The polyomavirus BK agnoprotein co-localizes with lipid droplets
- Transplantation Virology, Institute for Medical Microbiology, Department of Biomedicine, University of Basel, CH-4003 Basel (Switzerland)
- Bio-Optics Facility, Department of Biomedicine, University of Basel, Basel (Switzerland)
- Department of Microbiology and Infection Control, University Hospital of North Norway, Tromso (Norway)
Agnoprotein encoded by human polyomavirus BK (BKV) is a late cytoplasmic protein of 66 amino acids (aa) of unknown function. Immunofluorescence microscopy revealed a fine granular and a vesicular distribution in donut-like structures. Using BKV(Dunlop)-infected or agnoprotein-transfected cells, we investigated agnoprotein co-localization with subcellular structures. We found that agnoprotein co-localizes with lipid droplets (LD) in primary human renal tubular epithelial cells as well as in other cells supporting BKV replication in vitro (UTA, Vero cells). Using agnoprotein-enhanced green fluorescent protein (EGFP) fusion constructs, we demonstrate that agnoprotein aa 20-42 are required for targeting LD, whereas aa 1-20 or aa 42-66 were not. Agnoprotein aa 22-40 are predicted to form an amphipathic helix, and mutations A25D and F39E, disrupting its hydrophobic domain, prevented LD targeting. However, changing the phosphorylation site serine-11 to alanine or aspartic acid did not alter LD co-localization. Our findings provide new clues to unravel agnoprotein function.
- OSTI ID:
- 21357607
- Journal Information:
- Virology, Vol. 399, Issue 2; Other Information: DOI: 10.1016/j.virol.2010.01.011; PII: S0042-6822(10)00028-0; Copyright (c) 2010 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; ISSN 0042-6822
- Country of Publication:
- United States
- Language:
- English
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