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Molecules 2017, 22(12), 2263; https://doi.org/10.3390/molecules22122263

Pathogenic Acanthamoeba castellanii Secretes the Extracellular Aminopeptidase M20/M25/M40 Family Protein to Target Cells for Phagocytosis by Disruption

1
Institute of Basic Medical Sciences, College of Medicine, National Cheng Kung University, Tainan 701, Taiwan
2
Institute of Biotechnology, College of Bioscience and Biotechnology, National Cheng Kung University, Tainan 701, Taiwan
3
Department of Biotechnology and Bioindustry Sciences, College of Bioscience and Biotechnology, National Cheng Kung University, Tainan 701, Taiwan
4
Department of Microbiology and Immunology, College of Medicine, National Cheng Kung University, Tainan 701, Taiwan
5
Physiology Division, Livestock Research Institute, Council of Agriculture, Taichung 41362, Taiwan
6
Department of Parasitology, College of Medicine, National Cheng Kung University, Tainan City 701, Taiwan
The first two authors contributed equally.
*
Author to whom correspondence should be addressed.
Received: 23 November 2017 / Revised: 14 December 2017 / Accepted: 15 December 2017 / Published: 18 December 2017
(This article belongs to the Special Issue Protein Modifications and Bioconjugation)
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Abstract

Acanthamoeba is free-living protist pathogen capable of causing a blinding keratitis and granulomatous encephalitis. However, the mechanisms of Acanthamoeba pathogenesis are still not clear. Here, our results show that cells co-cultured with pathogenic Acanthamoeba would be spherical and floated, even without contacting the protists. Then, the Acanthamoeba protists would contact and engulf these cells. In order to clarify the contact-independent pathogenesis mechanism in Acanthamoeba, we collected the Acanthamoeba-secreted proteins (Asp) to incubate with cells for identifying the extracellular virulent factors and investigating the cytotoxicity process. The Asps of pathogenic Acanthamoeba express protease activity to reactive Leu amino acid in ECM and induce cell-losing adhesion ability. The M20/M25/M40 superfamily aminopeptidase protein (ACA1_264610), an aminopeptidase be found in Asp, is upregulated after Acanthamoeba and C6 cell co-culturing for 6 h. Pre-treating the Asp with leucine aminopeptidase inhibitor and the specific antibodies of Acanthamoeba M20/M25/M40 superfamily aminopeptidase could reduce the cell damage during Asp and cell co-incubation. These results suggest an important functional role of the Acanthamoeba secreted extracellular aminopeptidases in the Acanthamoeba pathogenesis process. This study provides information regarding clinically pathogenic isolates to target specific molecules and design combined drugs. View Full-Text
Keywords: Acanthamoeba; pathogenesis; M20/M25/M40 superfamily aminopeptidase Acanthamoeba; pathogenesis; M20/M25/M40 superfamily aminopeptidase
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Huang, J.-M.; Liao, C.-C.; Kuo, C.-C.; Chen, L.-R.; Huang, L.L.H.; Shin, J.-W.; Lin, W.-C. Pathogenic Acanthamoeba castellanii Secretes the Extracellular Aminopeptidase M20/M25/M40 Family Protein to Target Cells for Phagocytosis by Disruption. Molecules 2017, 22, 2263.

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