Stability of Hepatitis A Virus

Siegl, G.; Weitz, Manfred; Kronauer, G.

doi:10.1159/000149554

Cited by 153 publications

(73 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The effective inactivating temperature is approximately at 60°C (36) since the D value dropped dramatically at 60°C. This result agreed with previous studies, indicating that hepatitis A virus and PV were heat resistant up to 60°C (39,43).…”

Section: Discussionsupporting

confidence: 93%

Thermal Inactivation of Foot-and-Mouth Disease Viruses in Suspension

Kamolsiripichaiporn

Subharat

Udon

et al. 2007

Appl Environ Microbiol

View full text Add to dashboard Cite

The heat resistance of foot-and-mouth disease virus (FMDV) strains isolated from outbreaks inFoot-and-mouth disease virus (FMDV) is classified within the genus Aphthovirus, family Picornaviridae. FMDV is a nonenveloped, icosahedral symmetric, and single-stranded RNA virus; therefore, it is somewhat resistant to harsh environments, e.g., UV radiation, low water activities, and heat (3). FMDV causes foot-and-mouth disease (FMD) and is highly contagious to cloven-hoofed animals. The common mode of transmission of FMDV is direct contact; however, oral-route transmission via indirect contact has frequently caused epidemics in pigs (2). FMD is the first disease on the OIE List A and also was the first disease for which the OIE established an official list of free countries and zones. FMD has a great potential for causing severe economic loss for many countries (2). In order to export meat from an FMD-infected country to an FMD-free country, meat is subjected to heat treatment to reach an internal core temperature of at least 70°C for a minimum of 30 min or to any equivalent treatment which has been demonstrated to inactivate the FMD virus (38).The efficiency of thermal inactivation is a function of time and temperature. Thermal destruction hypothetically follows first order kinetics. The decimal reduction time (D value, DRT, or D T ) is the time at a specified temperature required to reduce the number of microorganisms by a factor of 10 (23, 24, 44, 45). The D value is the negative reciprocal of the slope of the inactivation curve, where the inactivation of microorganisms is a logarithmic function of time. The z value is defined as the temperature change required to reduce D value by a factor of 10 (23, 24, 44, 45). Likewise, the z value can be calculated by the negative reciprocal of the slope of the decimal reduction curve where D values of different temperatures are plotted on a semilogarithmic scale against temperatures. The z value is specific for a given strain of microorganism in a given medium or product, but the z value does not differ across media as widely as does the D value. This association of D value and temperature in a DRT curve is helpful to calculate the D value of temperatures that were not included in the experiment. Many studies have demonstrated the heat resistance of FMDV (10, 12, 14-16, 30-32, 34). However, these studies involved only a few temperatures, different media, and strains that were not epidemic in Thailand. Therefore, these data are not appropriate bases for bilateral trade negotiations involving Thai animal products. The objective of the present study was to determine the heat resistance of FMDV strains isolated from outbreaks in Thailand, in terms of D value and z value in phosphate-buffered saline (PBS) at 50, 60, 70, 80, 90, and 100°C. MATERIALS AND METHODSVirus and cell culture. FMDV serotypes O (strains O189 and OPN), A (strains A118, A-Sakol, and A132), and Asia 1 (strain AS1) were obtained from the Regional Reference Laboratory for FMD in Southeast Asia, Pakchong, Thailand....

show abstract

Section: Discussionsupporting

confidence: 93%

Thermal Inactivation of Foot-and-Mouth Disease Viruses in Suspension

Kamolsiripichaiporn

Subharat

Udon

et al. 2007

Appl Environ Microbiol

View full text Add to dashboard Cite

show abstract

“…These modifications were also observed in the physical properties of the capsids, and during the adaptation to increasing levels of cellular shutoff, there was a general tendency toward the loss of the otherwise highly stable phenotype of HAV at high temperature, at low pH, and in the presence of biliary salts. The phenotype of the population long adapted to a high level of cellular shutoff was more similar to that of other picornaviruses than to that of the parental HAV (54)(55)(56). However, as predicted by the quasispecies theory (57), each population evolved in a particular manner in each specific environment as evidenced during the processes of readaptation to the original conditions.…”

Section: Discussionmentioning

confidence: 87%

Hepatitis A Virus Adaptation to Cellular Shutoff Is Driven by Dynamic Adjustments of Codon Usage and Results in the Selection of Populations with Altered Capsids

Costafreda

Pérez-Rodríguez

D’Andrea

et al. 2014

J Virol

View full text Add to dashboard Cite

Hepatitis A virus (HAV) has a highly biased and deoptimized codon usage compared to the host cell and fails to inhibit host protein synthesis. It has been proposed that an optimal combination of abundant and rare codons controls the translation speed required for the correct capsid folding. The artificial shutoff host protein synthesis results in the selection of variants containing mutations in the HAV capsid coding region critical for folding, stability, and function. Here, we show that these capsid mutations resulted in changes in their antigenicity; in a reduced stability to high temperature, low pH, and biliary salts; and in an increased efficacy of cell entry. In conclusion, the adaptation to cellular shutoff resulted in the selection of large-plaque-producing virus populations. IMPORTANCEHAV has a naturally deoptimized codon usage with respect to that of its cell host and is unable to shut down the cellular translation. This fact contributes to the low replication rate of the virus, in addition to other factors such as the highly inefficient internal ribosome entry site (IRES), and explains the outstanding physical stability of this pathogen in the environment mediated by a folding-dependent highly cohesive capsid. Adaptation to artificially induced cellular transcription shutoff resulted in a redeoptimization of its capsid codon usage, instead of an optimization. These genomic changes are related to an overall change of capsid folding, which in turn induces changes in the cell entry process. Remarkably, the adaptation to cellular shutoff allowed the virus to significantly increase its RNA uncoating efficiency, resulting in the selection of large-plaque-producing populations. However, these populations produced much-debilitated virions.

show abstract

“…The largest capsid protein, VP1, also contains a unique C-terminal extension that appears to function in pentamer assembly (3). Congruent with this evidence for a unique assembly pathway for the viral particle, the thermal stability of the HAV virion far exceeds that of other picornaviruses (7,20). HAV also lacks a 2A proteinase, and unlike other picornaviruses, the primary proteolytic cleavage of the viral polyprotein at the 2A/2B junction is mediated by the only proteinase expressed by the virus, 3C pro (18).…”

mentioning

confidence: 99%

Identification of a Conserved RNA Replication Element ( cre ) within the 3D ^pol -Coding Sequence of Hepatoviruses

Yang

Evans

et al. 2008

J Virol

View full text Add to dashboard Cite

Internally located, cis-acting RNA replication elements (cre) have been identified within the genomes of viruses representing each of the major picornavirus genera (Enterovirus, Rhinovirus, Aphthovirus, and Cardiovirus) except Hepatovirus. Previous efforts to identify a stem-loop structure with cre function in hepatitis A virus (HAV), the type species of this genus, by phylogenetic analyses or thermodynamic predictions have not succeeded. However, a region of markedly suppressed synonymous codon variability was identified in alignments of HAV sequences near the 5 end of the 3D pol -coding sequence of HAV, consistent with noncoding constraints imposed by an underlying RNA secondary structure. Subsequent MFOLD predictions identified a 110-nucleotide (nt) complex stem-loop in this region with a typical AAACA/G cre motif in its top loop. A potentially homologous RNA structure was identified in this region of the avian encephalitis virus genome, despite little nucleotide sequence relatedness between it and HAV. Mutations that disrupted secondary RNA structure or the AAACA/G motif, without altering the amino acid sequence of 3D pol , ablated replication of a subgenomic HAV replicon in transfected human hepatoma cells. Replication competence could be rescued by reinsertion of the native 110-nt stem-loop structure (but not an abbreviated 45-nt stem-loop) upstream of the HAV coding sequence in the replicon. These results suggest that this stem-loop is functionally similar to cre elements of other picornaviruses and likely involved in templating VPg uridylylation as in other picornaviruses, despite its significantly larger size and lower free folding energy.Hepatitis A virus (HAV), a member of the family Picornaviridae, is a common etiological agent of acute hepatitis in humans. Several characteristics of HAV distinguish it from other picornaviruses, justifying its classification within a separate genus in this family, the genus Hepatovirus (10). First, the primary sequence of the positive-sense, single-stranded RNA genome of HAV shares little homology with that of other picornaviruses. Avian encephalitis virus (AEV) is the only exception to this statement, as it bears considerable sequence relatedness to HAV and has been tentatively classified as the second member of this genus. Details of the organization and function of the HAV polyprotein also differ in several respects from the typical LP1P2P3 organization found in other picornaviruses (10). The amino-terminal capsid protein, VP4, is remarkably small, lacks an N-terminal consensus myristoylation signal, and appears to have an alternative function in viral assembly compared to the VP4 proteins of other picornaviruses (24). The largest capsid protein, VP1, also contains a unique C-terminal extension that appears to function in pentamer assembly (3). Congruent with this evidence for a unique assembly pathway for the viral particle, the thermal stability of the HAV virion far exceeds that of other picornaviruses (7,20). HAV also lacks a 2A proteinase, and unlike other pi...

show abstract

Stability of Hepatitis A Virus

Cited by 153 publications

References 13 publications

Thermal Inactivation of Foot-and-Mouth Disease Viruses in Suspension

Thermal Inactivation of Foot-and-Mouth Disease Viruses in Suspension

Hepatitis A Virus Adaptation to Cellular Shutoff Is Driven by Dynamic Adjustments of Codon Usage and Results in the Selection of Populations with Altered Capsids

Identification of a Conserved RNA Replication Element ( cre ) within the 3D ^pol -Coding Sequence of Hepatoviruses

Contact Info

Product

Resources

About

Stability of Hepatitis A Virus

Cited by 153 publications

References 13 publications

Thermal Inactivation of Foot-and-Mouth Disease Viruses in Suspension

Thermal Inactivation of Foot-and-Mouth Disease Viruses in Suspension

Hepatitis A Virus Adaptation to Cellular Shutoff Is Driven by Dynamic Adjustments of Codon Usage and Results in the Selection of Populations with Altered Capsids

Identification of a Conserved RNA Replication Element ( cre ) within the 3D pol -Coding Sequence of Hepatoviruses

Contact Info

Product

Resources

About

Identification of a Conserved RNA Replication Element ( cre ) within the 3D ^pol -Coding Sequence of Hepatoviruses