Crystal structure of the rabies virus nucleoprotein-RNA complex

被引:258
作者
Albertini, Aurelie A. V.
Wernimont, Amy K.
Muziol, Tadeusz
Ravelli, Raimond B. G.
Clapier, Cedric R.
Schoehn, Guy
Weissenhorn, Winfried
Ruigrok, Rob W. H.
机构
[1] European Mol Biol Lab, F-38042 Grenoble, France
[2] Univ Grenoble 1, Inst Virol Mol & Struct, CNRS, FRE 2854, F-38042 Grenoble, France
关键词
D O I
10.1126/science.1125280
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Negative-strand RNA viruses condense their genome into a helical nucleoprotein-RNA complex, the nucleocapsid, which is packed into virions and serves as a template for the RNA-dependent RNA polymerase complex. The crystal structure of a recombinant rabies virus nucleoprotein-RNA complex, organized in an undecameric ring, has been determined at 3.5 angstrom resolution. Polymerization of the nucleoprotein is achieved by domain exchange between protomers, with flexible hinges allowing nucleocapsid formation. The two core domains of the nucleoprotein clamp around the RNA at their interface and shield it from the environment. RNA sequestering by nucleoproteins is likely a common mechanism used by negative-strand RNA viruses to protect their genomes from the innate immune response directed against viral RNA in human host cells at certain stages of an infectious cycle.
引用
收藏
页码:360 / 363
页数:4
相关论文
共 25 条
[1]   Pathogen recognition and innate immunity [J].
Akira, S ;
Uematsu, S ;
Takeuchi, O .
CELL, 2006, 124 (04) :783-801
[2]   ROLE OF THE NUCLEOCAPSID PROTEIN IN REGULATING VESICULAR STOMATITIS-VIRUS RNA-SYNTHESIS [J].
ARNHEITER, H ;
DAVIS, NL ;
WERTZ, G ;
SCHUBERT, M ;
LAZZARINI, RA .
CELL, 1985, 41 (01) :259-267
[3]   N-PROTEIN OF VESICULAR STOMATITIS-VIRUS SELECTIVELY ENCAPSIDATES LEADER RNA INVITRO [J].
BLUMBERG, BM ;
GIORGI, C ;
KOLAKOFSKY, D .
CELL, 1983, 32 (02) :559-567
[4]  
Dietzschold B, 2005, CURR TOP MICROBIOL, V292, P45
[5]   LOCALIZATION AND IMMUNOLOGICAL CHARACTERIZATION OF ANTIGENIC DOMAINS OF THE RABIES VIRUS INTERNAL N-PROTEIN AND NS PROTEIN [J].
DIETZSCHOLD, B ;
LAFON, M ;
WANG, H ;
OTVOS, L ;
CELIS, E ;
WUNNER, WH ;
KOPROWSKI, H .
VIRUS RESEARCH, 1987, 8 (02) :103-125
[6]   RECONSTITUTION STUDIES DETECT A SINGLE POLYMERASE ENTRY SITE ON THE VESICULAR STOMATITIS-VIRUS GENOME [J].
EMERSON, SU .
CELL, 1982, 31 (03) :635-642
[7]   LOCATION OF THE BINDING DOMAINS FOR THE RNA POLYMERASE-L AND THE RIBONUCLEOCAPSID TEMPLATE WITHIN DIFFERENT HALVES OF THE NS PHOSPHOPROTEIN OF VESICULAR STOMATITIS-VIRUS [J].
EMERSON, SU ;
SCHUBERT, M .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1987, 84 (16) :5655-5659
[8]   ISG20, a new interferon-induced RNase specific for single-stranded RNA, defines an alternative antiviral pathway against RNA genomic viruses [J].
Espert, L ;
Degols, G ;
Gongora, C ;
Blondel, D ;
Williams, BR ;
Silverman, RH ;
Mechti, N .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (18) :16151-16158
[9]   Structure of the RNA inside the vesicular stomatitis virus nucleocapsid [J].
Iseni, F ;
Baudin, F ;
Blondel, D ;
Ruigrok, RWH .
RNA, 2000, 6 (02) :270-281
[10]   Characterization of rabies virus nucleocapsids and recombinant nucleocapsid-like structures [J].
Iseni, F ;
Barge, A ;
Baudin, F ;
Blondel, D ;
Ruigrok, RWH .
JOURNAL OF GENERAL VIROLOGY, 1998, 79 :2909-2919