共 35 条
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
相关论文