Immunologic control of a parasitic arthropod. Identification of a protective antigen from Boophilus microplus

• Published in: The Journal of immunology (1950) Vol. 143; no. 4; pp. 1346 - 1351
• Main Authors: Willadsen, P, Riding, GA, McKenna, RV, Kemp, DH, Tellam, RL, Nielsen, JN, Lahnstein, J, Cobon, GS, Gough, JM
• Format: Journal Article
• Language: English
• Published: United States Am Assoc Immnol 15.08.1989
• Subjects: Acari; Amino Acid Sequence; Animals; Antigens - administration & dosage; Antigens - immunology; Antigens - isolation & purification; Cattle; Cattle Diseases - immunology; Cattle Diseases - parasitology; Cattle Diseases - prevention & control; Female; Immune Sera - pharmacology; Ixodidae; Molecular Sequence Data; Peptide Fragments - administration & dosage; Peptide Fragments - immunology; Peptide Fragments - isolation & purification; Tick Control - methods; Tick Infestations - immunology; Tick Infestations - prevention & control; Tick Infestations - veterinary; Vaccines - immunology
• ISSN: 0022-1767; 1550-6606
• DOI: 10.4049/jimmunol.143.4.1346

Cattle can be vaccinated against the tick Boophilus microplus by inducing an immunologic reaction against Ag in the tick gut. The uptake of antibody during feeding leads to severe damage to the parasite. One of the responsible tick gut Ag has now been purified and characterized: the Bm86 Ag. It is a membrane-bound glycoprotein present in very low abundance in extracts of partially engorged adult female ticks. It has an apparent m.w. of 89,000, an isoelectric point of 5.1 to 5.6 and an affinity for wheat germ lectin. Microgram amounts of this Ag are able to induce effective protection in cattle against the parasite, as shown by the decreased survival of ticks on vaccinated cattle and a reduction in engorgement weights and egg laying capacity of the survivors. Antisera to the Ag react with the surface of digest cells in the tick gut. As a result of the reaction with antibody, the endocytotic activity of these cells, which is a critical step in bloodmeal digestion in this tick, is strongly and rapidly inhibited. A number of peptides from this Ag, produced by digestion of the reduced and alkylated protein with endoproteinase lys-C, have been sequenced. One peptide has significant amino acid sequence homology with the epidermal growth factor precursor and a second peptide has homology with a putative protective antigen from Plasmodium falciparum.