NDLI: Characterization of a novel secretory spherical body protein in Babesia orientalis and Babesia orientalis-infected erythrocytes

Content Provider	Springer Nature : BioMed Central
Author	Guo, Jiaying Li, Muxiao Sun, Yali Yu, Long He, Pei Nie, Zheng Zhan, Xueyan Zhao, Yangnan Luo, Xiaoying Wang, Sen Aoyang, Siqi Liu, Qin Huang, Cuiqin He, Lan Zhao, Junlong
Abstract	Background The spherical body, a membrane bound organelle localized in the apical organelle complex, is unique to Babesia and Theileria spp. The spherical body proteins (SBPs) secreted by spherical bodies include SBP1, SBP2, SBP3 and SBP4. Up to now, only SBP3 has been characterized in Babesia orientalis. Methods The BoSBP4 gene was amplified from cDNA and gDNA and cloned into the pGEX-6P-1 vector by homologous recombination, sequenced and analyzed by bioinformatics tools. The amino acid (aa) sequence of BoSBP4 was compared with that of Babesia bovis and Babesia bigemina as well as SBP3 of B. orientalis. The immunoreactivity was evaluated by incubating recombinant BoSBP4 (rBoSBP4) with the serum of B. orientalis-infected water buffalo. The native form of BoSBP4 was identified by incubating lysate of B. orientalis-infected water buffalo erythrocytes with the anti-rBoSBP4 mouse serum. The cellular localization of BoSBP4 was determined by indirect immunofluorescence assay. Results The full length of the BoSBP4 gene was estimated to be 945 bp without introns, encoding a 314 aa polypeptide with a predicted molecular weight of 37 kDa. The truncated recombinant protein was expressed from 70 to 945 bp as a GST fusion protein with a practical molecular weight of 70 kDa. BoSBP4 shared a 40% and 30% identity with B. bovis and B. bigemina, respectively. Furthermore, it was 31% identical to SBP3 of B. orientalis. BoSBP4 was identified in the lysate of B. orientalis-infected water buffalo erythrocytes with a molecular weight of 37 kDa, corresponding to the expected molecular mass of BoSBP4. The result of rBoSBP4 with positive serum revealed that BoSBP4 can elicit an immune response to B. orientalis-infected water buffalo. The cellular localization of BoSBP4 was detected to be adjacent to the merozoite nucleus in the intracellular phase, followed by the diffusion of the fluorescence of BoSBP4 into the cytoplasm of B. orientalis-infected erythrocytes as puncta-like specks and a gradual increase of the fluorescence. Conclusions In this study, SBP4 in B. orientalis was characterized for the first time. It may play a key role in interaction with the host cell by being secreted into the cytoplasm of the B. orientalis-infected erythrocytes to facilitate parasite growth and reproduction.
Related Links	https://parasitesandvectors.biomedcentral.com/counter/pdf/10.1186/s13071-018-3018-y.pdf
Ending Page	11
Page Count	11
Starting Page	1
File Format	HTM / HTML
ISSN	17563305
DOI	10.1186/s13071-018-3018-y
Journal	Parasites & Vectors
Issue Number	1
Volume Number	11
Language	English
Publisher	BioMed Central
Publisher Date	2018-07-25
Access Restriction	Open
Subject Keyword	Parasitology Entomology Tropical Medicine Infectious Diseases Veterinary Medicine Veterinary Science Virology Babesia orientalis Spherical body Apical organelle complex Native form Immunoreactivity Cellular localization Veterinary Medicine/Veterinary Science
Content Type	Text
Resource Type	Article
Subject	Veterinary Infectious Diseases Parasitology
Journal Impact Factor	3/2023
5-Year Journal Impact Factor	3.3/2023

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