Archives of Virology

, Volume 123, Issue 3–4, pp 367–377 | Cite as

Nucleotide sequence of the 3′ terminal region of belladonna mottle virus-Iowa (renamed Physalis mottle virus) RNA and an analysis of the relationships of tymoviral coat proteins

  • A. N. K. Jacob
  • M. R. N. Murthy
  • H. S. Savithri
Original Papers


The 3′ terminal 1255nt sequence of Physalis mottle virus (PhMV) genomic RNA has been determined from a set of overlapping cDNA clones. The open reading frame (ORF) at the 3′ terminus corresponds to the amino acid sequence of the coat protein (CP) determined earlier except for the absence of the dipeptide, Lys-Leu, at position 110–111. In addition, the sequence upstream of the CP gene contains the message coding for 178 amino acid residues of the C-terminus of the putative replicase protein (RP). The sequence downstream of the CP gene contains an untranslated region whose terminal 80 nucleotides can be folded into a characteristic tRNA-like structure. A phylogenetic tree constructed after aligning separately the sequence of the CP, the replicase protein (RP) and the tRNA-like structure determined in this study with the corresponding sequences of other tymoviruses shows that PhMV wrongly named belladonna mottle virus [BDMV(I)] is a separate tymovirus and not another strain of BDMV(E) as originally envisaged. The phylogenetic tree in all the three cases is identical showing that any subset of genomic sequence of sufficient length can be used for establishing evolutionary relationships among tymoviruses.


Nucleotide Amino Acid Sequence Nucleotide Sequence Phylogenetic Tree Amino Acid Residue 
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Copyright information

© Springer-Verlag 1992

Authors and Affiliations

  • A. N. K. Jacob
    • 1
  • M. R. N. Murthy
    • 2
  • H. S. Savithri
    • 1
  1. 1.Department of BiochemistryIndian Institute of ScienceBangaloreIndia
  2. 2.Department of Molecular BiophysicsIndian Institute of ScienceBangaloreIndia

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