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

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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.

Original languageEnglish (US)
Article numbere0194618
JournalPLoS One
Volume13
Issue number3
DOIs
StatePublished - Mar 2018

Bibliographical note

Funding Information:
Partial funding was provided by the Agriculture and Food Research Initiative of the USDA’s National Institute of Food and Agriculture, grant number # 2017-67017-26172. Partial funding was provided National Science Foundation for Major Research Instrumentation grants 9871237 and NSF-DBI-0215759. Partial funding was provided by the Cultural Affairs and Mission Sector, Ministry of Higher Education and Scientific Research, Egypt, and partial funding was provided by University of Minnesota.

PubMed: MeSH publication types

  • Journal Article
  • Research Support, Non-U.S. Gov't

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