Characterization of cDNA clones coding for muscle tropomyosin of the nematode Trichostrongylus colubriformis.
The host-protective antigen from detergent-solubilised extracts of the sheep intestinal helminth Trichostrongylus colubriformis has been identified as tropomyosin. Complementary DNA clones coding for T. colubriformis muscle tropomyosin have been isolated and characterised as the first step in obtaining recombinant protein to carry out more extensive vaccination trials. The clones represent an mRNA of 1544 bases, including a relatively long 5' untranslated sequence of 307 bases and a 3' non-coding region of 344 bases. The mRNA codes for a highly alpha-helical protein of 284 residues with a molecular weight of 33,000; characteristics typically observed for the muscle tropomyosins of higher organisms. The T. colubriformis protein has 58% sequence identity with rabbit and Drosophila melanogaster muscle tropomyosins, and the differences in the protein sequence are randomly distributed throughout the molecule. There is complete identity between the three sequences for the N-terminal 9 residues, the region believed to be essential for the polymerisation of tropomyosin molecules and for binding to actin and troponin.[1]References
- Characterization of cDNA clones coding for muscle tropomyosin of the nematode Trichostrongylus colubriformis. Frenkel, M.J., Savin, K.W., Bakker, R.E., Ward, C.W. Mol. Biochem. Parasitol. (1989) [Pubmed]
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