Parvovirus B19 uptake is a highly selective process controlled by VP1u, a novel determinant of viral tropism

Leisi, Remo; Ruprecht, Nico; Kempf, Christoph; Ros, Carlos (2013). Parvovirus B19 uptake is a highly selective process controlled by VP1u, a novel determinant of viral tropism. Journal of virology, 87(24), pp. 13161-13167. American Society for Microbiology 10.1128/JVI.02548-13

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The VP1 unique region (VP1u) of human parvovirus B19 (B19V) is the immunodominant part of the viral capsid. Originally inaccessible, the VP1u becomes exposed upon primary attachment to the globoside receptor. To study the function of the exposed VP1u in B19V uptake, we expressed this region as a recombinant protein. Here, we report that purified recombinant VP1u binds and is internalized in UT7/Epo cells. By means of truncations and specific antibodies, we identified the most N-terminal amino acid residues of VP1u as the essential region for binding and internalization. Furthermore, the recombinant VP1u was able to block B19V uptake, suggesting that the protein and the virus undertake the same internalization pathway. Assays with different erythroid and nonerythroid cell lines showed that the N-terminal VP1u binding was restricted to a few cell lines of the erythroid lineage, which were also the only cells that allowed B19V internalization and infection. These results together indicate that the N-terminal region of VP1u is responsible for the internalization of the virus and that the interacting receptor is restricted to B19V-susceptible cells. The highly selective uptake mechanism represents a novel determinant of the tropism and pathogenesis of B19V.

Item Type:

Journal Article (Original Article)

Division/Institute:

08 Faculty of Science > Department of Chemistry, Biochemistry and Pharmaceutical Sciences (DCBP)

UniBE Contributor:

Leisi, Remo; Ruprecht, Nico; Kempf, Christoph and Ros Bascunana, Carlos

Subjects:

500 Science > 570 Life sciences; biology
500 Science > 540 Chemistry
500 Science

ISSN:

0022-538X

Publisher:

American Society for Microbiology

Language:

English

Submitter:

Christoph Kempf

Date Deposited:

20 Aug 2014 13:35

Last Modified:

31 May 2021 15:36

Publisher DOI:

10.1128/JVI.02548-13

PubMed ID:

24067971

BORIS DOI:

10.7892/boris.58020

URI:

https://boris.unibe.ch/id/eprint/58020

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