PMID:29566061

Citation	Aboubakr, HA, Mor, SK, Higgins, L, Armien, A, Youssef, MM, Bruggeman, PJ and Goyal, SM (2018) Cold argon-oxygen plasma species oxidize and disintegrate capsid protein of feline calicivirus. PLoS ONE 13:e0194618
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.
Links	PubMed PMC5864060 Online version:10.1371/journal.pone.0194618
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
9CALI:Q2NNN5		GO:0019028: viral capsid	ECO:0000314:		C		The Mass Spectroscopy results in Figure 6 and the accompanying table 3 show evidence of 9CALI:Q2NNN5 as a viral capsid protein. When the FCV was exposed to CAP the mass spec analysis resulted in several unique peaks for the capsid protien (Met+16). This was identified to be an oxygenation of several of the methionine groups. When this is taken with the evidence of CAP disintegrating capsid proteins shown by RT-PCR in figure 4 it indicates that 9CALI:Q2NNN5 protein is the capsid protein.	complete CACAO 13172

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