| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
Department of Genetics and Microbiology, University of Geneva Medical School, C.M.U., 9 Avenue de Champel, 1211 Geneva 4, Switzerland
The matrix (M) protein is viewed as the regulator of paramyxovirus particle assembly and budding. Accordingly it was observed to be mutated, and/or decreased in amount, in cases where virus particle production was significantly reduced. Here, a non-productive [non-defective and defective interfering (DI)] Sendai virus infection of COS cells is presented where virus particle production is abolished in the presence of a normal amount of intracellular M protein. In this infection the haemagglutinin—neuraminidase envelope glycoprotein is shown to be dispensable for virion production, and the fusion (F0) envelope glycoprotein behaves as in a productive infection. The M protein is shown to accumulate in perinuclear patches within the cytoplasm. In contrast, localization in the plasma membrane is observed in productive infections. However in both productive and non-productive infections a significant fraction of M protein is found in association with cellular membranes. The M protein-membrane association is shown to take place in the absence of any other viral component, and the M protein-membrane complex exhibits properties similar to those observed for the integral membrane protein F0. However these properties are distinct from those of the phosphoprotein, which is thought to associate with membranes in a non-specific manner. Concomitant with the cytoplasmic accumulation of M protein and the reduction of virus particle production in this non-productive infection, DI nucleocapsids are shown not to associate with cellular membrane fractions. This is a property which coincides with their poor envelopment in virus particles. Taken together, these data indicate the need for M protein to be recruited at the perinuclear membranes by the nucleocapsids to participate in viral assembly and budding. This view is consistent with a process of viral assembly taking place on internal cytoplasmic membranes rather than at the plasma membrane.
Received 13 September 1993;
accepted 26 November 1993.
This article has been cited by other articles:
|
|
 |
|
  G. Mottet-Osman, F. Iseni, T. Pelet, M. Wiznerowicz, D. Garcin, and L. Roux Suppression of the Sendai Virus M Protein through a Novel Short Interfering RNA Approach Inhibits Viral Particle Production but Does Not Affect Viral RNA Synthesis J. Virol., March 15, 2007; 81(6): 2861 - 2868. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. J. Ciancanelli and C. F. Basler Mutation of YMYL in the Nipah Virus Matrix Protein Abrogates Budding and Alters Subcellular Localization J. Virol., December 15, 2006; 80(24): 12070 - 12078. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
H. D. Pantua, L. W. McGinnes, M. E. Peeples, and T. G. Morrison Requirements for the Assembly and Release of Newcastle Disease Virus-Like Particles J. Virol., November 15, 2006; 80(22): 11062 - 11073. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Armeanu, M. Bitzer, I. Smirnow, S. Bossow, S. Appel, G. Ungerechts, C. Bernloehr, W. J. Neubert, U. M. Lauer, and P. Brossart Severe Impairment of Dendritic Cell Allostimulatory Activity by Sendai Virus Vectors Is Overcome by Matrix Protein Gene Deletion J. Immunol., October 15, 2005; 175(8): 4971 - 4980. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. Sakaguchi, A. Kato, F. Sugahara, Y. Shimazu, M. Inoue, K. Kiyotani, Y. Nagai, and T. Yoshida AIP1/Alix Is a Binding Partner of Sendai Virus C Protein and Facilitates Virus Budding J. Virol., July 15, 2005; 79(14): 8933 - 8941. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 L. Rodriguez, I. Cuesta, A. Asenjo, and N. Villanueva Human respiratory syncytial virus matrix protein is an RNA-binding protein: binding properties, location and identity of the RNA contact residues J. Gen. Virol., March 1, 2004; 85(3): 709 - 719. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. Kolesnikova, H. Bugany, H.-D. Klenk, and S. Becker VP40, the Matrix Protein of Marburg Virus, Is Associated with Membranes of the Late Endosomal Compartment J. Virol., February 15, 2002; 76(4): 1825 - 1838. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. Takimoto, K. G. Murti, T. Bousse, R. A. Scroggs, and A. Portner Role of Matrix and Fusion Proteins in Budding of Sendai Virus J. Virol., December 1, 2001; 75(23): 11384 - 11391. [Abstract] [Full Text]
|
|
|
|
|
|
G. Mottet, V. Müller, and L. Roux Characterization of Sendai virus M protein mutants that can partially interfere with virus particle production J. Gen. Virol., November 1, 1999; 80(11): 2977 - 2986. [Abstract] [Full Text]
|
|
|
|
|
|
T. Takimoto, T. Bousse, E. C. Coronel, R. A. Scroggs, and A. Portner Cytoplasmic Domain of Sendai Virus HN Protein Contains a Specific Sequence Required for Its Incorporation into Virions J. Virol., December 1, 1998; 72(12): 9747 - 9754. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. Cathomen, H. Y. Naim, and R. Cattaneo Measles Viruses with Altered Envelope Protein Cytoplasmic Tails Gain Cell Fusion Competence J. Virol., February 1, 1998; 72(2): 1224 - 1234. [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 | |
