Cloning and expression of a protective antigen from the cattle tick Boophilus microplus.

We report here the isolation and characterization of a cDNA that encodes Bm86

K. N. Rand; T. Moore; A. Sriskantha; K. Spring; R. Tellam; P. Willadsen; G. S. Cobon

2006

Scholarcy highlights

  • Glycoproteins located on the luminal surface of the plasma membrane of tick gut epithelial cells, when used to vaccinate cattle, are capable of stimulating an immune response that protects cattle against subsequent tick infestation
  • All of the peptide sequences used for designing probes as well as the other sequences determined from the endoproteinase Lys-C peptide fragments can be identified
  • The sequence Ser-Gly-Ser at amino acid positions 235-237 is different from that determined by peptide sequencing
  • In epidermal growth factor, 5 amino acids precede the first cysteine and there are 11 after the sixth, but we show only the sequence between the cysteine residues in Fig. 2 because it cannot be predicted where the regions begin and end in the Bm86 sequence
  • Because the strongest feature of EGF-like regions is the conservation of the cysteine residues, we considered that a mutation could have occurred at some stage in the construction of the cDNA library
  • At amino acid position 507, the asterisk highlights the phenylalanine identified from the sequence of the first Bm86 cDNA clone that is predicted as a cysteine from the sequence of a second cDNA isolated from a separate library
  • These results demonstrate that protective epitopes are present in the protein portion of Bm86, and we are confident that it will be possible to produce an effective recombinant anti-tick vaccine

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