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Journal of Virology, August 2007, p. 8766-8773, Vol. 81, No. 16
0022-538X/07/$08.00+0     doi:10.1128/JVI.00075-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

A Mutation on Influenza C Virus M1 Protein Affects Virion Morphology by Altering the Membrane Affinity of the Protein{triangledown}

Yasushi Muraki,1* Toshio Murata,2 Emi Takashita,1 Yoko Matsuzaki,1 Kanetsu Sugawara,1 and Seiji Hongo1

Department of Infectious Diseases, Yamagata University School of Medicine, Iida-Nishi, 990-9585, Yamagata, Japan,1 Department of Microbiology, Yamagata Prefectural Institute of Public Health, Toka-machi, 990-0031, Yamagata, Japan2

Received 11 January 2007/ Accepted 16 May 2007

Reverse genetics has been documented for influenza A, B, and Thogoto viruses belonging to the family Orthomyxoviridae. We report here the reverse genetics of influenza C virus, another member of this family. The seven viral RNA (vRNA) segments of C/Ann Arbor/1/50 were expressed in 293T cells from cloned cDNAs, together with nine influenza C virus proteins. At 48 h posttransfection, the infectious titer of the culture supernatant was determined to be 2.51 x 103 50% egg infectious doses/ml, which is lower than the number of influenza C virus-like particles (VLPs) (106/ml) generated using the same system. By generating influenza C VLPs containing a given vRNA segment, we showed that each of the vRNA segments was similarly synthesized in the plasmid-transfected cells but that some segments were less efficiently incorporated into the VLPs. This finding leads us to speculate that the differences in incorporation efficiency into VLPs between segments might be a reason for the inefficient production of infectious viruses. Second, we generated a mutant recombinant virus, rMG96A, which possesses an Ala->Thr mutation at residue 24 of the M1 protein, a substitution demonstrated to be involved in the morphology (filamentous or spherical) of the influenza C VLPs. As expected, rMG96A exhibited a spherical morphology, whereas recombinant wild-type of C/Ann Arbor/1/50, rWT, exhibited a mainly filamentous morphology. Membrane flotation analysis of the cells infected with rWT or rMG96A revealed a difference in the ratio of membrane-associated M1 proteins, suggesting that the affinity of M1 protein to the cell membrane is a determinant for virion morphology.

* Corresponding author. Mailing address: Department of Infectious Diseases, Yamagata University School of Medicine, Iida-Nishi, 990-9585, Yamagata, Japan. Phone: 81-23-628-5249. Fax: 81-23-628-5250. E-mail: ymuraki{at}med.id.yamagata-u.ac.jp

{triangledown} Published ahead of print on 30 May 2007.

Journal of Virology, August 2007, p. 8766-8773, Vol. 81, No. 16
0022-538X/07/$08.00+0     doi:10.1128/JVI.00075-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Gao, Q., Brydon, E. W. A., Palese, P. (2008). A Seven-Segmented Influenza A Virus Expressing the Influenza C Virus Glycoprotein HEF. J. Virol. 82: 6419-6426 [Abstract] [Full Text]  
  • Crescenzo-Chaigne, B., van der Werf, S. (2007). Rescue of Influenza C Virus from Recombinant DNA. J. Virol. 81: 11282-11289 [Abstract] [Full Text]  


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