ArticleParasitology research2020
A cysteine protease of Babesia microti and its interaction with tick cystatins.
Article in Parasitology research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 9 citations in OpenAlex.
- Exploring the longitudinal expression dynamics of midguts in adult female Amblyomma americanum ticks.BMC genomics · 2024Article
- Exploring midgut expression dynamics: longitudinal transcriptomic analysis of adult femalebioRxiv : the preprint server for biology · 2024Article
- A longitudinal transcriptomic analysis of Rhipicephalus microplus midgut upon feeding.Ticks and tick-borne diseases · 2024Article
- Comparative Degradome Analysis of the Bovine Piroplasmid PathogensPathogens (Basel, Switzerland) · 2023Article
- Tick innate immune responses to hematophagy andFrontiers in immunology · 2023Article
- In Silico Survey and Characterization ofPathogens (Basel, Switzerland) · 2021Article
- Effect of protease inhibitors on the intraerythrocytic development of Babesia microti and Babesia duncani, the causative agents of human babesiosis.The Journal of eukaryotic microbiologyArticle
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Babesiosis is a tick-borne protozoonosis caused by Babesia, which can cause fever, hemolytic anemia, hemoglobinuria, and even death. Babesia microti is a parasite found in rodents and can be pathogenic to humans. In this study, the full-length cDNA of a B. microti cysteine protease (BmCYP) was expressed and the recombinant rBmCYP protein analyzed and characterized. BmCYP is encoded by an ORF of 1.3 kb, with a predicted molecular weight of 50 kDa and a theoretical pI of 8.5. The amino acid sequence of BmCYP exhibits an identity of 32.9 to 35.2% with cysteine proteases of Babesia ovis, Babesia bovis, and Theileria, respectively. The results of the proteinase assays show that rBmCYP has cysteine protease enzymatic activity. In addition, we demonstrate that tick cystatins rRhcyst-1 and rRhcyst-2 were able to effectively inhibit the activity of rBmCYP; the inhibition rates were 57.2% and 30.9%, respectively. Tick cystatins Rhcyst-1 and Rhcyst-2 were differentially expressed in ticks that fed on Babesia-infected mice relative to non-infected control ticks. Our results suggest that BmCYP is a functional enzyme with cysteine protease enzymatic activity and may be involved in tick-B. microti interactions.
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Registered trials
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