Evidence map›Paper›PMID 29566061›Full record

ArticlePloS one2018

Cold argon-oxygen plasma species oxidize and disintegrate capsid protein of feline calicivirus.

Hamada A Aboubakr, Sunil K Mor, LeeAnn Higgins, Anibal Armien, Mohammed M Youssef, Peter J Bruggeman, Sagar M Goyal

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

19 citing papers in PubMed, 57 citations in OpenAlex.

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  7. Effects of non-thermal atmospheric plasma on protein.Journal of clinical biochemistry and nutrition · 2022
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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

7 authors at 2 institutions in 2 countries.

Hamada A AboubakrDepartment of Veterinary Population Medicine and Veterinary Diagnostic Laboratory, College of Veterinary Medicine, University of Minnesota, St. Paul, MN, United States of America.ORCID 0000-0002-8233-2353
Sunil K MorDepartment of Veterinary Population Medicine and Veterinary Diagnostic Laboratory, College of Veterinary Medicine, University of Minnesota, St. Paul, MN, United States of America.
LeeAnn HigginsDepartment of Biochemistry, Molecular Biology, and Biophysics & Proteomics Center for Mass Spectrometry, University of Minnesota, St. Paul, MN, United States of America.
Anibal ArmienDepartment of Veterinary Population Medicine and Veterinary Diagnostic Laboratory, College of Veterinary Medicine, University of Minnesota, St. Paul, MN, United States of America.
Mohammed M YoussefFood Science and Technology Department, Faculty of Agriculture, Alexandria University, Aflaton St, El-Shatby, Alexandria, Egypt.
Peter J BruggemanDepartment of Mechanical Engineering, College of Science and Engineering, University of Minnesota, Minneapolis, MN, United States of America.
Sagar M GoyalDepartment of Veterinary Population Medicine and Veterinary Diagnostic Laboratory, College of Veterinary Medicine, University of Minnesota, St. Paul, MN, United States of America.
University of Minnesota · USAlexandria University · EG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Possible mechanisms that lead to inactivation of feline calicivirus (FCV) by cold atmospheric-pressure plasma (CAP) generated in 99% argon-1% O2 admixture were studied. We evaluated the impact of CAP exposure on the FCV viral capsid protein and RNA employing several cultural, molecular, proteomic and morphologic characteristics techniques. In the case of long exposure (2 min) to CAP, the reactive species of CAP strongly oxidized the major domains of the viral capsid protein (VP1) leading to disintegration of a majority of viral capsids. In the case of short exposure (15 s), some of the virus particles retained their capsid structure undamaged but failed to infect the host cells in vitro. In the latter virus particles, CAP exposure led to the oxidation of specific amino acids located in functional peptide residues in the P2 subdomain of the protrusion (P) domain, the dimeric interface region of VP1 dimers, and the movable hinge region linking the S and P domains. These regions of the capsid are known to play an essential role in the attachment and entry of the virus to the host cell. These observations suggest that the oxidative effect of CAP species inactivates the virus by hindering virus attachment and entry into the host cell. Furthermore, we found that the oxidative impact of plasma species led to oxidation and damage of viral RNA once it becomes unpacked due to capsid destruction. The latter effect most likely plays a secondary role in virus inactivation since the intact FCV genome is infectious even after damage to the capsid.

Indexed as

ArgonPlasma GasesVirus InactivationAnimalsArgon Plasma CoagulationCaliciviridae InfectionsCalicivirus, FelineCapsid ProteinsCat DiseasesCatsCells, CulturedCold TemperatureOxidation-ReductionOxygenProteolysisArgonCapsid ProteinsOxygenPlasma Gases

Identifiers

PMID29566061
PMCPMC5864060
OpenAlexW2790346053

What OpenQuestion 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 OpenQuestion graph.