J Gen Virol
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J Gen Virol 72 (1991), 237-242; DOI 10.1099/0022-1317-72-2-237
© 1991 Society for General Microbiology
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Unexpected sequence diversity in the amino-terminal ends of the coat proteins of strains of sugarcane mosaic virus

M. J. Frenkel1, J. M. Jilka2,{dagger}, N. M. McKern1, P. M. Strike1, J. M. Clark, Jr.2, D. D. Shukla1 and C. W. Ward1

1 CSIRO, Division of Biomolecular Engineering, 343 Royal Parade, Parkville, Victoria 3052, Australia
and2 Biochemistry Department, University of Illinois, Urbana, Illinois 61801, U.S.A.

The sequence of the 3'-terminal 1343 nucleotides of the SC strain of the sugarcane mosaic virus (SCMV-SC) genome was compared with the 1376 nucleotides at the 3' terminus of maize dwarf mosaic virus B (MDMV-B). The SCMV-SC sequence includes an open reading frame which codes for the viral coat protein of 313 amino acids (nucleotides 157 to 1116), followed by a 3' non-coding region of 235 nucleotides and a poly(A) tail. The MDMV-B sequence codes for the capsid protein (nucleotides 157 to 1139) of 328 amino acids and has a 3' non-coding region of 236 nucleotides. The coat protein of SCMV-SC has 92% identity with that of MDMV-B except for the region between amino acid residues 27 and 70 of SCMV-SC. This region of SCMV-SC is smaller (44 residues) than the equivalent region in MDMV-B (59 residues) and has only 22% identity with the MDMV-B sequence. Possible mechanisms for the generation of this sequence diversity are discussed. Despite this diversity, the sequence identities of both the major part of the coat proteins and the 3' non-coding regions confirm the proposal, based on previously described serological data, that SCMV-SC and MDMV-B are strains of SCMV.

{dagger} Present address: Monsanto Company, St Louis, Missouri 63198, U.S.A.

Received 26 October 1990; accepted 30 October 1990.




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Copyright © 1991 by the Society for General Microbiology.