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Cellular localization and effects of ectopically expressed hepatitis A virus proteins 2B, 2C, 3A and their intermediates 2BC, 3AB and 3ABC

Authors
  • Seggewiß, Nicole1
  • Kruse, Hedi Verena1
  • Weilandt, Rebecca1
  • Domsgen, Erna1, 2
  • Dotzauer, Andreas1
  • Paulmann, Dajana1
  • 1 University of Bremen, Laboratory of Virus Research, Leobener Straße/UFT, Bremen, 28359, Germany , Bremen (Germany)
  • 2 Karolinska University Hospital Huddinge, Department of Medicine Huddinge, Karolinska Institutet, Center for Infectious Medicine (CIM), F59, Stockholm, 141 86, Sweden , Stockholm (Sweden)
Type
Published Article
Journal
Archives of Virology
Publisher
Springer-Verlag
Publication Date
Dec 28, 2015
Volume
161
Issue
4
Pages
851–865
Identifiers
DOI: 10.1007/s00705-015-2723-5
Source
Springer Nature
Keywords
License
Yellow

Abstract

In the course of hepatitis A virus (HAV) infections, the seven nonstructural proteins and their intermediates are barely detectable. Therefore, little is known about their functions and mechanisms of action. Ectopic expression of the presumably membrane-associated proteins 2B, 2C, 3A and their intermediates 2BC, 3AB and 3ABC allowed the intracellular localization of these proteins and their possible function during the replication cycle of HAV to be investigated. In this study, we used rhesus monkey kidney cells, which are commonly used for cell culture experiments, and human liver cells, which are the natural target cells. We detected specific associations of these proteins with distinct membrane compartments and the cytoskeleton, different morphological alterations of the respective structures, and specific effects on cellular functions. Besides comparable findings in both cell lines used with regard to localization and effects of the proteins examined, we also found distinct differences. The data obtained identify so far undocumented interactions with and effects of the HAV proteins investigated on cellular components, which may reflect unknown aspects of the interaction of HAV with the host cell, for example the modification of the ERGIC (ER-Golgi intermediate compartment) structure, an interaction with lipid droplets and lysosomes, and inhibition of the classical secretory pathway.

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