Key result
Erysimum latent tymovirus virion protein has 11 extra N-terminal amino acids linked to distant serological relationships.
Why the study?
The amino acid sequence and structure of the virion protein gene of erysimum latent tymovirus had not been determined and compared to other tymoviruses.
Answers are grounded in this paper and cite their sources.
The study determines the primary structure of the ELV virion protein, confirming its distant relationship to other tymoviruses.
The nucleotide sequence of the virion protein (VP) gene of erysimum latent tymovirus (ELV) has been determined and the amino acid sequence of the VP deduced and confirmed by peptide analysis. The ELV VP is larger than the VPs of other tymoviruses because it has, unexpectedly, 11 more amino acid residues at its N terminus. The amino acid sequences of the VPs of ELV and four other tymoviruses align unequivocally and their relationships, as assessed from the percentage of identical residues, correlate well with previously reported serological tests which have shown ELV to be distant from other tymoviruses.
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Srifah et al. (1990) studied Erysimum latent tymovirus. Nucleotide sequencing and peptide analysis vs. Other tymoviruses was evaluated on Nucleotide and amino acid sequence of the virion protein gene. The erysimum latent tymovirus virion protein has 11 more amino acid residues at its N terminus compared to other tymoviruses, correlating with its distant serological relationship.
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