Cold argon-oxygen plasma species oxidize and disintegrate capsid protein of feline calicivirus.
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 an...
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doaj-02548812aa0d406db19cbc64bf7bcb1f2020-11-24T21:47:46ZengPublic Library of Science (PLoS)PLoS ONE1932-62032018-01-01133e019461810.1371/journal.pone.0194618Cold argon-oxygen plasma species oxidize and disintegrate capsid protein of feline calicivirus.Hamada A AboubakrSunil K MorLeeAnn HigginsAnibal ArmienMohammed M YoussefPeter J BruggemanSagar M GoyalPossible 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.http://europepmc.org/articles/PMC5864060?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Hamada A Aboubakr Sunil K Mor LeeAnn Higgins Anibal Armien Mohammed M Youssef Peter J Bruggeman Sagar M Goyal |
spellingShingle |
Hamada A Aboubakr Sunil K Mor LeeAnn Higgins Anibal Armien Mohammed M Youssef Peter J Bruggeman Sagar M Goyal Cold argon-oxygen plasma species oxidize and disintegrate capsid protein of feline calicivirus. PLoS ONE |
author_facet |
Hamada A Aboubakr Sunil K Mor LeeAnn Higgins Anibal Armien Mohammed M Youssef Peter J Bruggeman Sagar M Goyal |
author_sort |
Hamada A Aboubakr |
title |
Cold argon-oxygen plasma species oxidize and disintegrate capsid protein of feline calicivirus. |
title_short |
Cold argon-oxygen plasma species oxidize and disintegrate capsid protein of feline calicivirus. |
title_full |
Cold argon-oxygen plasma species oxidize and disintegrate capsid protein of feline calicivirus. |
title_fullStr |
Cold argon-oxygen plasma species oxidize and disintegrate capsid protein of feline calicivirus. |
title_full_unstemmed |
Cold argon-oxygen plasma species oxidize and disintegrate capsid protein of feline calicivirus. |
title_sort |
cold argon-oxygen plasma species oxidize and disintegrate capsid protein of feline calicivirus. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2018-01-01 |
description |
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. |
url |
http://europepmc.org/articles/PMC5864060?pdf=render |
work_keys_str_mv |
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