ArticlePloS one2015
Essential Role for an M17 Leucine Aminopeptidase in Encystation of Acanthamoeba castellanii.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 34 citations in OpenAlex.
- New Viability Assays for Acanthamoeba castellanii Trophozoites and Cysts Allow Rapid Assessment of Drug Activity.The Journal of infectious diseases · 2026Article
- High-efficiency transfection of Acanthamoeba castellanii using a cationic polymer.Cell reports methods · 2026Article
- Aminopeptidase M17 in bacteria: insights into structure, function, and potential as a drug target.Journal of bacteriology · 2026Review
- Encystment and Excystment Processes inPathogens (Basel, Switzerland) · 2025Review
- Phylogenomic, structural, and cell biological analyses reveal thatMicrobiology spectrum · 2024Article
- Identification of a potent and selective LAPTc inhibitor by RapidFire-Mass Spectrometry, with antichagasic activity.PLoS neglected tropical diseases · 2024Article
- Ubenimex combined with Albendazole for the treatment ofFrontiers in veterinary science · 2024Article
- Antiamoebic Activity of Imidazothiazole Derivatives against Opportunistic PathogenAntibiotics (Basel, Switzerland) · 2022Article
- Sirtinol Supresses Trophozoites Proliferation and Encystation of Acanthamoeba via Inhibition of Sirtuin Family Protein.The Korean journal of parasitology · 2022Article
- Anti-PeerJ · 2022Article
- Using microbial metalo-aminopeptidases as targets in human infectious diseases.Microbial cell (Graz, Austria) · 2021Review
- A Novel Cysteine Protease Inhibitor ofPathogens (Basel, Switzerland) · 2021Article
- In vitro activity of Camellia sinensis (green tea) against trophozoites and cysts of Acanthamoeba castellanii.International journal for parasitology. Drugs and drug resistance · 2020Article
- The role of the Acanthamoeba castellanii Sir2-like protein in the growth and encystation of Acanthamoeba.Parasites & vectors · 2020Article
- The Biochemical and Functional Characterization of M28 Aminopeptidase Protein Secreted byMolecules (Basel, Switzerland) · 2019Article
- Screening and verification for proteins that interact with leucine aminopeptidase of Taenia pisiformis using a yeast two-hybrid system.Parasitology research · 2019Article
- Quantitative proteomic analysis and functional characterization of Acanthamoeba castellanii exosome-like vesicles.Parasites & vectors · 2019Article
- Expression, Tissue Localization and Serodiagnostic Potential of Echinococcus granulosus Leucine Aminopeptidase.International journal of molecular sciences · 2018Article
- Pathogenic Acanthamoeba castellanii Secretes the Extracellular Aminopeptidase M20/M25/M40 Family Protein to Target Cells for Phagocytosis by Disruption.Molecules (Basel, Switzerland) · 2017Article
- A leucine aminopeptidase is involved in kinetoplast DNA segregation in Trypanosoma brucei.PLoS pathogens · 2017Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Encystation of Acanthamoeba leads to the formation of resilient cysts from vegetative trophozoites. This process is essential for parasite survival under unfavorable conditions such as starvation, low temperatures, and exposure to biocides. During encystation, a massive turnover of intracellular components occurs, and a large number of organelles and proteins are degraded by proteases. Previous studies with specific protease inhibitors have shown that cysteine and serine proteases are involved in encystation of Acanthamoeba, but little is known about the role of metalloproteases in this process. Here, we have biochemically characterized an M17 leucine aminopeptidase of Acanthamoeba castellanii (AcLAP) and analyzed its functional involvement in encystation of the parasite. Recombinant AcLAP shared biochemical properties such as optimal pH, requirement of divalent metal ions for activity, substrate specificity for Leu, and inhibition profile by aminopeptidase inhibitors and metal chelators with other characterized M17 family LAPs. AcLAP was highly expressed at a late stage of encystation and mainly localized in the cytoplasm of A. castellanii. Knockdown of AcLAP using small interfering RNA induced a decrease of LAP activity during encystation, a reduction of mature cyst formation, and the formation of abnormal cyst walls. In summary, these results indicate that AcLAP is a typical M17 family enzyme that plays an essential role during encystation of Acanthamoeba.
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