Next Article in Journal
SARS-CoV-2 Delta Variant (AY.3) in the Feces of a Domestic Cat
Next Article in Special Issue
Evaluation of Molecular Test for the Discrimination of “Naked” DNA from Infectious Parvovirus B19 Particles in Serum and Bone Marrow Samples
Previous Article in Journal
How RSV Proteins Join Forces to Overcome the Host Innate Immune Response
Previous Article in Special Issue
A Functional Minigenome of Parvovirus B19
Article

A Conserved Receptor-Binding Domain in the VP1u of Primate Erythroparvoviruses Determines the Marked Tropism for Erythroid Cells

1
Department of Chemistry, Biochemistry and Pharmaceutical Sciences, University of Bern, 3012 Bern, Switzerland
2
CSL Behring AG, 3000 Bern, Switzerland
*
Author to whom correspondence should be addressed.
Academic Editor: Giorgio Gallinella
Viruses 2022, 14(2), 420; https://doi.org/10.3390/v14020420
Received: 11 January 2022 / Revised: 6 February 2022 / Accepted: 15 February 2022 / Published: 17 February 2022
(This article belongs to the Special Issue Advances in Parvovirus Research 2022)
Parvovirus B19 (B19V) is a human pathogen with a marked tropism for erythroid progenitor cells (EPCs). The N-terminal of the VP1 unique region (VP1u) contains a receptor-binding domain (RBD), which mediates virus uptake through interaction with an as-yet-unknown receptor (VP1uR). Considering the central role of VP1uR in the virus tropism, we sought to investigate its expression profile in multiple cell types. To this end, we established a PP7 bacteriophage-VP1u bioconjugate, sharing the size and VP1u composition of native B19V capsids. The suitability of the PP7-VP1u construct as a specific and sensitive VP1uR expression marker was validated in competition assays with B19V and recombinant VP1u. VP1uR expression was exclusively detected in erythroid cells and cells reprogrammed towards the erythroid lineage. Sequence alignment and in silico protein structure prediction of the N-terminal of VP1u (N-VP1u) from B19V and other primate erythroparvoviruses (simian, rhesus, and pig-tailed) revealed a similar structure characterized by a fold of three or four α-helices. Functional studies with simian parvovirus confirmed the presence of a conserved RBD in the N-VP1u, mediating virus internalization into human erythroid cells. In summary, this study confirms the exclusive association of VP1uR expression with cells of the erythroid lineage. The presence of an analogous RBD in the VP1u from non-human primate erythroparvoviruses emphasizes their parallel evolutionary trait and zoonotic potential. View Full-Text
Keywords: parvovirus B19; B19V; VP1u; VP1uR; receptor; tropism; primate erythroparvovirus; simian erythroparvovirus; rhesus erythroparvovirus; pig-tailed erythroparvovirus parvovirus B19; B19V; VP1u; VP1uR; receptor; tropism; primate erythroparvovirus; simian erythroparvovirus; rhesus erythroparvovirus; pig-tailed erythroparvovirus
Show Figures

Figure 1

MDPI and ACS Style

Bircher, C.; Bieri, J.; Assaraf, R.; Leisi, R.; Ros, C. A Conserved Receptor-Binding Domain in the VP1u of Primate Erythroparvoviruses Determines the Marked Tropism for Erythroid Cells. Viruses 2022, 14, 420. https://doi.org/10.3390/v14020420

AMA Style

Bircher C, Bieri J, Assaraf R, Leisi R, Ros C. A Conserved Receptor-Binding Domain in the VP1u of Primate Erythroparvoviruses Determines the Marked Tropism for Erythroid Cells. Viruses. 2022; 14(2):420. https://doi.org/10.3390/v14020420

Chicago/Turabian Style

Bircher, Cornelia, Jan Bieri, Ruben Assaraf, Remo Leisi, and Carlos Ros. 2022. "A Conserved Receptor-Binding Domain in the VP1u of Primate Erythroparvoviruses Determines the Marked Tropism for Erythroid Cells" Viruses 14, no. 2: 420. https://doi.org/10.3390/v14020420

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop