期刊
MICROBES AND INFECTION
卷 11, 期 13, 页码 1019-1028出版社
ELSEVIER
DOI: 10.1016/j.micinf.2009.07.009
关键词
West Nile virus; prM; VLP
资金
- Ministry of Education. Science, Technology, Sports, and Culture of Japan
- Ministry of Health, Labor, and Welfare
- Japanese Health Sciences Foundation
Expression of genes for precursor M (prM) and envelope (E) proteins of West Nile virus (WNV) leads to the production of small. capsidless, and non-infectious virus-like particles (VLPs) possessing the E antigen which is responsible for viral entry and immune protection It has been reported that processing of the secretion signal affects viral release We examined the secretion efficiency of VLPs into the culture medium front RK13 or 293 T cells transfected with expression vectors for prM and E proteins of WNV which were constructed to comprise different lengths of signal peptides upstream of the prM-E domain The number of amino acid residues present in the segment markedly affected the production, processing, and secretion of VLPs Secreted VLPs possessed both the processed M protein and the glycosylated E protein In addition, immunization with VLPs induced neutralizing, antibodies in C3H/HeN mice. These results indicate that the number of amino acid residues comprising the N-terminus of the signal segment controls the efficiency of assembly, maturation, and release of VLPs; in the absence of viral protease, which in turn indicates the potential of VLPs as a candidate for an effective WNV subunit vaccine. (C) 2009 Elsevier Masson SAS. All rights reserved
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