Structural disorder within the replicative complex of measles virus: Functional implications

被引:78
作者
Bourhis, JM
Canard, B
Longhi, S
机构
[1] CNRS, AFMB, UMR 6098, F-13288 Marseille 09, France
[2] Univ Aix Marseille 1, F-13288 Marseille 09, France
关键词
measles virus; Paramyxoviridae; negative strand RNA viruses; replication; replicative complex; P and N structure; intrinsic or structural disorder; induced folding;
D O I
10.1016/j.virol.2005.09.025
中图分类号
Q93 [微生物学];
学科分类号
071005 [微生物学]; 100705 [微生物与生化药学];
摘要
Measles virus belongs to the Paramyxoviridae family within the Mononegavirales order. Its non-segmented, single stranded, negative sense RNA genome is encapsidated by the nucleoprotein (N) to form a helical nucleocapsid. This ribonucleoproteic complex is the substrate for both transcription and replication. The RNA-dependent RNA polymerase binds to the nucleocapsid template via its co-factor, the phosphoprotein (P). In this review, we summarize the main experimental data pointing out the abundance of structural disorder within measles virus N and P. We also describe studies indicating that structural disorder is a widespread property in the replicative complex of Paramyxoviridae and, more generally, of Mononegavirales. The functional implications of structural disorder are also discussed. Finally, we propose a model where the flexibility of the disordered N and P domains allows the formation of a tripartite complex (N degrees-P-L) during replication, followed by the delivery of N monomers to the newly synthesized genomic RNA chain. (c) 2005 Elsevier Inc. All rights reserved.
引用
收藏
页码:94 / 110
页数:17
相关论文
共 112 条
[1]
Albertini A. A. V., 2005, Virologie (Montrouge), V9, P83
[2]
Domains of the measles virus N protein required for binding to P protein and self-assembly [J].
Bankamp, B ;
Horikami, SM ;
Thompson, PD ;
Huber, M ;
Billeter, M ;
Moyer, SA .
VIROLOGY, 1996, 216 (01) :272-277
[3]
SEQUENCE OF THE MAJOR NUCLEOCAPSID PROTEIN GENE OF PNEUMONIA VIRUS OF MICE - SEQUENCE COMPARISONS SUGGEST STRUCTURAL HOMOLOGY BETWEEN NUCLEOCAPSID PROTEINS OF PNEUMOVIRUSES, PARAMYXOVIRUSES, RHABDOVIRUSES AND FILOVIRUSES [J].
BARR, J ;
CHAMBERS, P ;
PRINGLE, CR ;
EASTON, AJ .
JOURNAL OF GENERAL VIROLOGY, 1991, 72 :677-685
[4]
Conformational flexibility in recombinant measles virus nucleocapsids visualised by cryo-negative stain electron microscopy and real-space helical reconstruction [J].
Bhella, D ;
Ralph, A ;
Yeo, RP .
JOURNAL OF MOLECULAR BIOLOGY, 2004, 340 (02) :319-331
[5]
Significant differences in nucleocapsid morphology within the Paramyxoviridae [J].
Bhella, D ;
Ralph, A ;
Murphy, LB ;
Yeo, RP .
JOURNAL OF GENERAL VIROLOGY, 2002, 83 :1831-1839
[6]
N-PROTEIN OF VESICULAR STOMATITIS-VIRUS SELECTIVELY ENCAPSIDATES LEADER RNA INVITRO [J].
BLUMBERG, BM ;
GIORGI, C ;
KOLAKOFSKY, D .
CELL, 1983, 32 (02) :559-567
[7]
The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner [J].
Bourhis, JM ;
Johansson, K ;
Receveur-Bréchot, V ;
Oldfield, CJ ;
Dunker, KA ;
Canard, B ;
Longhi, S .
VIRUS RESEARCH, 2004, 99 (02) :157-167
[8]
The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded [J].
Bourhis, JM ;
Receveur-Bréchot, V ;
Oglesbee, M ;
Zhang, XS ;
Buccellato, M ;
Darbon, H ;
Canard, B ;
Finet, S ;
Longhi, S .
PROTEIN SCIENCE, 2005, 14 (08) :1975-1992
[9]
Profilin is required for optimal actin-dependent transcription of respiratory syncytial virus genome RNA [J].
Burke, E ;
Mahoney, NM ;
Almo, SC ;
Barik, S .
JOURNAL OF VIROLOGY, 2000, 74 (02) :669-675
[10]
Deciphering protein sequence information through hydrophobic cluster analysis (HCA): current status and perspectives [J].
Callebaut, I ;
Labesse, G ;
Durand, P ;
Poupon, A ;
Canard, L ;
Chomilier, J ;
Henrissat, B ;
Mornon, JP .
CELLULAR AND MOLECULAR LIFE SCIENCES, 1997, 53 (08) :621-645