Thermal inactivation of32P-poliovirus at 37�C and 50�C in the presence of NaCl with high molarity

Majer, M; Thomssen, R.

doi:10.1007/bf01262235

Cited by 11 publications

(5 citation statements)

References 9 publications

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“…Others have found that 1--2 ~ NaC1 enhances the inactivation of poliovirus at moderate temperatures, but the influence of pH on this effect was not investigated (24,39). A more rapid inactivation of enteroviruses occurred at pH 9 with Kolthoff's borax-phosphate buffer than with Sorensen's glycine I I buffer.…”

Section: Discussionmentioning

confidence: 99%

“…T e m p e r a t u r e is another factor t h a t influences the stability of extracellular viruses. No alteration to the protein coat has been detected t h a t could be associated with thermal inactivation of poliovirus at t e m p e r a t u r e s less t h a n 44 ° C (9,24). The t~NA of poliovirus was the less stable component at 20 ° and 44 ° C, and the protein coat was less stable at 44 ° to 60 ° C. I n a c t i v a t i o n of poliovirus within the higher t e m p e r a t u r e range has been thoroughly d e m o n s t r a t e d to be an effect on the protein coat (4, 5, 10, t5).…”

Section: Introductionmentioning

confidence: 99%

“…DIMMOCI~ (9) concluded t h a t thermal inactivation of poliovirus and rhinovirus occurred through damage to both the R N A and the protein coat and t h a t inactivation at a particular t e m p e r a t u r e takes place through whichever component is the less stable at t h a t temperature. Increasing concentrations of NaC1 (0--0.3 M) enhance inactivation of poliovirus a t p H 10 (3), and NaC1 (1--2 ~) enhances inactivation of poliovirus at p H 7 (24,39). The R N A seems to be the inactivation site of enteroviruses at lower temperatures, because the infectivity of the t~NA within the virus particle is lost at the same rate as the infectivity of the whole virus particle (9).…”

Section: Introductionmentioning

confidence: 99%

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Effect of acid pH, salts, and temperature on the infectivity and physical integrity of enteroviruses

Salo

Cliver

1976

Archives of Virology

103

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At 2 degrees and 30 degrees C, enteroviruses are more stable on the acid than on the alkaline side of neutrality. In the range from pH 3 to 9, temperature is so influential that the fastest inactivation rate at 2 degrees C is slower than the slowest inactivation rate at 30 degrees C. Specific ions or salts also affect the rate of inactivation of enteroviruses. NaCl and other chloride salts enhance the inactivation of poliovirus at pH 3. NaCl is considerably less effective against poliovirus in the range of pH 4.5 to 7.0 than at pH less than 4.5. Loss of RNA infectivity of the virus particle proceeds as rapidly as the loss of infectivity of the particle itself, except at pH 3 in the presence of MgCl2. Inactivation results in alterations to the physical integrity of enteroviruses. At pH 5 and 7, RNA hydrolysis of poliovirus particles occurs; and at pH3, 5,6, and 7 the nucleic acid becomes susceptible to ribonuclease. Only virus particles inactivated at pH 3 show a sensitivity to chymotrypsin. The hemagglutinins of echovirus type 7 are destroyed during inactivation at pH 3,4,5, and 6; but at pH 6 this alteration precedes the loss of infectivity. The pH of the suspension is a primary determinant of the mechanism of virus destruction and possibly of the loss of infectivity at these temperatures.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Effect of acid pH, salts, and temperature on the infectivity and physical integrity of enteroviruses

Salo

Cliver

1976

Archives of Virology

103

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“…Among them, trehalose can enhance protein–protein binding by modifying protein hydration properties [ 13 – 15 ]. Metal ions could strengthen the van der Waals attraction forces at the inter-pentameric interface by forming “transition metal ion” [ 16 – 18 ].…”

Section: Introductionmentioning

confidence: 99%

Formulation enhanced the stability of Foot-and-mouth virus and prolonged vaccine storage

Chang²,

Yang

et al. 2022

Virol J

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Foot-and-mouth disease (FMD) is a highly contagious viral disease that affects cloven-hoofed animals. Vaccination is the most effective measure to control FMD. However, FMDV particles are prone to dissociation, leading to insufficient potency of vaccine. Based on this characteristic, a combination of twenty percentage trehalose, 500 mM NaCl and 3 mM CuSO4·5H2O was developed to increase viral stability. Heating-resistance test showed that FMDV infectivity was maintained when formulated with formulation. Additionally, the half-life of FMDV inactivation was prolonged remarkably. Sequencing analysis demonstrated that viral genome could not be altered in serial passages. Vaccine stability was monitored for up to 1 year at 4 °C, with a higher level of 146S content remained. This study suggested that the formulation could protect FMDV against massive structural breakdown and extend the shelf life of vaccine. Our findings could provide strategy to develop more solutions for the stabilization of viral vaccine.

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“…Besides changes to the capsid composition, the thermostability of enteroviruses can be affected by the composition of the suspending matrix. Most importantly, it has long been recognized that the thermostability of enteroviruses is enhanced in the presence of dissolved salts and that the enhancement depends on the salt concentration and identity (23)(24)(25). The mechanism by which salts achieve this thermostabilizing effect, however, remains unclear.…”

mentioning

confidence: 99%

Salt Enhances the Thermostability of Enteroviruses by Stabilizing Capsid Protein Interfaces

Meister

Prunotto

Peraro

et al. 2020

J Virol

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Enteroviruses are common agents of infectious disease that are spread by the fecal-oral route. They are readily inactivated by mild heat, which causes the viral capsid to disintegrate or undergo conformational change. While beneficial for the thermal treatment of food or water, this heat sensitivity poses challenges for the stability of enterovirus vaccines. The thermostability of an enterovirus can be modulated by the composition of the suspending matrix, though the effects of the matrix on virus stability are not understood. Here, we determined the thermostability of four enterovirus strains in solutions with various concentrations of NaCl and different pH values. The experimental findings were combined with molecular modeling of the protein interaction forces at the pentamer and the protomer interfaces of the viral capsids. While pH only had a modest effect on thermostability, increasing NaCl concentrations raised the breakpoint temperatures of all viruses tested by up to 20°C. This breakpoint shift could be explained by an enhancement of the van der Waals attraction forces at the two protein interfaces. In comparison, the (net repulsive) electrostatic interactions were less affected by NaCl. Depending on the interface considered, the breakpoint temperature shifted by 7.5 or 5.6°C per 100-kcal/(mol·Å) increase in protein interaction force. IMPORTANCE The genus Enterovirus encompasses important contaminants of water and food (e.g., coxsackieviruses), as well as viruses of acute public health concern (e.g., poliovirus). Depending on the properties of the surrounding matrix, enteroviruses exhibit different sensitivities to heat, which in turn influences their persistence in the environment, during food treatment, and during vaccine storage. Here, we determined the effect of NaCl and pH on the heat stability of different enteroviruses and related the observed effects to changes in protein interaction forces in the viral capsid. We demonstrate that NaCl renders enteroviruses thermotolerant and that this effect stems from an increase in van der Waals forces at different protein subunits in the viral capsid. This work sheds light on the mechanism by which salt enhances virus stability.

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Thermal inactivation of32P-poliovirus at 37�C and 50�C in the presence of NaCl with high molarity

Cited by 11 publications

References 9 publications

Effect of acid pH, salts, and temperature on the infectivity and physical integrity of enteroviruses

Effect of acid pH, salts, and temperature on the infectivity and physical integrity of enteroviruses

Formulation enhanced the stability of Foot-and-mouth virus and prolonged vaccine storage

Salt Enhances the Thermostability of Enteroviruses by Stabilizing Capsid Protein Interfaces

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