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J Gen Virol 73 (1992), 2479-2482; DOI 10.1099/0022-1317-73-9-2479
© 1992 Society for General Microbiology

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Nucleotide sequence of carnation ringspot dianthovirus RNA-2

T. L. Kendall and S. A. Lommel

Department of Plant Pathology, Box 7616, North Carolina State University, Raleigh, North Carolina 27695-7616, U.S.A.

RNA-2 of carnation ringspot virus (CRSV), the type member of the dianthovirus group, has been cDNA cloned and sequenced. CRSV RNA-2 is 1394 nucleotides in length and contains a single open reading frame encoding a 304 amino acid polypeptide of 33.8K. Amino acid sequence alignment of this polypeptide with the cell-to-cell movement proteins encoded by RNA-2 of red clover necrotic mosaic virus (RCNMV) Australian (Aus) and Czechoslovakian (TpM-34) isolates indicates 59.6% and 55.7% sequence identity, respectively. The N-terminal 230 amino acids are more highly conserved, with 64.3% and 62.6% sequence identity, respectively. The cell-to-cell movement proteins of the two RCNMV isolates are themselves 82.5% and 91.7% identical when the amino-terminal 230 amino acids are compared. Structural prediction comparison of the RCNMV-Aus, RCNMV-TpM-34 and tobacco mosaic virus cell-to-cell movement proteins to the putative CRSV RNA-2-encoded movement protein suggests that even though no primary amino acid sequence similarity exists, the movement protein polypeptides are possibly similar in structure and function.

Received 9 March 1992; accepted 3 June 1992.


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T. L. Sit, P. R. Haikal, A. S. Callaway, and S. A. Lommel
A Single Amino Acid Mutation in the Carnation Ringspot Virus Capsid Protein Allows Virion Formation but Prevents Systemic Infection
J. Virol., October 1, 2001; 75(19): 9538 - 9542.
[Abstract] [Full Text] [PDF]


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T. L. Sit, A. A. Vaewhongs, and S. A. Lommel
RNA-Mediated Trans-Activation of Transcription from a Viral RNA
Science, August 7, 1998; 281(5378): 829 - 832.
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