ArticleParasitology research2019
Heterologous overexpression of active hexokinases from microsporidia Nosema bombycis and Nosema ceranae confirms their ability to phosphorylate host glucose.
Article in Parasitology research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 25 citations in OpenAlex.
- Rice-Fish Farming Improved Antioxidant Defences, Glucose Metabolism, and Muscle Nutrient ofMetabolites · 2024Article
- Functional characterization of Nosema bombycis (microsporidia) trehalase 3.Parasitology research · 2023Article
- Dynamic Interplay of Metabolic and Transcriptional Responses in Shrimp during Early and Late Infection Stages ofInternational journal of molecular sciences · 2023Article
- Molecular and biochemical changes in Locusta migratoria (Orthoptera: Acrididae) infected with Paranosema locustae.Journal of insect science (Online) · 2023Article
- Editorial: Genomic and evolutionary analysis of microsporidian parasites.Frontiers in microbiology · 2023Article
- Heterologous Expressed NbSWP12 from MicrosporidiaJournal of fungi (Basel, Switzerland) · 2022Article
- Review
- Nosema apis and N. ceranae Infection in Honey bees: A Model for Host-Pathogen Interactions in Insects.Experientia supplementum (2012) · 2022Article
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4 authors at 1 institution in 1 country.
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Abstract
The secretion of hexokinases (HKs) by microsporidia followed by their accumulation in insect host nuclei suggests that these enzymes play regulatory and catalytic roles in infected cells. To confirm whether HKs exert catalytic functions in insect cells, we expressed in E. coli the functionally active HKs of two entomopathogenic microsporidia, Nosema bombycis and Nosema ceranae, that cause silkworm and honey bee nosematoses. N. bombycis HK with C-terminal polyHis tag and N. ceranae enzyme with N-terminal polyHis tag were cloned into pOPE101 and pRSET vectors, respectively, and overexpressed. Specific activities of N. bombycis and N. ceranae enzymes isolated by metal chelate affinity chromatography were 29.2 ± 0.5 and 60.2 ± 1.2 U/mg protein at an optimal pH range of 8.5-9.5. The kinetic characteristics of the recombinant enzymes were similar to those of HKs from other parasitic and free-living organisms. N. bombycis HK demonstrated Km 0.07 ± 0.01 mM and k
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