Kaufmann, Baerbel and Baxa, U. and Chipman, P. R. and Rossmann, M. G. and Modrow, Susanne and Seckler, Robert (2005) Parvovirus B19 does not bind to membrane-associated globoside in vitro. VIROLOGY, 332 (1). pp. 189-198. ISSN 0042-6822,
Full text not available from this repository. (Request a copy)Abstract
The glycosphingolipid globoside (globotetraosylceramide, Gb4Cer) has been proposed to be the cellular receptor of human parvovirus B19. Quantitative measurements of the binding of parvovirus B19 to Gb4Cer were performed to explore the molecular basis of the virus tropism. Solid-phase assays with fluorescence-labeled liposomes or (125)iodine-labeled empty capsids were used to characterize the specificity of binding. In addition, surface plasmon resonance on lipid layers, as well as isothermal titration microcalorimetry, was utilized for real-time analysis of the virus-receptor interaction. These studies did not confirm binding of Gb4Cer to recombinant B19 VP2 capsids, suggesting that Gb4Cer does not function on its own as the cellular receptor of human parvovirus B19, but might be involved in a more complex recognition event. The biochemical results were further confirmed by cryo-electron microscopy image reconstructions at 10 A resolution, in which the structures of empty capsids were compared with empty capsids incubated with Gb4Cer. (C) 2004 Elsevier Inc. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | SURFACE-PLASMON RESONANCE; ERYTHROCYTE-P-ANTIGEN; MARROW CELL-CULTURES; B19 PARVOVIRUS; CANINE PARVOVIRUS; KINETIC-ANALYSIS; VIRUS RECEPTORS; SENSOR CHIP; FETAL LIVER; INFECTION; Parvoviridae; parvovirus B19; globoside; receptor binding; hemagglutination; SPR; electron microscopy; ITC; liposomes |
| Subjects: | 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Lehrstuhl für Medizinische Mikrobiologie und Hygiene |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 28 May 2021 09:52 |
| Last Modified: | 28 May 2021 09:52 |
| URI: | https://pred.uni-regensburg.de/id/eprint/36489 |
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