الفهرس 
Nomenclature and classifications of Canine babesiosis.Only 14 pages are availabe for public view
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Abstract
Identification and molecular characterization of Babesia gibsoni proteins with potential antigenic properties are crucial for the development and validation of the serodiagnostic method. In this study, we isolated a cDNA clone consists of an ORF of 1,995 bp encoding 664 amino acid residues encoding a novel B. gibsoni 76-kDa protein by immunoscreening of the parasite cDNA library. The translated BgGARP contained a glutamic acid-rich region profile at amino acid residues (174-583 aa) in the C-terminal, therefore, the protein was designated as Babesia gibsoni glutamic acid-rich protein (BgGARP). A BLASTp analysis of the translated BgGARP polypeptide demonstrated that the peptide shared shared 35.4% and 27.4% degree of identity with B. bigemina P200 (GenBank: AAF63787.1) and B. bovis P200 (GenBank: XP_001608924.1) proteins, respectively. The translated BgGARP revealed high hydrophilicity with a good antigenicity index. Analysis of the probability that the sequence will adopt a coiled-coil conformation revealed that BgGARP contained a coiled-coil domain at amino acid residues (181-452 aa).
A truncated BgGARP cDNA (BgGARPt) of 342 bp encoding a predicted 13-kDa peptide was expressed in Escherichia coli (E. coli). Six 6-week-old female ICR mice (Clea, Japan) were intraperitoneally immunized with 100 μg of purified rBgGARPt emulsified with an equal volume of complete Freund’s adjuvant (Difco Laboratories, USA).