NDLI: A novel Babesia orientalis 135-kilodalton spherical body protein like: identification of its secretion into cytoplasm of infected erythrocytes

Content Provider	Springer Nature : BioMed Central
Author	Guo, Jiaying Hu, Jinfang Sun, Yali Yu, Long He, Junwei He, Pei Nie, Zheng Li, Muxiao Zhan, Xueyan Zhao, Yangnan Luo, Xiaoying Liu, Junlong He, Lan Zhao, Junlong
Abstract	Background The spherical body is a distinct organelle only existing in Babesia and Theileria. Spherical body proteins (SBPs) are secreted from spherical bodies and incorporated into the cytoplasm of infected erythrocytes during invasion and post-invasion stages. Four different SBP homologues (SBP1, SBP2, SBP3 and SBP4) have been identified in Babesia bovis and Babesia bigemina. So far, there has been no report available about the identification of SBPs in Babesia orientalis. Methods The SBP3-like in B. orientalis (BoSBP3-like) was cloned, sequenced, characterized and compared to the SBP3 sequences of B. bovis and B. bigemina by bioinformatics analyses. The BoSBP3-like gene was truncated into three fragments: BoSBP3-like-1 (915 bp), BoSBP3-like-2 (1311 bp) and BoSBP3-like-3 (1011 bp), which were amplified and cloned into the expression vector pET-28a and expressed as three truncated recombinant (His-fusion) proteins. The immunogenicity, native forms and localization of BoSBP3-like were identified by western blot and indirect immunofluorescence assay (IFA). Results The BoSBP3-like gene was intronless with an open reading frame (ORF) of 3237 bp, encoded a 1079 amino acid polypeptide with a predicted size of 135 kDa, and contained a cysteine-rich region, three dispersing FAINT domains and a signal peptide (1–16 aa) at the N-terminus. The amino acid sequence of BoSBP3-like was 61.6 and 35.0% identical to that of B. bovis and B. bigemina, respectively. BoSBP3-like was identified as 135 kDa in the parasite lysate by rabbit antiserum against the truncated recombinant BoSBP3-like-1 (rBoSBP3-like-1). Three specific bands corresponding to rBoSBP3-like-1 (1–305 aa, 43 kDa), rBoSBP3-like-2 (306–742 aa, 58 kDa) and rBoSBP3-like-3 (743–1079 aa, 52 kDa) were detected by reaction with serum from B. orientalis-infected buffalo. The BoSBP3-like was not only localized in the spherical body of B. orientalis but also in the cytoplasm of infected erythrocytes of buffalo as puncta-like protein specks at both single and paired parasite development stages. Conclusions Through secretion into the cytoplasm of infected erythrocytes, BoSBP3-like may play a significant role in adaptation, interaction, and modification related to the host environment to benefit the growth and survival of Babesia. BoSBP3-like could react with the serum from B. orientalis-infected buffalo, but not healthy buffalo, implicating that BoSBP3-like is highly antigenic and may serve as a candidate diagnostic antigen for the detection of B. orientalis.
Related Links	https://parasitesandvectors.biomedcentral.com/counter/pdf/10.1186/s13071-018-2795-7.pdf
Ending Page	10
Page Count	10
Starting Page	1
File Format	HTM / HTML
ISSN	17563305
DOI	10.1186/s13071-018-2795-7
Journal	Parasites & Vectors
Issue Number	1
Volume Number	11
Language	English
Publisher	BioMed Central
Publisher Date	2018-03-27
Access Restriction	Open
Subject Keyword	Parasitology Entomology Tropical Medicine Infectious Diseases Veterinary Medicine Veterinary Science Virology Babesia orientalis Spherical body protein Erythrocyte Localization Cytoplasm 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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