Kinetic Characterization and Inhibitor Screening of Pyruvate Kinase I From .

The apicomplexan is a main pathogenic parasite causing human babesiosis, which is one of the most widely distributed tick-borne diseases in humans. Pyruvate kinase (PYK) plays a central metabolic regulatory role in most living organisms and catalyzes the essentially irreversible step in glycolysis that converts phosphoenolpyruvate (PEP) to pyruvate. Hence, PYK is recognized as an attractive therapeutic target in cancer and human pathogens such as apicomplexans.

Recombinase polymerase amplification lateral flow dipstick (RPA-LF) detection of Babesia orientalis in water buffalo (Bubalus babalis, Linnaeus, 1758).

Babesiosis caused by Babesia orientalis, an intraerythrocytic apicomplexan protozoan, is one of the most important diseases for water buffalo in central and southern China, leading to huge economic losses, and its main diagnostic method is microscopic examination. In this study, a recombinase polymerase amplification - lateral flow dipstick (RPA-LF) assay, targeting the mitochondrial COXI gene of B. orientalis, was developed to detect B.

Erythrocyte Adhesion of Merozoite Surface Antigen 2c1 Expressed During Extracellular Stages of .

, a major infectious agent of water buffalo hemolytic babesiosis, is transmitted by . However, no effective vaccine is available. Essential antigens that are involved in parasite invasion of host red blood cells (RBCs) are potential vaccine candidates.

Recombinase polymerase amplification with lateral flow strip for detecting Babesia microti infections.

Babesia microti is one of the most important pathogens causing humans and rodents babesiosis-an emerging tick-borne disease that occurs worldwide. At present, the gold standard for the detection of Babesia is the microscopic examination of blood smears, but this diagnostic test has several limitations. The recombinase polymerase amplification with lateral flow (LF-RPA) assay targeting the mitochondrial cytochrome oxidase subunit I (cox I) gene of B.

Characterization of the variable merozoite surface antigen (VMSA) gene family of Babesia orientalis.

Due to its wide presence in apicomplexan parasites as well as high polymorphism and antigenic diversity, the variable merozoite surface antigen (VMSA) family in Babesia sp. has attracted increasing attention of researchers. Here, all the reported VMSA genes of Babesia spp.

Identifying the Naphthalene-Based Compound 3,5-Dihydroxy 2-Napthoic Acid as a Novel Lead Compound for Designing Lactate Dehydrogenase-Specific Antibabesial Drug.

Human babesiosis is caused by apicomplexan parasites, including , , sp. MOI, , , and . Among them, is the most common cause of human and rodent babesiosis.

Surface Antigen 1 Is a Crucial Secreted Protein That Mediates Invasion Into Host Cells.

, a tick-borne intraerythrocytic zoonotic protozoan, causes most of human babesiosis in the world, and patients usually experience intermittent fever, fatigue, and chills, followed by a combination of additional symptoms and even death in severe cases. Unfortunately, there is no curable drug or effective vaccine available, and the mechanism of related virulence factors in invasion to host cells during the merozoite stage is unclear. Here, we evaluated a secreted protein annotated as surface antigen 1 (BmSA1) and identified from culture supernatant by liquid chromatography coupled with tandem mass spectrometry (LC-MS/MS).

Evaluation of GPI-anchored Protein 47 (BgGPI47-WH) as a Potential Diagnostic Antigen by Enzyme-Linked Immunosorbent Assay.

is one of the important pathogens causing severe incurable canine babesiosis, suggesting the necessity to develop a sensitive, specific, and highly automated diagnostic method for clinical application. Surface proteins are ideal candidates for diagnostic targets because they are the primary targets for host immune responses during host-parasite interactions. Glycosylphosphatidylinositol (GPI)-anchored proteins are abundant on the surface of parasites and play an important role in parasite diagnosis.

Crystal structures of lactate dehydrogenase BmLDH reveal a critical role for Arg99 in catalysis.

The tick- and transfusion-transmitted human pathogen infects host erythrocytes to cause the pathologic symptoms associated with human babesiosis, an emerging disease with worldwide distribution and potentially fatal clinical outcome. Drugs currently recommended for the treatment of babesiosis are associated with a high failure rate and significant adverse events, highlighting the urgent need for more-effective and safer babesiosis therapies. Unlike other apicomplexan parasites, lacks a canonical lactate dehydrogenase (LDH) but instead expresses a unique enzyme, LDH (BmLDH), acquired through evolution by horizontal transfer from a mammalian host.

Identification of a novel thrombospondin-related anonymous protein (BoTRAP2) from Babesia orientalis.

Background: The 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.

Methods: The functional domain of TRAP2 in B.

Identification and molecular characterization of a novel Babesia orientalis thrombospondin-related anonymous protein (BoTRAP1).

Background: The 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.

Methods: The 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.

Detection of Babesia gibsoni in dogs by combining recombinase polymerase amplification (RPA) with lateral flow (LF) dipstick.

Babesia gibsoni is a protozoan parasite responsible for the majority of reported cases of canine babesiosis in China. Currently, microscopic examination of the Giemsa-stained thin blood smears is the main diagnosis method in clinic. Here, we report the recombinase polymerase amplification-lateral flow (LF-RPA) dipstick detection method for targeting B.

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

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.

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

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.