期刊
JOURNAL OF VIROLOGICAL METHODS
卷 179, 期 1, 页码 1-7出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jviromet.2011.05.009
关键词
Virus-like particle; VLP; Norovirus; P domain protein; Diagnostics
资金
- Academy of Finland [1115976]
- Pirkanmaa Hospital District
- National Graduate School in Informational and Structural Biology (ISB), Finland
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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