Assembly of double-shelled, virus-like particles in transgenic rice plants expressing two major structural proteins of rice dwarf virus

被引:30
作者
Zheng, HH
Yu, L
Wei, CH
Hu, DW
Shen, WP
Chen, ZL
Li, Y [1 ]
机构
[1] Peking Univ, Coll Life Sci, Beijing 100871, Peoples R China
[2] Zhejiang Univ, Inst Biotechnol, Hangzhou 310029, Peoples R China
关键词
D O I
10.1128/JVI.74.20.9808-9810.2000
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Rice dwarf virus (RDV) is a double-shelled particle that contains a major capsid protein (P8), a major core protein (P3), several minor core proteins, and viral genomic double-stranded RNA. Coexpression of P8 and P3 in transgenic rice plants resulted in formation of double-shelled, virus-like particles (VLPs) similar to the authentic RDV particles. The VLPs were not detected in transgenic rice plant cells expressing P8 alone. This in vivo result suggests that P8 interacted with P3 and that these two proteins provide the structural integrity required for the formation of VLPs in rice cells independently of other structural proteins, nonstructural proteins, or viral genomic double-stranded RNAs.
引用
收藏
页码:9808 / 9810
页数:3
相关论文
共 22 条
[1]   Virus-like particles assemble in plants and bacteria expressing the coat protein gene of Indian peanut clump virus [J].
Bragard, C ;
Duncan, GH ;
Wesley, SV ;
Naidu, RA ;
Mayo, MA .
JOURNAL OF GENERAL VIROLOGY, 2000, 81 :267-272
[2]  
Chang GJ, 1999, TAIWAN J MATH, V3, P73
[3]   Invasion of minor veins of tobacco leaves inoculated with tobacco mosaic virus mutants defective in phloem-dependent movement [J].
Ding, XS ;
Shintaku, MH ;
Carter, SA ;
Nelson, RS .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (20) :11155-11160
[4]   EXPRESSION OF TOBACCO MOSAIC-VIRUS COAT PROTEIN AND ASSEMBLY OF PSEUDOVIRUS PARTICLES IN ESCHERICHIA-COLI [J].
HWANG, DJ ;
ROBERTS, IM ;
WILSON, TMA .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1994, 91 (19) :9067-9071
[5]   Structure of double-shelled rice dwarf virus [J].
Lu, GY ;
Zhou, ZH ;
Baker, ML ;
Jakana, J ;
Cai, DY ;
Wei, XC ;
Chen, SX ;
Gu, XC ;
Chiu, W .
JOURNAL OF VIROLOGY, 1998, 72 (11) :8541-8549
[6]   The 42K protein of rice dwarf virus is a post-translational cleavage product of the 46K outer capsid protein [J].
Mao, ZJ ;
Li, Y ;
Xu, H ;
Zheng, HH ;
Schiemann, J ;
Casper, R ;
Chen, ZL .
ARCHIVES OF VIROLOGY, 1998, 143 (09) :1831-1838
[7]   CRYSTALLIZATION AND PRELIMINARY-X-RAY STUDY OF A DOUBLE-SHELLED SPHERICAL VIRUS, RICE DWARF VIRUS [J].
MIZUNO, H ;
KANO, H ;
OMURA, T ;
KOIZUMI, M ;
KONDOH, M ;
TSUKIHARA, T .
JOURNAL OF MOLECULAR BIOLOGY, 1991, 219 (04) :665-669
[8]   RAPID ISOLATION OF HIGH MOLECULAR-WEIGHT PLANT DNA [J].
MURRAY, MG ;
THOMPSON, WF .
NUCLEIC ACIDS RESEARCH, 1980, 8 (19) :4321-4325
[9]   A low-resolution structure of rice dwarf virus determined by ab initio phasing [J].
Naitow, H ;
Morimoto, Y ;
Mizuno, H ;
Kano, H ;
Omura, T ;
Koizumi, M ;
Tsukihara, T .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1999, 55 :77-84
[10]   SEQUENCE-ANALYSIS OF THE RICE DWARF PHYTOREOVIRUS SEGMENT S3 TRANSCRIPT ENCODING FOR THE MAJOR STRUCTURAL CORE PROTEIN OF 114 KDA [J].
SUZUKI, N ;
WATANABE, Y ;
KUSANO, T ;
KITAGAWA, Y .
VIROLOGY, 1990, 179 (01) :455-459