Archives of Virology

, Volume 132, Issue 3–4, pp 399–408 | Cite as

Sequence diversity in the surface-exposed amino-terminal region of the coat proteins of seven strains of sugarcane mosaic virus correlates with their host range

  • X. W. Xiao
  • M. J. Frenkel
  • D. S. Teakle
  • C. W. Ward
  • D. D. Shukla
Original Papers


The N-terminal region of the coat proteins of five strains (Isis, Brisbane, Sabi, Bundaberg, and BC) of sugarcane mosaic virus (SCMV) isolated from four different plant species (sugarcane, sabi grass, wild sorghum, and blue couch grass) have been compared with the previously published data for SCMV-SC and SCMV-MDB, isolated from sugarcane and maize, respectively. The region, beginning at residue 11 and ending 16 residues beyond the second trypsin cleavage site of the coat protein, varied in size from 68 amino acid residues (Bundaberg) to 115 residues (BC) and contained repeat sequence motifs. Comparisons of the sequence identity and the nature of the repeats in the seven sequences showed that there were five different sequence patterns. These could be grouped further into three subsets which appeared to correlate with the host range of the strains. SCMV-Brisbane, SC, and Isis, isolated from sugarcane, showed almost identical sequence patterns and formed one subset. The other four strains had different sequence patterns and could be grouped further into a Sabi and Bundaberg subset (isolated from sabi grass), and a BC and MDB subset.


Plant Species Infectious Disease Trypsin Amino Acid Residue Sequence Diversity 
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Copyright information

© Springer-Verlag 1993

Authors and Affiliations

  • X. W. Xiao
    • 1
  • M. J. Frenkel
    • 1
  • D. S. Teakle
    • 2
  • C. W. Ward
    • 1
  • D. D. Shukla
    • 1
  1. 1.Division of Biomolecular EngineeringCSIROParkvilleAustralia
  2. 2.Department of MicrobiologyUniversity of QueenslandSt. Lucia, BrisbaneAustralia

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