ArticleBMC microbiology2006
Identification and properties of proteases from an Acanthamoeba isolate capable of producing granulomatous encephalitis.
Article in BMC microbiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 74 citations in OpenAlex.
- Experimental Granulomatous Amebic Encephalitis Caused byTropical medicine and infectious disease · 2024Article
- Epidemiology of and Genetic Factors Associated withPathogens (Basel, Switzerland) · 2024Review
- Proteases of Acanthamoeba.Parasitology research · 2023Review
- Extracellular Vesicles Secreted byMicroorganisms · 2023Article
- Biological characteristics and pathogenicity ofFrontiers in microbiology · 2023Review
- Article
- Various brain-eating amoebae: the protozoa, the pathogenesis, and the disease.Frontiers of medicine · 2021Review
- Article
- A Surviving Case of Acanthamoeba Granulomatous Amebic Encephalitis in a Hematopoietic Stem Cell Transplant Recipient.The American journal of case reports · 2020Article
- Extracellular protease profile of Acanthamoeba after prolonged axenic culture and after interaction with MDCK cells.Parasitology research · 2020Article
- Review
- Characterization of extracellular proteases of Acanthamoeba genotype T4 isolated from different sources in Iran.Parasitology research · 2017Article
- Essential Role for an M17 Leucine Aminopeptidase in Encystation of Acanthamoeba castellanii.PloS one · 2015Article
- Acanthamoeba protease activity promotes allergic airway inflammation via protease-activated receptor 2.PloS one · 2014Article
- Amoebic forms of Blastocystis spp. - evidence for a pathogenic role.Parasites & vectors · 2013Article
- Morpho-Physiological and Biochemical Criteria of Acanthamoeba spp. Isolated from the Egyptian Aquatic Environment.Iranian journal of parasitology · 2013Article
- Proteases from Entamoeba spp. and Pathogenic Free-Living Amoebae as Virulence Factors.Journal of tropical medicine · 2013Article
- Host-parasite interaction: parasite-derived and -induced proteases that degrade human extracellular matrix.Journal of parasitology research · 2012Article
- Acanthamoeba culbertsoni elicits soluble factors that exert anti-microglial cell activity.Infection and immunity · 2010Article
- Identification, purification, and characterization of a secretory serine protease in an Indian strain of Leishmania donovani.Molecular and cellular biochemistry · 2009Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundGranulomatous amoebic encephalitis due to Acanthamoeba is often a fatal human disease. However, the pathogenesis and pathophysiology of Acanthamoeba encephalitis remain unclear. In this study, the role of extracellular Acanthamoeba proteases in central nervous system pathogenesis and pathophysiology was examined.
resultsUsing an encephalitis isolate belonging to T1 genotype, we observed two major proteases with approximate molecular weights of 150 KD and 130 KD on SDS-PAGE gels using gelatin as substrate. The 130 KD protease was inhibited with phenylmethylsulfonyl fluoride (PMSF) suggesting that it is a serine protease, while the 150 KD protease was inhibited with 1, 10-phenanthroline suggesting that it is a metalloprotease. Both proteases exhibited maximal activity at neutral pH and over a range of temperatures, indicating their physiological relevance. These proteases degrade extracellular matrix (ECM), which provide structural and functional support to the brain tissue, as shown by the degradation of collagen I and III (major components of collagenous ECM), elastin (elastic fibrils of ECM), plasminogen (involved in proteolytic degradation of ECM), as well as casein and haemoglobin. The proteases were purified partially using ion-exchange chromatography and their effects were tested in an in vitro model of the blood-brain barrier using human brain microvascular endothelial cells (HBMEC). Neither the serine nor the metalloprotease exhibited HBMEC cytotoxicity. However, the serine protease exhibited HBMEC monolayer disruptions (trypsin-like) suggesting a role in blood-brain barrier perturbations.
conclusionOverall, these data suggest that Acanthamoeba proteases digest ECM, which may play crucial role(s) in invasion of the brain tissue by amoebae.
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