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

Kempf, Christoph; Leisi, Remo; Ros, Carlos; Ruprecht, Nico (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 > Departement of Chemistry and Biochemistry

UniBE Contributor:

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

Subjects:

500 Science
500 Science > 570 Life sciences; biology

ISSN:

0022-538X

Publisher:

American Society for Microbiology

Language:

English

Submitter:

Christoph Kempf

Date Deposited:

20 Aug 2014 13:35

Last Modified:

02 Sep 2015 10:57

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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