lund University, Lund, Sweden.
Denise MeinbergerInstitute for Clinical Chemistry, Medical Faculty and University Hospital Cologne, University of Cologne, Cologne, Germany.
Gabriele HermesInstitute for Clinical Chemistry, Medical Faculty and University Hospital Cologne, University of Cologne, Cologne, Germany.
Gerhard SengleDepartment of Pediatrics and Adolescent Medicine, Faculty of Medicine and University Hospital Cologne, University of Cologne, Cologne, Germany.
Manuel KochCenter for Biochemistry, Medical Faculty and University Hospital Cologne, Cologne, Germany.
Marco DrexeliusInstitute for Biochemistry, Department of Chemistry, Faculty of Mathematics and Natural Sciences, University of Cologne, Cologne, Germany.
Jan GebauerInstitute for Biochemistry, Department of Chemistry, Faculty of Mathematics and Natural Sciences, University of Cologne, Cologne, Germany.
Ines NeundorfInstitute for Biochemistry, Department of Chemistry, Faculty of Mathematics and Natural Sciences, University of Cologne, Cologne, Germany.
Dzemal ElezagicInstitute for Clinical Chemistry, Medical Faculty and University Hospital Cologne, University of Cologne, Cologne, Germany.
Mats PaulssonCenter for Biochemistry, Medical Faculty and University Hospital Cologne, Cologne, Germany.
Thomas StreichertInstitute for Clinical Chemistry, Medical Faculty and University Hospital Cologne, University of Cologne, Cologne, Germany.
Andreas R KlattInstitute for Clinical Chemistry, Medical Faculty and University Hospital Cologne, University of Cologne, Cologne, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Background: The role of vitamin D in Coronavirus Disease 2019 (COVID-19) outcomes remains debated, but emerging evidence suggests it may enhance recovery by strengthening immune responses. Vitamin D upregulates LL-37, an antimicrobial peptide with broad antiviral activity, including potential benefits against SARS-CoV-2. LL-37's interactions with viral proteins, however, remain incompletely understood. Methods: We investigated LL-37's interactions with the SARS-CoV-2 Spike glycoprotein and the accessory proteins ORF7a and ORF8 using surface plasmon resonance and negative-stain electron microscopy. These approaches were employed to assess LL-37's binding capabilities and potential impact on viral infectivity. Results: LL-37 bound multiple domains of the Spike protein and inhibited its interaction with the human angiotensin-converting enzyme 2 (hACE2) receptor Conclusions: LL-37 disrupts key viral-host interactions by binding to Spike, ORF7a, and ORF8, thereby reducing SARS-CoV-2 infectivity. These findings highlight LL-37's potential as a therapeutic agent in COVID-19 and provide mechanistic insight into its antiviral actions.

Indexed as

Antimicrobial Cationic PeptidesCathelicidinsSARS-CoV-2Spike Glycoprotein, CoronavirusViral ProteinsViral Regulatory and Accessory ProteinsVitamin DAngiotensin-Converting Enzyme 2Antimicrobial PeptidesAntiviral AgentsCOVID-19HumansProtein BindingACE2 protein, humanAngiotensin-Converting Enzyme 2Antimicrobial Cationic PeptidesAntimicrobial PeptidesAntiviral AgentsCathelicidinsORF8 protein, SARS-CoV-2Spike Glycoprotein, Coronavirusspike protein, SARS-CoV-2Viral ProteinsViral Regulatory and Accessory ProteinsVitamin DCOVID-19LL-37ORF7aORF8SARS-CoV-2Spikesurface plasmon resonancevitamin D

Identifiers

PMID41064641
PMCPMC12500691

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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.