scholarly journals Identification and Characterization of a Poliovirus Capsid Mutant with Enhanced Thermal Stability

2018 ◽  
Vol 93 (6) ◽  
Author(s):  
Y Nguyen ◽  
Palmy R. Jesudhasan ◽  
Elizabeth R. Aguilera ◽  
Julie K. Pfeiffer

ABSTRACTEnteric viruses, including poliovirus, are spread by the fecal-oral route. In order to persist and transmit to a new host, enteric virus particles must remain stable once they are in the environment. Environmental stressors such as heat and disinfectants can inactivate virus particles and prevent viral transmission. It has been previously demonstrated that bacteria or bacterial surface glycans can enhance poliovirus virion stability and limit inactivation from heat or bleach. While investigating the mechanisms underlying bacterially enhanced virion thermal stability, we identified and characterized a poliovirus (PV) mutant with increased resistance to heat inactivation. The M132V mutant harbors a single amino acid change in the VP1 capsid coding that is sufficient to confer heat resistance but not bleach resistance. Although the M132V virus was stable in the absence of bacteria or feces at most temperatures, M132V virus was stabilized by feces at very high temperatures. M132V PV had reduced specific infectivity and RNA uncoating compared with those of wild-type (WT) PV, but viral yields in HeLa cells were similar. In orally inoculated mice, M132V had a slight fitness cost since fecal titers were lower and 12.5% of fecal viruses reverted to the WT. Overall, this work sheds light on factors that influence virion stability and fitness.IMPORTANCEViruses spread by the fecal-oral route need to maintain viability in the environment to ensure transmission. Previous work indicated that bacteria and bacterial surface polysaccharides can stabilize viral particles and enhance transmission. To explore factors that influence viral particle stability, we isolated a mutant poliovirus that is heat resistant. This mutant virus does not require feces for stability at most temperatures but can be stabilized by feces at very high temperatures. Even though the mutant virus is heat resistant, it is susceptible to inactivation by treatment with bleach. This work provides insight into how viral particles maintain infectivity in the environment.

2018 ◽  
Author(s):  
Y Nguyen ◽  
Palmy R. Jesudhasan ◽  
Elizabeth R. Aguilera ◽  
Julie K. Pfeiffer

ABSTRACTEnteric viruses, including poliovirus, are spread by the fecal-oral route. In order to persist and transmit to a new host, enteric virus particles must remain stable once they are in the environment. Environmental stressors such as heat and disinfectants can inactivate virus particles and prevent viral transmission. It has been previously demonstrated that bacteria or bacterial surface glycans can enhance poliovirus virion stability and limit inactivation from heat or bleach. While investigating the mechanisms underlying bacterial-enhanced virion thermal stability, we identified and characterized a poliovirus mutant with increased resistance to heat inactivation. This poliovirus mutant, M132V, harbors a single amino acid change in the VP1 capsid-coding that is sufficient to confer heat resistance. M132V was comparable to wild-type virus for replicationin vitro, as well as for replication and pathogenesis in orally-inoculated mice. Although the M132V virus was stable in the absence of bacteria or feces at most temperatures, M132V virus was stabilized by feces at very high temperatures. Additionally, the M132V virus does not have enhanced stability during bleach treatment, suggesting that thermal and bleach inactivation mechanisms are separable. Our results suggest that different mechanisms underlie virion stabilization by bacteria and the M132V mutation. Overall, this work sheds light on factors that influence virion stability.IMPORTANCEViruses spread by the fecal-oral route need to maintain viability in the environment to ensure transmission. Previous work indicated that bacteria and bacterial surface polysaccharides can stabilize viral particles and enhance transmission. To explore factors that influence viral particle stability, we isolated a mutant poliovirus that is heat resistant. This mutant virus does not require feces for stability at most temperatures, but can be stabilized by feces at very high temperatures. Even though the mutant virus is heat resistant, it is susceptible to inactivation by treatment with bleach. This work provides insight into how viral particles maintain infectivity in the environment.


Author(s):  
Debashis Mukherji ◽  
Joachim Rösler ◽  
Pavel Strunz ◽  
Ralph Gilles ◽  
Gerhard Schumacher ◽  
...  

1989 ◽  
Vol 21 (3) ◽  
pp. 199-204 ◽  
Author(s):  
G. J. Knight ◽  
W. W. Wright

1988 ◽  
Vol 28 (3) ◽  
pp. 315-321 ◽  
Author(s):  
J. T. Malmo ◽  
O. J. Jøkberg ◽  
G. A. Slettemoen
Keyword(s):  

During the researches upon high-pressure explosions of carbonic oxide-air, hydrogen-air, etc., mixtures, which have been described in the previous papers of this series, a mass of data has been accumulated relating to the influence of density and temperature upon the internal energy of gases and the dissociation of steam and carbon dioxide. Some time ago, at Prof. Bone’s request, the author undertook a systematic survey of the data in question, and the present paper summarises some of the principal results thereof, which it is hoped will throw light upon problems interesting alike to chemists, physicists and internal-combustion engineers. The explosion method affords the only means known at present of determining the internal energies of gases at very high temperatures, and it has been used for this purpose for upwards of 50 years. Although by no means without difficulties, arising from uncertainties of some of the assumptions upon which it is based, yet, for want of a better, its results have been generally accepted as being at least provisionally valuable. Amongst the more recent investigations which have attracted attention in this connection should be mentioned those of Pier, Bjerrum, Siegel and Fenning, all of whom worked at low or medium pressures.


2012 ◽  
Vol 58 (5) ◽  
pp. 589-595
Author(s):  
Guy Lemay ◽  
Martin Bisaillon

Many temperature-sensitive mutants have been isolated in early studies of mammalian reovirus. However, the biological properties and nature of the genetic alterations remain incompletely explored for most of these mutants. The mutation harbored by the tsI138 mutant was already assigned to the L3 gene encoding the λ1 protein. In the present study, this mutant was further studied as a possible tool to establish the role of the putative λ1 enzymatic activities in viral multiplication. It was observed that synthesis of viral proteins is only marginally reduced, while it was difficult to recover viral particles at the nonpermissive temperature. A single nucleotide substitution resulting in an amino acid change was found; the position of this amino acid is consistent with a probable defect in assembly of the inner capsid at the nonpermissive temperature.


2004 ◽  
Vol 26 (2) ◽  
pp. 84-86 ◽  
Author(s):  
Leo van Wüllen ◽  
Georg Schwering ◽  
Ernst Naumann ◽  
Martin Jansen
Keyword(s):  
Mas Nmr ◽  

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