NDLI: Screening and identification of Theileria annulata subtelomere-encoded variable secreted protein-950454 (SVSP454) interacting proteins from bovine B cells

Content Provider	Springer Nature : BioMed Central
Author	Li, Zhi Liu, Junlong Ma, Quanying Liu, Aihong Li, Youquan Guan, Guiquan Luo, Jianxun Yin, Hong
Abstract	Background Theileria annulata is a protozoan parasite that can infect and transform bovine B cells, macrophages, and dendritic cells. The mechanism of the transformation is still not well understood, and some parasite molecules have been identified, which contribute to cell proliferation by regulating host signaling pathways. Subtelomeric variable secreted proteins (SVSPs) of Theileria might affect the host cell phenotype, but its function is still not clear. Therefore, in the present study, we explored the interactions of SVSP454 with host cell proteins to investigate the molecular mechanism of T. annulata interaction with host cells. Methods The transcription level of an SVSP protein from T. annulata, SVSP454, was analyzed between different life stages and transformed cell passages using qRT-PCR. Then, SVSP454 was used as a bait to screen its interacting proteins from the bovine B cell cDNA library using a yeast two-hybrid (Y2H) system. The potential interacting proteins of host cells with SVSP454 were further identified by using a coimmunoprecipitation (Co-IP) and bimolecular fluorescence complementation (BiFC) assays. Results SVSP454 was transcribed in all three life stages of T. annulata but had the highest transcription during the schizont stage. However, the transcription level of SVSP454 continuously decreased as the cultures passaged. Two proteins, Bos Taurus coiled-coil domain 181 (CCDC181) and Bos Taurus mitochondrial ribosomal protein L30 (MRPL30), were screened. The proteins CCDC181 and MRPL30 of the host were further identified to directly interact with SVSP454. Conclusion In the present study, SVSP454 was used as a bait plasmid, and its prey proteins CCDC181 and MRPL30 were screened out by using a Y2H system. Then, we demonstrated that SVSP454 directly interacted with both CCDC181 and MRPL30 by Co-IP and BiFC assays. Therefore, we speculate that SVSP454-CCDC181/SVSP454MRPL30 is an interacting axis that regulates the microtubule network and translation process of the host by some vital signaling molecules. Identification of the interaction of SVSP454 with CCDC181 and MRPL30 will help illustrate the transformation mechanisms induced by T. annulata. Graphic abstract
Related Links	https://parasitesandvectors.biomedcentral.com/counter/pdf/10.1186/s13071-021-04820-4.pdf
Ending Page	13
Page Count	13
Starting Page	1
File Format	HTM / HTML
ISSN	17563305
DOI	10.1186/s13071-021-04820-4
Journal	Parasites & Vectors
Issue Number	1
Volume Number	14
Language	English
Publisher	BioMed Central
Publisher Date	2021-06-11
Access Restriction	Open
Subject Keyword	Parasitology Entomology Tropical Medicine Infectious Diseases Veterinary Medicine Veterinary Science Virology Theileria annulata SVSP454 Yeast two-hybrid Co-IP BiFC CCDC181 MRPL30 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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