Parasites, Hosts and Diseases

"phagosome"

Original Articles

Phagocytosis-associated genes in Acanthamoeba castellanii feeding on Escherichia coli: Min-Jeong Kim, Eun-Kyung Moon, Hye-Jeong Jo, Fu-Shi Quan, Hyun-Hee Kong; Parasites Hosts Dis 2023;61(4):397-404.
Published online November 28, 2023; DOI: https://doi.org/10.3347/PHD.23088

Acanthamoeba species are free-living amoebae those are widely distributed in the environment. They feed on various microorganisms, including bacteria, fungi, and algae. Although majority of the microbes phagocytosed by Acanthamoeba spp. are digested, some pathogenic bacteria thrive within them. Here, we identified the roles of 3 phagocytosis-associated genes (ACA1_077100, ACA1_175060, and AFD36229.1) in A. castellanii. These 3 genes were upregulated after the ingestion of Escherichia coli. However, after the ingestion of Legionella pneumophila, the expression of these 3 genes was not altered after the consumption of L. pneumophila. Furthermore, A. castellanii transfected with small interfering RNS (siRNA) targeting the 3 phagocytosis-associated genes failed to digest phagocytized E. coli. Silencing of ACA1_077100 disabled phagosome formation in the E. coli-ingesting A. castellanii. Alternatively, silencing of ACA1_175060 enabled phagosome formation; however, phagolysosome formation was inhibited. Moreover, suppression of AFD36229.1 expression prevented E. coli digestion and consequently led to the rupturing of A. castellanii. Our results demonstrated that the ACA1_077100, ACA1_175060, and AFD36229.1 genes of Acanthamoeba played crucial roles not only in the formation of phagosome and phagolysosome but also in the digestion of E. coli.

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Phylogenomic, structural, and cell biological analyses reveal that Stenotrophomonas maltophilia replicates in acidified Rab7A-positive vacuoles of Acanthamoeba castellanii
Javier Rivera, Julio C. Valerdi-Negreros, Diana M. Vázquez-Enciso, Fulvia-Stefany Argueta-Zepeda, Pablo Vinuesa, Michael L. Ginger, Monica Crary, Sutherland K. Maciver
Microbiology Spectrum.2024;[Epub] CrossRef

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Atg3-Mediated Lipidation of Atg8 Is Involved in Encystation of Acanthamoeba: Eun-Kyung Moon, Dong-Il Chung, Yeonchul Hong, Hyun-Hee Kong; Korean J Parasitol 2011;49(2):103-108.
Published online June 14, 2011; DOI: https://doi.org/10.3347/kjp.2011.49.2.103

Abstract
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Autophagy is a catabolic process involved in the degradation of a cell's own components for cell growth, development, homeostasis, and the recycling of cellular products. Autophagosome is an essential component in the protozoan parasite during differentiation and encystation. The present study identified and characterized autophagy-related protein (Atg) 3, a member of Atg8 conjugation system, in Acanthamoeba castellanii (AcAtg3). AcAtg3 encoding a 304 amino acid protein showed high similarity with the catalytic cysteine site of other E2 like enzymes of ubiquitin system. Predicted 3D structure of AcAtg3 revealed a hammer-like shape, which is the characteristic structure of E2-like enzymes. The expression level of AcAtg3 did not increase during encystation. However, the formation of mature cysts was significantly reduced in Atg3-siRNA transfected cells in which the production of Atg8-phosphatidylethanolamine conjugate was inhibited. Fluorescent microscopic analysis revealed that dispersed AcAtg3-EGFP fusion protein gathered around autophagosomal membranes during encystation. These results provide important information for understanding autophagic machinery through the lipidation reaction mediated by Atg3 in Acanthamoeba.

Citations

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