Evidence map›Paper›PMID 38448991›Full record

ArticleVirology journal2024

Aspergillus fumigatus secretes a protease(s) that displays in silico binding affinity towards the SARS-CoV-2 spike protein and mediates SARS-CoV-2 pseudovirion entry into HEK-293T cells.

Nozethu Mjokane, Eric O Akintemi, Saheed Sabiu, Onele M N Gcilitshana, Jacobus Albertyn, Carolina H Pohl, Olihile M Sebolai

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Virology journal, 2024. 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
1.2field-weighted citation impact, top 24% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. 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

7 authors at 2 institutions in 1 country.

Nozethu MjokaneDepartment of Microbiology and Biochemistry, University of the Free State, 205 Nelson Mandela Drive, Park West, 9301, Bloemfontein, South Africa.
Eric O AkintemiDepartment of Microbiology and Biochemistry, University of the Free State, 205 Nelson Mandela Drive, Park West, 9301, Bloemfontein, South Africa.
Saheed SabiuDepartment of Biotechnology and Food Science, Faculty of Applied Science, Durban University of Technology, 4000, Durban, P.O. Box 1334, South Africa.
Onele M N GcilitshanaDepartment of Microbiology and Biochemistry, University of the Free State, 205 Nelson Mandela Drive, Park West, 9301, Bloemfontein, South Africa.
Jacobus AlbertynDepartment of Microbiology and Biochemistry, University of the Free State, 205 Nelson Mandela Drive, Park West, 9301, Bloemfontein, South Africa.
Carolina H PohlDepartment of Microbiology and Biochemistry, University of the Free State, 205 Nelson Mandela Drive, Park West, 9301, Bloemfontein, South Africa.
Olihile M SebolaiDepartment of Microbiology and Biochemistry, University of the Free State, 205 Nelson Mandela Drive, Park West, 9301, Bloemfontein, South Africa. sebolaiom@ufs.ac.za.
University of the Free State · ZADurban University of Technology · ZA

Funding

Medical Research Council of South Africa SIR grantNational Research Foundation of South Africa grant no. 137965Poliomyelitis Research Foundation of South Africa grant no. 23/78
6 · The paper itself

Abstract

backgroundThe novel coronavirus disease of 2019 (COVID-19) is an infectious disease caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2). Data from the COVID-19 clinical control case studies showed that this disease could also manifest in patients with underlying microbial infections such as aspergillosis. The current study aimed to determine if the Aspergillus (A.) fumigatus culture media (i.e., supernatant) possessed protease activity that was sufficient to activate the SARS-CoV-2 spike protein.

methodsThe supernatant was first analysed for protease activity. Thereafter, it was assessed to determine if it possessed proteolytic activity to cleave a fluorogenic mimetic peptide of the SARS-CoV-2 spike protein that contained the S1/S2 site and a full-length spike protein contained in a SARS-CoV-2 pseudovirion. To complement this, a computer-based tool, HADDOCK, was used to predict if A. fumigatus alkaline protease 1 could bind to the SARS-CoV-2 spike protein.

resultsWe show that the supernatant possessed proteolytic activity, and analyses of the molecular docking parameters revealed that A. fumigatus alkaline protease 1 could bind to the spike protein. To confirm the in silico data, it was imperative to provide experimental evidence for enzymatic activity. Here, it was noted that the A. fumigatus supernatant cleaved the mimetic peptide as well as transduced the HEK-293T cells with SARS-CoV-2 pseudovirions.

conclusionThese results suggest that A. fumigatus secretes a protease(s) that activates the SARS-CoV-2 spike protein. Importantly, should these two infectious agents co-occur, there is the potential for A. fumigatus to activate the SARS-CoV-2 spike protein, thus aggravating COVID-19 development.

Indexed as

COVID-19Peptide HydrolasesAspergillus fumigatusHEK293 CellsHumansMolecular Docking SimulationPeptidesSARS-CoV-2Spike Glycoprotein, CoronavirusPeptide HydrolasesPeptidesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2A. Fumigatus alkaline protease 1Aspergillus (A) fumigatusHaddockHEK-293T cellsSARS-CoV-2 spike proteinSupernatantTransduction

Identifiers

PMID38448991
PMCPMC10919004
OpenAlexW4392519935

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.