ArticleParasitology research2014
Novel cathepsin B and cathepsin B-like cysteine protease of Naegleria fowleri excretory-secretory proteins and their biochemical properties.
Article in Parasitology research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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31 citing papers in PubMed, 49 citations in OpenAlex.
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- Understanding the pathogenicity of Naegleria fowleri in association with N. fowleri antigen-1 (Nfa1).Parasites, hosts and diseases · 2024Review
- Analysis of virulence factors in extracellular vesicles secreted by Naegleria fowleri.Parasitology research · 2024Article
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- Lactoferrin and Lysozyme Inhibit the Proteolytic Activity and Cytopathic Effect ofPathogens (Basel, Switzerland) · 2024Article
- Miconazole-like Scaffold is a Promising Lead forJournal of medicinal chemistry · 2023Article
- Roles of Cysteine Proteases in Biology and Pathogenesis of Parasites.Microorganisms · 2023Article
- Role of cathepsin B of Naegleria fowleri during primary amebic meningoencephalitis.Parasitology research · 2022Article
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- Comparative transcriptome profiling of virulent and avirulent isolates of Neoparamoeba perurans.Scientific reports · 2022Article
- Drug discovery for primary amebic meningoencephalitis: from screen to identification of leads.Expert review of anti-infective therapy · 2021Article
- Global transcriptome landscape of the rabbit protozoan parasite Eimeria stiedae.Parasites & vectors · 2021Article
- A Novel Cysteine Protease Inhibitor ofPathogens (Basel, Switzerland) · 2021Article
- Host-Parasite Interaction of Atlantic salmon (Frontiers in immunology · 2021Article
- HMG-CoA Reductase Inhibitors as Drug Leads againstACS chemical neuroscience · 2020Article
- Fowlerstefin, a cysteine protease inhibitor of Naegleria fowleri, induces inflammatory responses in BV-2 microglial cells in vitro.Parasites & vectors · 2020Article
- Nanopore sequencing improves the draft genome of the human pathogenic amoeba Naegleria fowleri.Scientific reports · 2019Article
- Review
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Naegleria fowleri causes a lethal primary amoebic meningoencephalitis (PAM) in humans and experimental animals, which leads to death within 7-14 days. Cysteine proteases of parasites play key roles in nutrient uptake, excystment/encystment, host tissue invasion, and immune evasion. In this study, we cloned N. fowleri cathepsin B (nfcpb) and cathepsin B-like (nfcpb-L) genes from our cDNA library of N. fowleri. The full-length sequences of genes were 1,038 and 939 bp (encoded 345 and 313 amino acids), and molecular weights were 38.4 and 34 kDa, respectively. Also, nfcpb and nfcpb-L showed a 56 and 46 % identity to Naegleria gruberi cathepsin B and cathepsin B-like enzyme, respectively. Recombinant NfCPB (rNfCPB) and NfCPB-L (rNfCPB-L) proteins were expressed by the pEX5-NT/TOPO vector that was transformed into Escherichia coli BL21, and they showed 38.4 and 34 kDa bands on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and Western blot analysis using their respective antibodies. Proteolytic activity of refolded rNfCPB and rNfCPB-L was maximum at a pH of 4.5, and the most effective substrate was Z-LR-MCA. rNfCPB and rNfCPB-L showed proteolytic activity for several proteins such as IgA, IgG, IgM, collagen, fibronectin, hemoglobin, and albumin. These results suggested that NfCPB and NfCPB-L cysteine protease are important components of the N. fowleri ESP, and they may play important roles in host tissue invasion and immune evasion as pathogens that cause N. fowleri PAM.
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