Characterization of the Ebola virus nucleoprotein-RNA complex

被引：73

作者：

Noda, Takeshi ^{[1
]}

Hagiwara, Kyoji ^{[2
]}

Sagara, Hiroshi ^{[3
]}

Kawaoka, Yoshihiro ^{[1
,4
,5
]}

机构：

[1] Univ Tokyo, Inst Med Sci, Int Res Ctr Infect Dis, Minato Ku, Tokyo 1088639, Japan

[2] RIKEN, Viral Infect Dis Unit, Wako, Saitama 3510198, Japan

[3] Univ Tokyo, Inst Med Sci, Med Prote Lab, Minato Ku, Tokyo 1088639, Japan

[4] Univ Wisconsin, Sch Vet Med, Dept Pathobiol Sci, Madison, WI 53706 USA

[5] Univ Tokyo, Inst Med Sci, Dept Microbiol & Immunol, Div Virol,Minato Ku, Tokyo 1088639, Japan

来源：

JOURNAL OF GENERAL VIROLOGY | 2010年 / 91卷

关键词：

VESICULAR STOMATITIS-VIRUS; NUCLEOCAPSID-LIKE STRUCTURES; PROTEOLYTIC CLEAVAGE; CRYSTAL-STRUCTURE; PROTEIN; PHOSPHOPROTEIN; MORPHOLOGY; EXPRESSION; CELLS;

D O I：

10.1099/vir.0.019794-0

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

When Ebola virus nucleoprotein (NP) is expressed in mammalian cells, it assembles into helical structures Here, the recombinant NP helix purified from cells expressing NP was characterized biochemically and morphologically. We found that the recombinant NP helix is associated with non-viral RNA, which is not protected from RNase digestion and that the morphology of the helix changes depending on the environmental salt concentration The N-terminal 450 aa residues of NP are sufficient for these properties. However, digestion of the NP-associated RNA eliminates the plasticity of the helix, suggesting that this RNA is an essential structural component of the helix, binding to individual NP molecules via the N-terminal 450 aa These findings enhance our knowledge of Ebola virus assembly and understanding of the Ebola virus life cycle

引用

页码：1478 / 1483

页数：6

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