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Journal of Virology, June 2000, p. 5619-5628, Vol. 74, No. 12
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Versatility of the Accessory C Proteins of Sendai Virus: Contribution to Virus Assembly as an Additional Role

Mohammad K. Hasan,1 Atsushi Kato,1 Miki Muranaka,2 Ryoji Yamaguchi,2 Yuko Sakai,3 Ikuyoshi Hatano,4 Masato Tashiro,1 and Yoshiyuki Nagai3,5,*

Department of Viral Diseases and Vaccine Control,1 Department of Safety Research on Biologics,4 and AIDS Research Center,5 National Institute of Infectious Diseases, Tokyo 208-0011, Department of Pathology, Faculty of Agriculture, Miyazaki University, Miyazaki 889-2155,2 and Department of Viral Infection, Institute of Medical Science, University of Tokyo, Tokyo 108-8639,3 Japan

Received 29 December 1999/Accepted 23 March 2000

The P/C mRNA of Sendai virus (SeV) encodes a nested set of accessory proteins, C', C, Y1, and Y2, referred to collectively as C proteins, using the +1 frame relative to the open reading frame of phospho (P) protein and initiation codons at different positions. The C proteins appear to be basically nonstructural proteins as they are found abundantly in infected cells but greatly underrepresented in the virions. We previously created a 4C(-) SeV, which expresses none of the four C proteins, and concluded that the C proteins are categorically nonessential gene products but greatly contribute to viral full replication and infectivity (A. Kurotani et al., Genes Cells 3:111-124, 1998). Here, we further characterized the 4C(-) virus multiplication in cultured cells. The viral protein and mRNA synthesis was enhanced with the mutant virus relative to the parental wild-type (WT) SeV. However, the viral yields were greatly reduced. In addition, the 4C(-) virions appeared to be highly anomalous in size, shape, and sedimentation profile in a sucrose gradient and exhibited the ratios of infectivity to hemagglutination units significantly lower than those of the WT. In the WT infected cells, C proteins appeared to colocalize almost perfectly with the matrix (M) proteins, pretty well with an external envelope glycoprotein (hemagglutinin-neuraminidase [HN]), and very poorly with the internal P protein. In the absence of C proteins, there was a significant delay of the incorporation of M protein and both of the envelope proteins, HN and fusion (F) proteins, into progeny virions. These results strongly suggest that the accessory and basically nonstructural C proteins are critically required in the SeV assembly process. This role of C proteins was further found to be independent of their recently discovered function to counteract the antiviral action of interferon-alpha /beta . SeV C proteins thus appear to be quite versatile.

* Corresponding author. Mailing address: AIDS Research Center, National Institute of Infectious Diseases, Toyama 1-23-1, Shinjuku-ku, Tokyo 162-8640, Japan. Phone: 81 3 5285-1111, ext. 2302. Fax: 81 3 5285-1165. E-mail: ynagai{at}nih.go.jp.

Journal of Virology, June 2000, p. 5619-5628, Vol. 74, No. 12
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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