Journal
JOURNAL OF VIROLOGICAL METHODS
Volume 179, Issue 1, Pages 1-7Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jviromet.2011.05.009
Keywords
Virus-like particle; VLP; Norovirus; P domain protein; Diagnostics
Funding
- Academy of Finland [1115976]
- Pirkanmaa Hospital District
- National Graduate School in Informational and Structural Biology (ISB), Finland
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Noroviruses are an important cause of epidemic acute gastroenteritis in humans. In this study the production and characterization of GII.4 norovirus virus-like particles (VLPs) in insect cells is reported. Furthermore, the expression of corresponding norovirus polyhistidine-tagged P domain protein in Escherichia coli is described. The protruding P domain of the norovirus capsid is known to contain determinants for antibody and receptor binding. Therefore, P domain proteins were studied as an alternative diagnostic tool for evaluating norovirus infection. Analyses by dynamic light scattering and cryo-electron microscopy revealed the presence of intact VLPs with an average diameter of about 40 nm. Immunostaining and ELISA assays using norovirus-specific human sera revealed that VLPs and the P domain are recognized by norovirus-specific antibodies and by their putative receptor. The VLPs and P domain protein are potentially useful in the development of diagnostic and vaccination tools for noroviruses. (C) 2011 Elsevier B.V. All rights reserved.
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