| Autor: |
Bastos RG; Department of Veterinary Microbiology and Pathology, College of Veterinary Medicine, Washington State University, Pullman, WA 99164, USA., Thekkiniath J; Fuller Laboratories, 1312 East Valencia Drive, Fullerton, CA 92831, USA., Ben Mamoun C; Section of Infectious Diseases, Department of Internal Medicine, Yale School of Medicine, New Haven, CT 06520, USA., Fuller L; Fuller Laboratories, 1312 East Valencia Drive, Fullerton, CA 92831, USA., Molestina RE; Protistology Laboratory, American Type Culture Collection, Manassas, VA 10801, USA., Florin-Christensen M; Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Buenos Aires C1033AAJ, Argentina.; Instituto de Patobiología Veterinaria, CICVyA, INTA-Castelar, Hurlingham, Buenos Aires C1033AAE, Argentina., Schnittger L; Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Buenos Aires C1033AAJ, Argentina.; Instituto de Patobiología Veterinaria, CICVyA, INTA-Castelar, Hurlingham, Buenos Aires C1033AAE, Argentina., Alzan HF; Department of Veterinary Microbiology and Pathology, College of Veterinary Medicine, Washington State University, Pullman, WA 99164, USA.; Parasitology and Animal Diseases Department, National Research Center, Dokki, Giza 12622, Egypt.; Tick and Tick-Borne Disease Research Unit, National Research Center, Dokki, Giza 12622, Egypt., Suarez CE; Department of Veterinary Microbiology and Pathology, College of Veterinary Medicine, Washington State University, Pullman, WA 99164, USA.; Animal Disease Research Unit, United States Department of Agricultural-Agricultural Research Service, Pullman, WA 99164, USA. |
| Abstrakt: |
Babesia , Cytauxzoon and Theileria are tick-borne apicomplexan parasites of the order Piroplasmida, responsible for diseases in humans and animals. Members of the piroplasmid rhoptry-associated protein-1 (pRAP-1) family have a signature cysteine-rich domain and are important for parasite development. We propose that the closely linked B. microti genes annotated as BMR1_03g00947 and BMR1_03g00960 encode two paralogue pRAP-1-like proteins named BmIPA48 and Bm960. The two genes are tandemly arranged head to tail, highly expressed in blood stage parasites, syntenic to rap-1 genes of other piroplasmids, and share large portions of an almost identical ~225 bp sequence located in their 5' putative regulatory regions. BmIPA48 and Bm960 proteins contain a N-terminal signal peptide, share very low sequence identity (<13%) with pRAP-1 from other species, and harbor one or more transmembrane domains. Diversification of the piroplasmid-confined prap-1 family is characterized by amplification of genes, protein domains, and a high sequence polymorphism. This suggests a functional involvement of pRAP-1 at the parasite-host interface, possibly in parasite adhesion, attachment, and/or evasion of the host immune defenses. Both BmIPA48 and Bm960 are recognized by antibodies in sera from humans infected with B. microti and might be promising candidates for developing novel serodiagnosis and vaccines. |
