Boensch, Claudia; Kempf, Christoph; Ros, Carlos (2008). Interaction of parvovirus B19 with human erythrocytes alters virus structure and cell membrane integrity. Journal of virology, 82(23), pp. 11784-11791. Baltimore: American Society for Microbiology 10.1128/JVI.01399-08
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The unique region of the capsid protein VP1 (VP1u) of B19 virus (B19V) elicits a dominant immune response and has a phospholipase A(2) (PLA(2)) activity required for the infection. Despite these properties, we have observed that the VP1u-PLA(2) motif occupies an internal position in the capsid. However, brief exposure to increasing temperatures induced a progressive accessibility of the PLA(2) motif as well as a proportional increase of the PLA(2) activity. Similarly, upon binding on human red blood cells (RBCs), a proportion of the capsids externalized the VP1u-PLA(2) motif. Incubation of B19V with RBCs from 17 healthy donors resulted in extensive virus attachment ranging between 3,000 and 30,000 virions per cell. B19V empty capsids represent an important fraction of the viral particles circulating in the blood (30 to 40%) and bind to RBCs in the same way as full capsids. The extensive B19V binding to RBCs did not cause direct hemolysis but an increased osmotic fragility of the cells by a mechanism involving the PLA(2) activity of the exposed VP1u. Analysis of a blood sample from an individual with a recent B19V infection revealed that, at this particular moment of the infection, the virions circulating in the blood were mostly associated to the RBC fraction. However, the RBC-bound B19V was not able to infect susceptible cells. These observations indicate that RBCs play a significant role during B19V infection by triggering the exposure of the immunodominant VP1u including its PLA(2) constituent. On the other hand, the early exposure of VP1u might facilitate viral internalization and/or uncoating in target cells.
Item Type: |
Journal Article (Original Article) |
|---|---|
Division/Institute: |
08 Faculty of Science > Department of Chemistry, Biochemistry and Pharmaceutical Sciences (DCBP) |
UniBE Contributor: |
Bönsch, Claudia, Kempf, Christoph (B), 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 15:10 |
Last Modified: |
29 Mar 2023 23:33 |
Publisher DOI: |
10.1128/JVI.01399-08 |
PubMed ID: |
18815302 |
Web of Science ID: |
000260789700030 |
BORIS DOI: |
10.48350/31000 |
URI: |
https://boris.unibe.ch/id/eprint/31000 (FactScience: 195380) |
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