|
|
||||||||
Animal: RNA Viruses |
Medical Research Council Virology Unit, Church Street, Glasgow G11 5JR, UK1
Author for correspondence: David Bhella. Fax +44 141 337 2236. e-mail d.bhella{at}vir.gla.ac.uk
Nucleocapsid (N) proteins from representative viruses of three genera within the Paramyxoviridae were expressed in insect cells using recombinant baculoviruses. RNA-containing structures, which appear morphologically identical to viral nucleocapsids, were isolated and subsequently imaged under a transmission electron microscope. Analysis of these images revealed marked differences in nucleocapsid morphology among the genera investigated, most notably between viruses of the Paramyxovirinae and the Pneumovirinae subfamilies. Helical pitch measurements were made, revealing that measles virus (MV, a Morbillivirus within the subfamily Paramyxovirinae) N protein produces helices that adopt multiple conformations with varying degrees of flexibility, while that of the Rubulavirus simian virus type 5 (SV5, subfamily Paramyxovirinae) produces more rigid structures with a less heterogeneous pitch distribution. Nucleocapsids produced by respiratory syncytial virus (RSV, subfamily Pneumovirinae) appear significantly narrower than those of MV and SV5 and have a longer pitch than the most extended form of MV. In addition to helical nucleocapsids, ring structures were also produced, image analysis of which has demonstrated that rings assembled from MV N protein consist of 13 subunits. This is consistent with previous reports that Sendai virus nucleocapsids have 13·07 subunits per turn. It was determined, however, that SV5 subnucleocapsid rings have 14 subunits, while rings derived from the radically different RSV nucleocapsid have been found to contain predominantly 10 subunits.
This article has been cited by other articles:
![]() |
S. T. Ong, K. Yusoff, C. L. Kho, J. O. Abdullah, and W. S. Tan Mutagenesis of the nucleocapsid protein of Nipah virus involved in capsid assembly J. Gen. Virol., February 1, 2009; 90(2): 392 - 397. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. Derdowski, T. R. Peters, N. Glover, R. Qian, T. J. Utley, A. Burnett, J. V. Williams, P. Spearman, and J. E. Crowe Jr Human metapneumovirus nucleoprotein and phosphoprotein interact and provide the minimal requirements for inclusion body formation J. Gen. Virol., November 1, 2008; 89(11): 2698 - 2708. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. Chen, T. Ogino, and A. K. Banerjee Interaction of Vesicular Stomatitis Virus P and N Proteins: Identification of Two Overlapping Domains at the N Terminus of P That Are Involved in N0-P Complex Formation and Encapsidation of Viral Genome RNA J. Virol., December 15, 2007; 81(24): 13478 - 13485. [Abstract] [Full Text] [PDF] |
||||
![]() |
K. MacLellan, C. Loney, R. P. Yeo, and D. Bhella The 24-Angstrom Structure of Respiratory Syncytial Virus Nucleocapsid Protein-RNA Decameric Rings J. Virol., September 1, 2007; 81(17): 9519 - 9524. [Abstract] [Full Text] [PDF] |
||||
![]() |
P. J. Santangelo and G. Bao Dynamics of filamentous viral RNPs prior to egress Nucleic Acids Res., June 28, 2007; 35(11): 3602 - 3611. [Abstract] [Full Text] [PDF] |
||||
![]() |
T.-L. Tran, N. Castagne, D. Bhella, P. F. Varela, J. Bernard, S. Chilmonczyk, S. Berkenkamp, V. Benhamo, K. Grznarova, J. Grosclaude, et al. The nine C-terminal amino acids of the respiratory syncytial virus protein P are necessary and sufficient for binding to ribonucleoprotein complexes in which six ribonucleotides are contacted per N protein protomer J. Gen. Virol., January 1, 2007; 88(1): 196 - 206. [Abstract] [Full Text] [PDF] |
||||
![]() |
V. M. Cowton, D. R. McGivern, and R. Fearns Unravelling the complexities of respiratory syncytial virus RNA synthesis J. Gen. Virol., July 1, 2006; 87(7): 1805 - 1821. [Abstract] [Full Text] [PDF] |
||||
![]() |
S. Watanabe, T. Noda, and Y. Kawaoka Functional mapping of the nucleoprotein of ebola virus. J. Virol., April 1, 2006; 80(8): 3743 - 3751. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. Schwardt, D. Mayer, R. Frank, U. Schneider, M. Eickmann, O. Planz, T. Wolff, and M. Schwemmle The negative regulator of Borna disease virus polymerase is a non-structural protein J. Gen. Virol., November 1, 2005; 86(11): 3163 - 3169. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. Eshaghi, W. S. Tan, S. T. Ong, and K. Yusoff Purification and Characterization of Nipah Virus Nucleocapsid Protein Produced in Insect Cells J. Clin. Microbiol., July 1, 2005; 43(7): 3172 - 3177. [Abstract] [Full Text] [PDF] |
||||
![]() |
D. Vulliemoz, S. Cordey, G. Mottet-Osman, and L. Roux Nature of a paramyxovirus replication promoter influences a nearby transcription signal J. Gen. Virol., January 1, 2005; 86(1): 171 - 180. [Abstract] [Full Text] [PDF] |
||||
![]() |
R. L. Kingston, W. A. Baase, and L. S. Gay Characterization of Nucleocapsid Binding by the Measles Virus and Mumps Virus Phosphoproteins J. Virol., August 15, 2004; 78(16): 8630 - 8640. [Abstract] [Full Text] [PDF] |
||||
![]() |
N. Castagne, A. Barbier, J. Bernard, H. Rezaei, J.-C. Huet, C. Henry, B. D. Costa, and J.-F. Eleouet Biochemical characterization of the respiratory syncytial virus P-P and P-N protein complexes and localization of the P protein oligomerization domain J. Gen. Virol., June 1, 2004; 85(6): 1643 - 1653. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. J. Easton, J. B. Domachowske, and H. F. Rosenberg Animal Pneumoviruses: Molecular Genetics and Pathogenesis Clin. Microbiol. Rev., April 1, 2004; 17(2): 390 - 412. [Abstract] [Full Text] [PDF] |
||||
![]() |
K. Johansson, J.-M. Bourhis, V. Campanacci, C. Cambillau, B. Canard, and S. Longhi Crystal Structure of the Measles Virus Phosphoprotein Domain Responsible for the Induced Folding of the C-terminal Domain of the Nucleoprotein J. Biol. Chem., November 7, 2003; 278(45): 44567 - 44573. [Abstract] [Full Text] [PDF] |
||||
![]() |
D. Laine, M.-C. Trescol-Biemont, S. Longhi, G. Libeau, J. C. Marie, P.-O. Vidalain, O. Azocar, A. Diallo, B. Canard, C. Rabourdin-Combe, et al. Measles Virus (MV) Nucleoprotein Binds to a Novel Cell Surface Receptor Distinct from Fc{gamma}RII via Its C-Terminal Domain: Role in MV-Induced Immunosuppression J. Virol., November 1, 2003; 77(21): 11332 - 11346. [Abstract] [Full Text] [PDF] |
||||
![]() |
H. L. Stokes, A. J. Easton, and A. C. Marriott Chimeric pneumovirus nucleocapsid (N) proteins allow identification of amino acids essential for the function of the respiratory syncytial virus N protein J. Gen. Virol., October 1, 2003; 84(10): 2679 - 2683. [Abstract] [Full Text] [PDF] |
||||
![]() |
S. Longhi, V. Receveur-Brechot, D. Karlin, K. Johansson, H. Darbon, D. Bhella, R. Yeo, S. Finet, and B. Canard The C-terminal Domain of the Measles Virus Nucleoprotein Is Intrinsically Disordered and Folds upon Binding to the C-terminal Moiety of the Phosphoprotein J. Biol. Chem., May 9, 2003; 278(20): 18638 - 18648. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| INT J SYST EVOL MICROBIOL | MICROBIOLOGY | J GEN VIROL |
| J MED MICROBIOL | ALL SGM JOURNALS | |