Characterization of the Lassa virus matrix protein Z: electron microscopic study of virus-like particles and interaction with the nucleoprotein (NP)

被引:76
作者
Eichler, R
Strecker, T
Kolesnikova, L
ter Meulen, J
Weissenhorn, W
Becker, S
Klenk, HD
Garten, W
Lenz, O
机构
[1] Univ Marburg, Inst Virol, D-35037 Marburg, Germany
[2] European Mol Biol Lab, F-38000 Grenoble, France
关键词
Arenavirus; Lassa virus; matrix protein; late domain; virus-like particles; nucleoprotein interaction;
D O I
10.1016/j.virusres.2003.11.017
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Lassa virus is the causative agent of a hemorrhagic fever endemic in west Africa. The RNA genome of Lassa virus encodes the glycoprotein precursor GP-C, a nucleoprotein (NP), the viral polymerase L and a small protein Z (11 kDa). Here, we analyze the role of Z protein for virus maturation. We have recently shown that expression of Z protein in the absence of other viral proteins is sufficient for the release of enveloped Z-containing particles. In this study, we examined particles secreted into the supernatant of a stably Z protein-expressing CHO cell line by electron microscopy. The observed Z-induced virus-like particles did not significantly differ in their morphology and size from Lassa virus particles. Mutation of two proline-rich domains within Z which are known to drastically reduce the release of virus-like particles, had no effect on the cellular localization of the protein nor on its membrane-association. Furthermore, we present evidence that Z interacts with the NP. We assume that Z recruits NP to cellular membranes where virus assembly takes place. We conclude from our data that Lassa virus Z protein plays an essential role in Lassa virus maturation. (C) 2003 Elsevier B.V. All rights reserved.
引用
收藏
页码:249 / 255
页数:7
相关论文
共 27 条
[21]   The small RING finger protein Z drives arenavirus budding: Implications for antiviral strategies [J].
Perez, M ;
Craven, RC ;
de la Torre, JC .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (22) :12978-12983
[22]   Mechanisms of enveloped RNA virus budding [J].
Pornillos, O ;
Garrus, JE ;
Sundquist, WI .
TRENDS IN CELL BIOLOGY, 2002, 12 (12) :569-579
[23]   BIOCHEMICAL AND IMMUNOLOGICAL EVIDENCE THAT THE 11-KDA ZINC-BINDING PROTEIN OF LYMPHOCYTIC CHORIOMENINGITIS VIRUS IS A STRUCTURAL COMPONENT OF THE VIRUS [J].
SALVATO, MS ;
SCHWEIGHOFER, KJ ;
BURNS, J ;
SHIMOMAYE, EM .
VIRUS RESEARCH, 1992, 22 (03) :185-198
[24]   THE COMPLETED SEQUENCE OF LYMPHOCYTIC CHORIOMENINGITIS VIRUS REVEALS A UNIQUE RNA STRUCTURE AND A GENE FOR A ZINC FINGER PROTEIN [J].
SALVATO, MS ;
SHIMOMAYE, EM .
VIROLOGY, 1989, 173 (01) :1-10
[25]   Lassa virus Z protein is a matrix protein sufficient for the release of virus-like particles [J].
Strecker, T ;
Eichler, R ;
ter Meulen, J ;
Weissenhorn, W ;
Klenk, HD ;
Garten, W ;
Lenz, O .
JOURNAL OF VIROLOGY, 2003, 77 (19) :10700-10705
[26]   Ebola virus matrix protein VP40 interaction with human cellular factors Tsg101 and Nedd4 [J].
Timmins, J ;
Schoehn, G ;
Ricard-Blum, S ;
Scianimanico, S ;
Vernet, T ;
Ruigrok, RWH ;
Weissenhorn, W .
JOURNAL OF MOLECULAR BIOLOGY, 2003, 326 (02) :493-502
[27]   Vesicular release of Ebola virus matrix protein VP40 [J].
Timmins, J ;
Scianimanico, S ;
Schoehn, G ;
Weissenhorn, W .
VIROLOGY, 2001, 283 (01) :1-6