Abstract

Parvovirus B19 (B19V) is a widespread human pathogen possessing a high tropism for erythroid precursor cells. However, the persistence or active replication of B19V in endothelial cells (EC) has been detected in diverse human pathologies. The VP1 unique region (VP1u) of the viral capsid has been reported to act as a major determinant of viral tropism for erythroid precursor cells. Nevertheless, the interaction of VP1u with EC has not been studied. We demonstrate that recombinant VP1u is efficiently internalized by rats’ pulmonary trunk blood vessel-derived EC in vitro compared to the human umbilical vein EC line. The exposure to VP1u was not acutely cytotoxic to either human- or rat-derived ECs, but led to the upregulation of cellular stress signaling-related pathways. Our data suggest that high levels of circulating B19V during acute infection can cause endothelial damage, even without active replication or direct internalization into the cells.

Highlights

  • DNA in endothelial cells (EC), the objective of our study was to elucidate the effect of B19V-VP1-unique region (VP1u) on EC

  • We chose two EC cultures isolated from rats and humans for our work

  • We showed that EC from rat pulmonary trunk blood vessels, but not human umbilical vein endothelial cells (HUVEC), can efficiently internalize recombinant B19V VP1u

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Summary

Introduction

Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. The Human parvovirus B19 (B19V) is a widespread human pathogen that belongs to Erythroparvovirus genus of the Parvoviridae family. B19V is a small non-enveloped DNA virus, of which the capsid is 20-28 nm in diameter and carries a 5.5 kilobase length genome encoded in a single-stranded DNA molecule [1]. The icosahedral B19V virion consists of two structural proteins—VP1 (83 kDa) and VP2 (58 kDa)—which differ only by the 227 amino acids at the N-terminal region of the VP1-protein, which is called the VP1-unique region (VP1u). Each capsid is composed of 60 capsomers: VP2 is the major capsid protein and constitutes approximately 95% of the total virus particle [2]

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