This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Yamashita, M Articles by Palese, P Search for Related Content PubMed PubMed Citation Articles by Yamashita, M Articles by Palese, P

 Previous Article  |  Next Article 

J Virol. 1988 September; 62(9): 3348-3355

Evidence that the matrix protein of influenza C virus is coded for by a spliced mRNA.

Department of Microbiology, Mount Sinai School of Medicine, City University of New York, New York 10029.

ABSTRACT

In contrast to influenza A and B viruses, which encode their matrix (M) proteins via an unspliced mRNA, the influenza C virus M protein appears to be coded for by a spliced mRNA from RNA segment 6. Although an open reading frame in RNA segment 6 of influenza C/JJ/50 virus could potentially code for a protein of 374 amino acids, a splicing event results in an mRNA coding for a 242-amino-acid M protein. The message for this protein represents the major M gene-specific mRNA species in C virus-infected cells. Despite the difference in coding strategies, there are sequence homologies among the M proteins of influenza A, B, and C viruses which confirm the evolutionary relationship of the three influenza virus types.

This article has been cited by other articles:

• Betakova, T., Hay, A. J. (2007). Evidence that the CM2 protein of influenza C virus can modify the pH of the exocytic pathway of transfected cells. J. Gen. Virol. 88: 2291-2296 [Abstract] [Full Text]  
• Muraki, Y., Washioka, H., Sugawara, K., Matsuzaki, Y., Takashita, E., Hongo, S. (2004). Identification of an amino acid residue on influenza C virus M1 protein responsible for formation of the cord-like structures of the virus. J. Gen. Virol. 85: 1885-1893 [Abstract] [Full Text]  
• Li, Z.-N., Hongo, S., Sugawara, K., Sugahara, K., Tsuchiya, E., Matsuzaki, Y., Nakamura, K. (2001). The sites for fatty acylation, phosphorylation and intermolecular disulphide bond formation of influenza C virus CM2 protein. J. Gen. Virol. 82: 1085-1093 [Abstract] [Full Text]  
• Pekosz, A., Lamb, R. A. (2000). Identification of a Membrane Targeting and Degradation Signal in the p42 Protein of Influenza C Virus. J. Virol. 74: 10480-10488 [Abstract] [Full Text]  
• Kochs, G., Weber, F., Gruber, S., Delvendahl, A., Leitz, C., Haller, O. (2000). Thogoto Virus Matrix Protein Is Encoded by a Spliced mRNA. J. Virol. 74: 10785-10789 [Abstract] [Full Text]  
• Alamgir, A. S. M., Matsuzaki, Y., Hongo, S., Tsuchiya, E., Sugawara, K., Muraki, Y., Nakamura, K. (2000). Phylogenetic analysis of influenza C virus nonstructural (NS) protein genes and identification of the NS2 protein. J. Gen. Virol. 81: 1933-1940 [Abstract] [Full Text]  
• Hongo, S., Sugawara, K., Muraki, Y., Matsuzaki, Y., Takashita, E., Kitame, F., Nakamura, K. (1999). Influenza C Virus CM2 Protein Is Produced from a 374-Amino-Acid Protein (P42) by Signal Peptidase Cleavage. J. Virol. 73: 46-50 [Abstract] [Full Text]  
• Pekosz, A., Lamb, R. A. (1998). Influenza C virus CM2 integral membrane glycoprotein is produced from a polypeptide precursor by cleavage of an internal signal sequence. Proc. Natl. Acad. Sci. USA 95: 13233-13238 [Abstract] [Full Text]