MOLECULAR VARIATION AND DIVERSITY IN CANDIDATE VACCINE ANTIGENS FROM BABESIA

Recombinant vaccines are being developed against a number of species of protozoan parasites in the genus Babesia. Protozoan parasites are notorious for their diversity of strains and their ability to express families of equivalent, but antigenically distinct, surface proteins. In order to reduce the likelihood of evasion of the immune response induced by a recombinant vaccine, ideal components should be essential proteins encoded by single copy genes. The proteins should also have a limited ability to tolerate polymorphism in amino acid sequence, especially in critical epitopes. While little is known about the function of the candidate protective antigens, there is now considerable information concerning the variation of a number of candidate vaccine antigens from several species of Babesia. Four of the well studied antigens are all members of multi-gene families. The members of the VMSA gene family of Babesia bovis are also highly polymorphic in sequence. The members of the Bv60/p58 family of rhoptry protein homologues exhibit more limited polymorphism within a single species of Babesia. However, comparison of the sequences of the equivalent proteins and the organisation of the corresponding genes from B. bovis, Babesia bigemina, Babesia canis and Babesia ovis suggests that members of this family have the potential to acquire and to tolerate substantial polymorphism in amino acid sequence. The choice of protein, and particular region of the protein, suitable for incorporation in a recombinant vaccine may require extensive analysis of the genetic systems encoding the candidate antigens.