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Ac-HSP20 Is Associated With the Infectivity and Encystation of Acanthamoeba castellanii
This study aimed to determine the biological functions of heat shock protein (HSP)-20 of A. castellanii (Ac-HSP20) involved in the maintenance of life cycle and the infectivity of A. castellanii. Immunoscreening A. castellanii cDNA library with A. castellanii infected rabbit sera identified three positive clones, one of them was a putative heat shock protein (Ac-HSP20). The recombinant 23 kDa Ac-HSP20 protein (rAc-HSP20) was successfully expressed in Escherichia coli BL21 (DE3) and purified using metal affinity chromatography. The rabbits immunized with rAc-HSP20 produced high titer antibody (1:25,600). Immunolocalization ...
Source: Frontiers in Microbiology - January 12, 2021 Category: Microbiology Source Type: research

Box Behnken design of siRNA-loaded liposomes for the treatment of a murine model of ocular keratitis caused by Acanthamoeba
In this study, PEGylated cationic liposomes were proposed and optimized using Box-Behnken design. The influence of DOTAP:DOPE ratio, DSPE-PEG concentration, and siRNA/DOTAP charge ratio were evaluated over both biological response and physicochemical properties of liposomes. The ratio of DOTAP:DOPE had an effect in the trophozoite activity whereas the charge ratio influenced both size and protease activity. The predicted values were very close to the observed values, yielding a formulation with good activity and toxicity profile, which was used in the following experiments. A murine model of ocular keratitis was treated wi...
Source: Colloids and Surfaces B: Biointerfaces - October 29, 2018 Category: Biochemistry Source Type: research

Identification and Characterization of Protein Arginine Methyltransferase 1 in Acanthamoeba castellanii.
In this study, the full-length 1,059 bp cDNA sequence of Acanthamoeba castellanii PRMT1 (AcPRMT1) was cloned for the first time. The AcPRMT1 protein comprised of 352 amino acids with a SAM-dependent methyltransferase PRMT-type domain. The expression level of AcPRMT1 was highly increased during encystation of A. castellanii. The EGFP-AcPRMT1 fusion protein was distributed over the cytoplasm, but it was mainly localized in the nucleus of Acanthamoeba. Knock down of AcPRMT1 by synthetic siRNA with a complementary sequence failed to form mature cysts. These findings suggested that AcPRMT1 plays a critical role in the regulatio...
Source: Korean Journal of Parasitology - May 17, 2017 Category: Parasitology Tags: Korean J Parasitol Source Type: research

siRNA ‐loaded liposomes: inhibition of encystment of Acanthamoeba and toxicity on the eye surface
This article is protected by copyright. All rights reserved. Glycogen phosphorilase, a key enzyme for encystment of Acanthamoeba,was silenced PEGylated cationic liposomes were used as carriers for siRNA delivery Ther was a significant reduction in the encystment of AP2 trophozoties
Source: Chemical Biology and Drug Design - January 29, 2017 Category: Biology Authors: Kathrin Faber, Giovanni K. Zorzi, Nathaly T. Brazil, Marilise B. Rott, Helder F. Teixeira Tags: Research Article Source Type: research

Identification of Protein Arginine Methyltransferase 5 as a Regulator for Encystation of Acanthamoeba.
Authors: Moon EK, Hong Y, Chung DI, Goo YK, Kong HH Abstract Encystation is an essential process for Acanthamoeba survival under nutrient-limiting conditions and exposure to drugs. The expression of several genes has been observed to increase or decrease during encystation. Epigenetic processes involved in regulation of gene expression have been shown to play a role in several pathogenic parasites. In the present study, we identified the protein arginine methyltransferase 5 (PRMT5), a known epigenetic regulator, in Acanthamoeba castellanii. PRMT5 of A. castellanii (AcPRMT5) contained domains found in S-adenosylmeth...
Source: Korean Journal of Parasitology - May 20, 2016 Category: Parasitology Tags: Korean J Parasitol Source Type: research

Evaluation of Acanthamoeba myosin-IC as a potential therapeutic target.
Abstract Members of the genus Acanthamoeba are facultative pathogens of humans, causing a sight threatening keratitis and a fatal encephalitis. We have targeted myosin-IC by siRNA silencing as a therapeutic approach, since it is known that the function of this protein is vital for the amoeba. In this work, specific siRNAs were developed against the Acanthamoeba myosin-IC gene. Treated and control amoebae were cultured in growth and encystment medium in order to evaluate the induced effects after myosin-IC gene knock-down as we have anticipated that cyst formation may be impaired. The effective of silencing the myo...
Source: Antimicrobial Agents and Chemotherapy - January 27, 2014 Category: Microbiology Authors: Martín-Navarro CM, Lorenzo-Morales J, López-Arencibia A, Reyes-Batlle M, Piñero JE, Valladares B, Maciver SK Tags: Antimicrob Agents Chemother Source Type: research