ArticleParasites & vectors2018
Identification and molecular characterization of a novel Babesia orientalis thrombospondin-related anonymous protein (BoTRAP1).
Article in Parasites & vectors, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 15 citations in OpenAlex.
- Changes in Paraoxonase-1 and Sialic Acid Levels due to Inflammatory and Oxidative Stress Response in Sheep Naturally Infected with Anaplasma spp.Acta parasitologica · 2026Article
- A conserved protein of Babesia microti elicits partial protection against Babesia and Plasmodium infection.Parasites & vectors · 2023Article
- Marine gregarine genomes reveal the breadth of apicomplexan diversity with a partially conserved glideosome machinery.BMC genomics · 2022Article
- Thrombospondin Related Anonymous Protein Superfamily in Vector-Borne Apicomplexans: The Parasite's Toolkit for Cell Invasion.Frontiers in cellular and infection microbiology · 2022Review
- Identification of a novel thrombospondin-related anonymous protein (BoTRAP2) from Babesia orientalis.Parasites & vectors · 2019Article
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14 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundThe thrombospondin-related anonymous protein (TRAP) family, a kind of transmembrane protein, is widely distributed with a conserved feature of structure in all apicomplexan parasites and plays a crucial role in the gliding motility and survival of parasites.
methodsThe Babesia orientalis TRAP1 gene (BoTRAP1) was truncated and cloned into a pET-42b expression vector and expressed as a GST-tag fusion protein with a TEV protease site. Rabbit anti-rBoTRAP1 antibody was produced and purified using a protein A chromatography column. Western blot analysis was performed to identify the native protein of BoTRAP1 and differentiate B. orientalis-infected positive from negative serum samples. The localization of BoTRAP1 on merozoites was identified by the indirect florescent antibody test (IFAT).
resultsThe partial sequence of the TRAP1 gene was cloned from B. orientalis cDNA and identified to contain a von Willebrand factor A (vWFA) region and a thrombospondin type-1 (TSP-1) domain; it had a length of 762 bp, encoding a polypeptide of 254 amino acid residues with a predicted size of 28.2 kDa. The partial sequence was cloned into a pET-42b expression vector and expressed in E. coli as a GST fusion protein. Western blot indicated that rBoTRAP1 has a high immunogenicity and can differentiate B. orientalis-infected positive and negative serum samples collected from water buffaloes. IFAT showed that BoTRAP1 is mainly localized on the apical end of intracellular parasites by using polyclonal antibodies (PcAb) against rBoTRAP1. Meanwhile, the PcAb test also identified the native BoTRAP1 as a ~65 kDa band from B. orientalis lysates. The predicted 3D structure of BoTRAP1 contains a metalion-dependent adhesion site (MIDAS), which could be important for interaction with ligand on the surface of the host cells.
conclusionsLike all known protozoa, B. orientalis has a TRAP family, comprising TRAP1, TRAP2, TRAP3 and TRAP4. The newly identified and characterized BoTRAP1 may play a key role in the invasion of B. orientalis into water buffalo erythrocytes.
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