The polyomavirus BK agnoprotein co-localizes with lipid droplets

• Published in: Virology (New York, N.Y.) Vol. 399; no. 2; pp. 322 - 331
• Main Authors: Unterstab, Gunhild, Gosert, Rainer, Leuenberger, David, Lorentz, Pascal, Rinaldo, Christine H, Hirsch, Hans H
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 10.04.2010
• Subjects: 60 APPLIED LIFE SCIENCES; Accessory protein; Agnoprotein; ALANINES; Amino Acid Sequence; AMINO ACIDS; Animals; ASPARTIC ACID; BK virus; BK Virus - chemistry; BODY; CARBOXYLIC ACIDS; Cell Nucleus - chemistry; Cells, Cultured; Cercopithecus aethiops; CHEMICAL REACTIONS; CLSM; Cytoplasm - chemistry; Deconvolution; DROPLETS; Humans; HYDROXY ACIDS; Infection; Infectious Disease; KIDNEYS; Lipid droplets; LIPIDS; Lipids - chemistry; MICROORGANISMS; Microscopy, Confocal; Microscopy, Fluorescence; Molecular Sequence Data; Mutation; MUTATIONS; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANS; PARASITES; PARTICLES; PHOSPHORYLATION; Polyomavirus; Protein Structure, Secondary; PROTEINS; SERINE; Transfection; Vero Cells; Viral Regulatory and Accessory Proteins - chemistry; VIRUSES; Agnoprotein; Infection; Deconvolution; Transfection; Lipid droplets; Polyomavirus; BK virus; Accessory protein; CLSM

Abstract 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 ce...