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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. | LitMetric

AI Article Synopsis

  • Hepatitis A virus (HAV) infections make it hard to study seven nonstructural proteins, as they are not easily detectable, leading to a gap in understanding their roles.
  • Researchers expressed certain HAV proteins in monkey kidney and human liver cells to examine their function and location during the virus replication process.
  • The study revealed specific interactions between these proteins and various cellular structures, showing both common and unique effects in different cell types, which could provide insights into how HAV alters host cell functions and its overall pathogenesis.

Article 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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Source
http://dx.doi.org/10.1007/s00705-015-2723-5DOI Listing

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