Filovirus assembly and budding

被引:96
作者
Hartlieb, B
Weissenhorn, W
机构
[1] European Mol Biol Lab, F-38042 Grenoble, France
[2] Inst Virol, D-35037 Marburg, Germany
关键词
D O I
10.1016/j.virol.2005.09.018
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Filoviruses belong to the order of negative-stranded non-segmented RNA viruses and are classified into two genera, Ebola and Marburg viruses. They have a characteristic filamentous shape, which is largely determined by the matrix protein VP40. Although VP40 is the main driving force for assembly and budding from the host cell, the production of infectious virus involves an intricate interplay between all viral structural proteins in addition to cellular factors, e.g., those that normally function in multi-vesicular body biogenesis. As a consequence, assembly and budding steps are defined to specific cellular compartments, and the recent progress in understanding how the different components are assembled into stable enveloped virus particles is reviewed. (c) 2005 Elsevier Inc. All rights reserved.
引用
收藏
页码:64 / 70
页数:7
相关论文
共 90 条
[1]   The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function [J].
Babst, M ;
Wendland, B ;
Estepa, EJ ;
Emr, SD .
EMBO JOURNAL, 1998, 17 (11) :2982-2993
[2]   Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body [J].
Babst, M ;
Katzmann, DJ ;
Snyder, WB ;
Wendland, B ;
Emr, SD .
DEVELOPMENTAL CELL, 2002, 3 (02) :283-289
[3]   ESCRT-III: An endosome-associated heterooligomeric protein complex required for MVB sorting [J].
Babst, M ;
Katzmann, DJ ;
Estepa-Sabal, EJ ;
Meerloo, T ;
Emr, SD .
DEVELOPMENTAL CELL, 2002, 3 (02) :271-282
[4]   Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes [J].
Bache, KG ;
Brech, A ;
Mehlum, A ;
Stenmark, H .
JOURNAL OF CELL BIOLOGY, 2003, 162 (03) :435-442
[5]   VP24 of Marburg virus influences formation of infectious particles [J].
Bamberg, S ;
Kolesnikova, L ;
Möller, P ;
Klenk, HD ;
Becker, S .
JOURNAL OF VIROLOGY, 2005, 79 (21) :13421-13433
[6]   Lipid raft microdomains: A gateway for compartmentalized trafficking of Ebola and Marburg viruses [J].
Bavari, S ;
Bosio, CM ;
Wiegand, E ;
Ruthel, G ;
Will, AB ;
Geisbert, TW ;
Hevey, M ;
Schmaljohn, C ;
Schmaljohn, A ;
Aman, MJ .
JOURNAL OF EXPERIMENTAL MEDICINE, 2002, 195 (05) :593-602
[7]   Interactions of Marburg virus nucleocapsid proteins [J].
Becker, S ;
Rinne, C ;
Hofsäss, U ;
Klenk, HD ;
Mühlberger, E .
VIROLOGY, 1998, 249 (02) :406-417
[8]   THE NUCLEOPROTEIN OF MARBURG VIRUS IS PHOSPHORYLATED [J].
BECKER, S ;
HUPPERTZ, S ;
KLENK, HD ;
FELDMANN, H .
JOURNAL OF GENERAL VIROLOGY, 1994, 75 :809-818
[9]   Nucleocapsid incorporation into parainfluenza virus is regulated by specific interaction with matrix protein [J].
Coronel, EC ;
Takimoto, T ;
Murti, KG ;
Varich, N ;
Portner, A .
JOURNAL OF VIROLOGY, 2001, 75 (03) :1117-1123
[10]   Overexpression of the N-terminal domain of TSG101 inhibits HIV-1 budding by blocking late domain function [J].
Demirov, DG ;
Ono, A ;
Orenstein, JM ;
Freed, EO .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (02) :955-960