Production and characterization of virus-like particles and the P domain protein of GII.4 norovirus

被引:36
作者
Koho, Tiia [1 ,2 ]
Huhti, Leena [3 ]
Blazevic, Vesna [3 ]
Nurminen, Kirsi [3 ]
Butcher, Sarah J. [4 ]
Laurinmaki, Pasi [4 ]
Kalkkinen, Nisse [4 ]
Ronnholm, Gunilla [4 ]
Vesikari, Timo [3 ]
Hytonen, Vesa P. [1 ,2 ]
Kulomaa, Markku S. [1 ,2 ]
机构
[1] Univ Tampere, Inst Biomed Technol & BioMediTech, FI-33014 Tampere, Finland
[2] Univ Tampere, Tampere Univ Hosp, FI-33014 Tampere, Finland
[3] Univ Tampere, Vaccine Res Ctr, FI-33014 Tampere, Finland
[4] Univ Helsinki, Inst Biotechnol, FI-00014 Helsinki, Finland
基金
芬兰科学院;
关键词
Virus-like particle; VLP; Norovirus; P domain protein; Diagnostics; GROUP ANTIGEN RECEPTORS; BLOOD GROUP ANTIGENS; NORWALK VIRUS; CAPSID PROTEIN; GASTROENTERITIS; FORMS; CLASSIFICATION; RECOGNITION; EXPRESSION; STABILITY;
D O I
10.1016/j.jviromet.2011.05.009
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:1 / 7
页数:7
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