ArticleParasites & vectors2019
Identification of a novel thrombospondin-related anonymous protein (BoTRAP2) from Babesia orientalis.
Article in Parasites & vectors, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 10 citations in OpenAlex.
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- Status of selected biochemical and coagulation profiles and platelet count in malaria and malaria-Schistosoma mansoni co-infection among patients attending at Dembiya selected Health Institutions, Northwest Ethiopia.Scientific reports · 2024Article
- Characterization of anti-erythrocyte and anti-platelet antibodies in hemolytic anemia and thrombocytopenia induced byFrontiers in cellular and infection microbiology · 2023Article
- Thrombospondin-Related Anonymous Protein (TRAP) Family Expression byMicroorganisms · 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 variant erythrocyte surface antigen-1 (VESA1) in Babesia orientalis.Parasitology research · 2021Article
- Erythrocyte Adhesion of Merozoite Surface Antigen 2c1 Expressed During Extracellular Stages ofFrontiers in immunology · 2021Article
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Authors and funding
12 authors at 1 institution in 1 country.
Funding
Abstract
backgroundThe thrombospondin-related anonymous protein (TRAP) was first discovered in the sporozoite of Plasmodium falciparum and TRAP family proteins are secreted by micronemes and transported to the parasite surface to participate in the invasion process. Various TRAP proteins have been identified in apicomplexan protozoans, but there have been few reports about TRAP proteins in Babesia orientalis.
methodsThe functional domain of TRAP2 in B. orientalis was cloned, sequenced, characterized and compared to the TRAP sequences of related apicomplexan parasites. The functional domain of BoTRAP2 was truncated, named BoTRAP2-1, and then cloned into the pET-28a expression vector. Rabbit anti-rBoTRAP2-1 polyclonal antibody was produced by immunizing three rabbits. Western blot analysis was used to identify the native form and immunogenicity of BoTRAP2. The localization of BoTRAP2 was identified by indirect fluorescence assay (IFA).
resultsThe amplified genes of BoTRAP2 are 2817 bp in length, encoding a functional domain of about 938 aa with two vWFA domains, one TSP domain and one transmembrane domain. The amino acid sequence of BoTRAP2 has a high similarity with that of B. bovis and B. gibsoni. The predicted tertiary structure of truncated BoTRAP2-1 confirmed that BoTRAP2 contains two vWFA domains and a TSP domain, the main functional areas of the protein. The native BoTRAP2 was identified from B. orientalis lysate by using rabbit polyclonal anti-rBoTRAP2-1. A band corresponding to rBoTRAP2-1 was detected by reaction with serum from a B. orientalis-infected water buffalo, indicating that the protein has a high immunogenicity. IFA showed that BoTRAP2 is mainly localized on the apical end of parasites by rabbit anti-rBoTRAP2-1 polyclonal serum.
conclusionsThe rBoTRAP2 could differentiate serum from B. orientalis-infected water buffalo and normal water buffalo, implicating that BoTRAP2 has high immunogenicity and could serve as a candidate antigen for diagnosis of B. orientalis infection in buffalo.
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