Characterization of the early steps of human parvovirus B19 infection

Quattrocchi, Silva; Ruprecht, Nico; Bönsch, Claudia; Bieli, Sven; Zürcher, Christoph; Boller, Klaus; Kempf, Christoph; Ros, Carlos (2012). Characterization of the early steps of human parvovirus B19 infection. Journal of virology, 86(17), pp. 9274-9284. Baltimore: American Society for Microbiology 10.1128/JVI.01004-12

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The early steps of human parvovirus B19 (B19V) infection were investigated in UT7/Epo cells. B19V and its receptor globoside (Gb4Cer) associate with lipid rafts, predominantly of the noncaveolar type. Pharmacological disruption of the lipid rafts inhibited infection when the drug was added prior to virus attachment but not after virus uptake. B19V is internalized by clathrin-dependent endocytosis and spreads rapidly throughout the endocytic pathway, reaching the lysosomal compartment within minutes, where a substantial proportion is degraded. B19V did not permeabilize the endocytic vesicles, indicating a mechanism of endosomal escape without apparent membrane damage. Bafilomycin A(1) (BafA1) and NH(4)Cl, which raise endosomal pH, blocked the infection by preventing endosomal escape, resulting in a massive accumulation of capsids in the lysosomes. In contrast, in the presence of chloroquine (CQ), the transfer of incoming viruses from late endosomes to lysosomes was prevented; the viral DNA was not degraded; and the infection was boosted. In contrast to the findings for untreated or BafA1-treated cells, the viral DNA was progressively associated with the nucleus in CQ-treated cells, reaching a plateau by 3 h postinternalization, a time coinciding with the initiation of viral transcription. At this time, more than half of the total intracellular viral DNA was associated with the nucleus; however, the capsids remained extranuclear. Our studies provide the first insight into the early steps of B19V infection and reveal mechanisms involved in virus uptake, endocytic trafficking, and nuclear penetration.

Item Type:

Journal Article (Original Article)

Division/Institute:

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

UniBE Contributor:

Quattrocchi, Silva; Ruprecht, Nico; Kempf, Christoph and Ros Bascunana, Carlos

Subjects:

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

ISSN:

0022-538X

Publisher:

American Society for Microbiology

Language:

English

Submitter:

Factscience Import

Date Deposited:

04 Oct 2013 14:38

Last Modified:

31 May 2021 15:32

Publisher DOI:

10.1128/JVI.01004-12

PubMed ID:

22718826

Web of Science ID:

000307627800032

BORIS DOI:

10.48350/15292

URI:

https://boris.unibe.ch/id/eprint/15292 (FactScience: 222601)

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