Molecular basis of the behavior of hepatitis a virus exposed to high hydrostatic pressure.

Abstract:

:Food-borne hepatitis A outbreaks may be prevented by subjecting foods at risk of virus contamination to moderate treatments of high hydrostatic pressure (HHP). A pretreatment promoting hepatitis A virus (HAV) capsid-folding changes enhances the virucidal effect of HHP, indicating that its efficacy depends on capsid conformation. HAV populations enriched in immature capsids (125S provirions) are more resistant to HHP, suggesting that mature capsids (150S virions) are more susceptible to this treatment. In addition, the monoclonal antibody (MAb) K24F2 epitope contained in the immunodominant site is a key factor for the resistance to HHP. Changes in capsid folding inducing a loss of recognition by MAb K24F2 render more susceptible conformations independently of the origin of such changes. Accordingly, codon usage-associated folding changes and changes stimulated by pH-dependent breathings, provided they confer a loss of recognition by MAb K24F2, induce a higher susceptibility to HHP. In conclusion, the resistance of HAV to HHP treatments may be explained by a low proportion of 150S particles combined with a good accessibility of the epitope contained in the immunodominant site close to the 5-fold axis.

journal_name

Appl Environ Microbiol

authors

D'Andrea L,Pérez-Rodríguez FJ,Costafreda MI,Beguiristain N,Fuentes C,Aymerich T,Guix S,Bosch A,Pintó RM

doi

10.1128/AEM.01693-14

subject

Has Abstract

pub_date

2014-10-01 00:00:00

pages

6499-505

issue

20

eissn

0099-2240

issn

1098-5336

pii

AEM.01693-14

journal_volume

80

pub_type

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