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Journal of Virology, December 2001, p. 11384-11391, Vol. 75, No. 23
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.23.11384-11391.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Role of Matrix and Fusion Proteins in Budding of Sendai Virus

Toru Takimoto,1,* K. Gopal Murti,1 Tatiana Bousse,1 Ruth Ann Scroggs,1 and Allen Portner1,2

Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105,1 and Department of Pathology, The Health Science Center, University of Tennessee---Memphis, Memphis, Tennessee 381632

Received 31 May 2001/Accepted 5 September 2001

Paramyxoviruses are assembled at the surface of infected cells, where virions are formed by the process of budding. We investigated the roles of three Sendai virus (SV) membrane proteins in the production of virus-like particles. Expression of matrix (M) proteins from cDNA induced the budding and release of virus-like particles that contained M, as was previously observed with human parainfluenza virus type 1 (hPIV1). Expression of SV fusion (F) glycoprotein from cDNA caused the release of virus-like particles bearing surface F, although their release was less efficient than that of particles bearing M protein. Cells that expressed only hemagglutinin-neuraminidase (HN) released no HN-containing vesicles. Coexpression of M and F proteins enhanced the release of F protein by a factor greater than 4. The virus-like particles containing F and M were found in different density gradient fractions of the media of cells that coexpressed M and F, a finding that suggests that the two proteins formed separate vesicles and did not interact directly. Vesicles released by M or F proteins also contained cellular actin; therefore, actin may be involved in the budding process induced by viral M or F proteins. Deletion of C-terminal residues of M protein, which has a sequence similar to that of an actin-binding domain, significantly reduced release of the particles into medium. Site-directed mutagenesis of the cytoplasmic tail of F revealed two regions that affect the efficiency of budding: one domain comprising five consecutive amino acids conserved in SV and hPIV1 and one domain that is similar to the actin-binding domain required for budding induced by M protein. Our results indicate that both M and F proteins are able to drive the budding of SV and propose the possible role of actin in the budding process.

* Corresponding author. Mailing address: Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, 332 N. Lauderdale, Memphis, TN 38105-2794. Phone: (901) 495-3438. Fax: (901) 523-2622. E-mail: toru.takimoto{at}stjude.org

Journal of Virology, December 2001, p. 11384-11391, Vol. 75, No. 23
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.23.11384-11391.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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