Proteases of Acanthamoeba.
Acanthamoeba
Extracellular
Intracellular
Pathogenic
Protease
Journal
Parasitology research
ISSN: 1432-1955
Titre abrégé: Parasitol Res
Pays: Germany
ID NLM: 8703571
Informations de publication
Date de publication:
08 Dec 2023
08 Dec 2023
Historique:
received:
05
07
2023
accepted:
27
10
2023
medline:
8
12
2023
pubmed:
8
12
2023
entrez:
8
12
2023
Statut:
epublish
Résumé
The members of genus Acanthamoeba are the etiological agent of uncommon but severe or even fatal opportunistic infections in human beings. The presence of different classes of intracellular and extracellular proteases including serine proteases, cysteine proteases, and metalloproteases has been well documented in environmental and clinical isolates of Acanthamoeba spp. However, the role of the proteolytic enzymes in physiological, biological, and pathological mechanisms of the amoeba remains partially investigated. Some attempts have been conducted using various methods to determine the profile of proteases (number, class, optimal conditions, and activity of the enzymes), and possible pathogenicity mechanism of the proteolytic enzymes (various protein substrate degradation, cytopathic effect on different cell lines). In some cases, it was attempted to correlate intracellular and extracellular protease profile with pathogenicity potential of strains. This review revealed that the protease profile of different strains of Acanthamoeba was extremely complex, therefore, further comprehensive studies with application of a combination of various methods may help to elucidate the role of the enzymes.
Identifiants
pubmed: 38063887
doi: 10.1007/s00436-023-08059-z
pii: 10.1007/s00436-023-08059-z
doi:
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
19Informations de copyright
© 2023. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.
Références
Alfieri SC, Correia CE, Motegi SA, Pral EM (2000) Proteinase activities in total extracts and in medium conditioned by Acanthamoeba polyphaga trophozoites. J Parasitol 86:220–227. https://doi.org/10.1645/0022-3395(2000)086[0220:PAITEA]2.0.CO;2
doi: 10.1645/0022-3395(2000)086[0220:PAITEA]2.0.CO;2
pubmed: 10780536
Alizadeh H, Neelam S, Niederkorn JY (2007) Effect of immunization with the mannose-induced Acanthamoeba protein and Acanthamoeba plasminogen activator in mitigating Acanthamoeba keratitis. Invest Ophthalmol vis Sci 48:5597–5604. https://doi.org/10.1167/iovs.07-0407
doi: 10.1167/iovs.07-0407
pubmed: 18055809
Alsam S, Sissons J, Jayasekera S, Khan NA (2005) Extracellular proteases of Acanthamoeba castellanii (encephalitis isolate belonging to T1 genotype) contribute to increased permeability in an in vitro model of the human blood-brain barrier. J Infect 51:150–156. https://doi.org/10.1016/j.jinf.2004.09.001
doi: 10.1016/j.jinf.2004.09.001
pubmed: 16038767
Badenoch PR, Johnson AM, Christy PE, Coster DJ (1990) Pathogenicity of Acanthamoeba and a Corynebacterium in the rat cornea. Arch Ophthalmol 108:107–112. https://doi.org/10.1001/archopht.1990.01070030113040
doi: 10.1001/archopht.1990.01070030113040
pubmed: 2297316
Barker J, Humphrey TJ, Brown MW (1999) Survival of Escherichia coli 0157 in a soil protozoan: implications for disease. FEMS Microbiol Lett 173:291–295. https://doi.org/10.1111/j.1574-6968.1999.tb13516.x
doi: 10.1111/j.1574-6968.1999.tb13516.x
pubmed: 10227158
Blaschitz M, Kohsler M, Aspock H, Walochnik J (2006) Detection of a serine proteinase gene in Acanthamoeba genotype T6 (Amoebozoa: Lobosea). Exp Parasitol 114:26–33. https://doi.org/10.1016/j.exppara.2006.02.004
doi: 10.1016/j.exppara.2006.02.004
pubmed: 16545805
Cano A, Mattana A, Henriquez FL, Alexander J, Roberts CW (2019) Acanthamoeba proteases contribute to macrophage activation through PAR1, but not PAR2. Parasite Immunol 41:e12612. https://doi.org/10.1111/pim.12612
doi: 10.1111/pim.12612
pubmed: 30578557
Cao Z, Jefferson DM, Panjwani N (1998) Role of carbohydrate-mediated adherence in cytopathogenic mechanisms of Acanthamoeba. J Biol Chem 273:15838–15845. https://doi.org/10.1074/jbc.273.25.15838
doi: 10.1074/jbc.273.25.15838
pubmed: 9624184
Cho JH, Na BK, Kim TS, Song CY (2000) Purification and characterization of an extracellular serine proteinase from Acanthamoeba castellanii. IUBMB Life 50:209–214. https://doi.org/10.1080/152165400300001534
doi: 10.1080/152165400300001534
pubmed: 11142349
Cirelli C, Mesquita EIS, Chagas IAR, Furst C, Possamai CO, Abrahão JS, dos Santos Silva LK, Grossi MF, Tagliati CA, Costa AO (2020) Extracellular protease profile of Acanthamoeba after prolonged axenic culture and after interaction with MDCK cells. Parasitol Res 119:659–666. https://doi.org/10.1007/s00436-019-06562-w
doi: 10.1007/s00436-019-06562-w
pubmed: 31848745
Corsaro D, Köhsler M, Montalbano Di Filippo M, Venditti D, Monno R, Di Cave D, Berrilli F, Walochnik J (2017) Update on Acanthamoeba jacobsi genotype T15, including full-length 18S rDNA molecular phylogeny. Parasitol Res 116:1273–1284. https://doi.org/10.1007/s00436-017-5406-1
doi: 10.1007/s00436-017-5406-1
pubmed: 28190156
Culbertson CG, Smith JW, Minner JR (1958) Acanthamoeba: observations on animal pathogenicity. Science 127:1506
doi: 10.1126/science.127.3313.1506
pubmed: 13555916
Culbertson CG, Smith JW, Cohen HK, Minner JR (1959) Experimental infection of mice and monkeys by Acanthamoeba. Am J Pathol 35:185–197
pubmed: 13617418
pmcid: 1934806
Cursons RT, Brown TJ (1978) Use of cell cultures as an indicator of pathogenicity of free-living amoebae. J Clin Pathol 31:1–11. https://doi.org/10.1136/jcp.31.1.1
doi: 10.1136/jcp.31.1.1
pubmed: 342543
pmcid: 476710
Cursons RT, Brown TJ, Keys EA (1978) Virulence of pathogenic free-living amebae. J Parasitol 64:744–745
doi: 10.2307/3279973
pubmed: 682074
da Rocha-Azevedo B, Costa e Silva-Filho F (2007) Biological characterization of a clinical and an environmental isolate of Acanthamoeba polyphaga: analysis of relevant parameters to decode pathogenicity. Arch Microbiol 188:441–449. https://doi.org/10.1007/s00203-007-0264-3
doi: 10.1007/s00203-007-0264-3
pubmed: 17569030
De Jonckheere JF (1980) Growth characteristics, cytopathic effect in cell culture, and virulence in mice of 36 type strains belonging to 19 different Acanthamoeba spp. Appl Environ Microbiol 39:681–685. https://doi.org/10.1128/aem.39.4.681-685.1980
doi: 10.1128/aem.39.4.681-685.1980
pubmed: 6769389
pmcid: 291404
de ObesoFernándezdel Valle A, Melgoza-Ramírez LJ, Esqueda Hernández MF, Rios-Pérez AD, Maciver SK (2023) Identification of an Antimicrobial Protease from Acanthamoeba via a Novel Zymogram. Processes 11:2620
doi: 10.3390/pr11092620
Diehl MLN, Paes J, Rott MB (2021) Genotype distribution of Acanthamoeba in keratitis: a systematic review. Parasitol Res 120:3051–3063. https://doi.org/10.1007/s00436-021-07261-1
doi: 10.1007/s00436-021-07261-1
pubmed: 34351492
pmcid: 8339388
Drozanski W (1956) Fatal bacterial infection in soil amoebae. Acta Microbiol Pol 5:315–317
Dudley R, Alsam S, Khan NA (2008) The role of proteases in the differentiation of Acanthamoeba castellanii. FEMS Microbiol Lett 286:9–15. https://doi.org/10.1111/j.1574-6968.2008.01249.x
doi: 10.1111/j.1574-6968.2008.01249.x
pubmed: 18616591
Duggal SD, Rongpharpi SR, Duggal AK, Kumar A, Biswal I (2017) Role of Acanthamoeba in granulomatous encephalitis: a review. J Infect Dis Immune Ther 1:2
Ferrante A, Bates EJ (1988) Elastase in the pathogenic free-living amoebae Naegleria and Acanthamoeba spp. Infect Immun 56:3320–3321. https://doi.org/10.1128/iai.56.12.3320-3321.1988
doi: 10.1128/iai.56.12.3320-3321.1988
pubmed: 3182083
pmcid: 259744
Ferreira GA, Magliano AC, Pral EM, Alfieri SC (2009) Elastase secretion in Acanthamoeba polyphaga. Acta Trop 112:156–163. https://doi.org/10.1016/j.actatropica.2009.07.015
doi: 10.1016/j.actatropica.2009.07.015
pubmed: 19632188
Fritsche TR, Gautom RK, Seyedirashti S, Bergeron DL, Lindquist TD (1993) Occurrence of bacterial endosymbionts in Acanthamoeba spp. isolated from corneal and environmental specimens and contact lenses. J Clin Microbiol 31:1122–1126. https://doi.org/10.1128/jcm.31.5.1122-1126.1993
doi: 10.1128/jcm.31.5.1122-1126.1993
pubmed: 8501212
pmcid: 262890
Fritsche TR, Sobek D, Gautom RK (1998) Enhancement of in vitro cytopathogenicity by Acanthamoeba spp. following acquisition of bacterial endosymbionts. FEMS Microbiol Lett 166:231–236. https://doi.org/10.1111/j.1574-6968.1998.tb13895.x
doi: 10.1111/j.1574-6968.1998.tb13895.x
pubmed: 9770279
Fuerst PA, Booton GC, Crary M (2015) Phylogenetic analysis and the evolution of the 18S rRNA gene typing system of Acanthamoeba. J Eukaryot Microbiol 62:69–84. https://doi.org/10.1111/jeu.12186
doi: 10.1111/jeu.12186
pubmed: 25284310
Gast RJ, Ledee DR, Fuerst PA, Byers TJ (1996) Subgenus systematics of Acanthamoeba: four nuclear 18S rDNA sequence types. J Eukaryot Microbiol 43:498–504. https://doi.org/10.1111/j.1550-7408.1996.tb04510.x
doi: 10.1111/j.1550-7408.1996.tb04510.x
pubmed: 8976608
Gelman BB, Rauf SJ, Nader R, Popov V, Borkowski J, Chaljub G, Nauta HW, Visvesvara GS (2001) Amoebic encephalitis due to Sappinia diploidea. JAMA 285:2450–2451. https://doi.org/10.1001/jama.285.19.2450
doi: 10.1001/jama.285.19.2450
pubmed: 11368696
Granelli-Piperno A, Reich E (1978) A study of proteases and protease-inhibitor complexes in biological fluids. J Exp Med 148:223–234. https://doi.org/10.1084/jem.148.1.223
doi: 10.1084/jem.148.1.223
pubmed: 78958
pmcid: 2184915
Hadas E, Mazur T (1993a) Biochemical markers of pathogenicity and virulence of Acanthamoeba sp. strains. Parasitol Res 79:696–698. https://doi.org/10.1007/BF00932513
doi: 10.1007/BF00932513
pubmed: 8295908
Hadas E, Mazur T (1993b) Proteolytic enzymes of pathogenic and non-pathogenic strains of Acanthamoeba spp. Trop Med Parasitol 44:197–200
pubmed: 8256097
Hall J, Voelz H (1985) Bacterial endosymbionts of Acanthamoeba sp. J Parasitol 71:89–95
doi: 10.2307/3281982
pubmed: 3981353
Heussen C, Dowdle EB (1980) Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates. Anal Biochem 102:196–202. https://doi.org/10.1016/0003-2697(80)90338-3
doi: 10.1016/0003-2697(80)90338-3
pubmed: 7188842
Horn M, Wagner M (2004) Bacterial endosymbionts of free-living amoebae. J Eukaryot Microbiol 51:509–514. https://doi.org/10.1111/j.1550-7408.2004.tb00278.x
doi: 10.1111/j.1550-7408.2004.tb00278.x
pubmed: 15537084
Hurt M, Neelam S, Niederkorn J, Alizadeh H (2003) Pathogenic Acanthamoeba spp secrete a mannose-induced cytolytic protein that correlates with the ability to cause disease. Infect Immun 71:6243–6255. https://doi.org/10.1128/IAI.71.11.6243-6255.2003
doi: 10.1128/IAI.71.11.6243-6255.2003
pubmed: 14573643
pmcid: 219557
Iovieno A, Ledee DR, Miller D, Alfonso EC (2010) Detection of bacterial endosymbionts in clinical Acanthamoeba isolates. Ophthalmology 117:445–452. https://doi.org/10.1016/j.ophtha.2009.08.033
doi: 10.1016/j.ophtha.2009.08.033
pubmed: 20031220
Kalra SK, Sharma P, Shyam K, Tejan N, Ghoshal U (2020) Acanthamoeba and its pathogenic role in granulomatous amebic encephalitis. Exp Parasitol 208:107788. https://doi.org/10.1016/j.exppara.2019.107788
doi: 10.1016/j.exppara.2019.107788
pubmed: 31647916
Khan NA (2003) Pathogenesis of Acanthamoeba infections. Microb Pathog 34:277–285. https://doi.org/10.1016/s0882-4010(03)00061-5
doi: 10.1016/s0882-4010(03)00061-5
pubmed: 12782480
Khan NA (2006) Acanthamoeba: biology and increasing importance in human health. FEMS Microbiol Rev 30:564–595. https://doi.org/10.1111/j.1574-6976.2006.00023.x
doi: 10.1111/j.1574-6976.2006.00023.x
pubmed: 16774587
Khan NA, Siddiqui R (2014) Predator vs aliens: bacteria interactions with Acanthamoeba. Parasitology 141:869–874. https://doi.org/10.1017/S003118201300231X
doi: 10.1017/S003118201300231X
pubmed: 24512693
Khan NA, Jarroll EL, Panjwani N, Cao Z, Paget TA (2000) Proteases as markers for differentiation of pathogenic and nonpathogenic species of Acanthamoeba. J Clin Microbiol 38:2858–2861. https://doi.org/10.1128/JCM.38.8.2858-2861.2000
doi: 10.1128/JCM.38.8.2858-2861.2000
pubmed: 10921939
pmcid: 87129
Khan NA, Jarroll EL, Paget TA (2001) Acanthamoeba can be differentiated by the polymerase chain reaction and simple plating assays. Curr Microbiol 43:204–208. https://doi.org/10.1007/s002840010288
doi: 10.1007/s002840010288
pubmed: 11400071
Khan NA, Jarroll EL, Paget TA (2002) Molecular and physiological differentiation between pathogenic and nonpathogenic Acanthamoeba. Curr Microbiol 45:197–202. https://doi.org/10.1007/s00284-001-0108-3
doi: 10.1007/s00284-001-0108-3
pubmed: 12177742
Kim WT, Kong HH, Ha YR, Hong YC, Jeong HJ, Yu HS, Chung DI (2006) Comparison of specific activity and cytopathic effects of purified 33 kDa serine proteinase from Acanthamoeba strains with different degree of virulence. Korean J Parasitol 44:321–330. https://doi.org/10.3347/kjp.2006.44.4.321
doi: 10.3347/kjp.2006.44.4.321
pubmed: 17170574
pmcid: 2559134
Klemba M, Goldberg DE (2002) Biological roles of proteases in parasitic protozoa. Annu Rev Biochem 71:275–305. https://doi.org/10.1146/annurev.biochem.71.090501.145453
doi: 10.1146/annurev.biochem.71.090501.145453
pubmed: 12045098
Köhsler M, Mrva M, Walochnik J (2016) Acanthamoeba. In Molecular Parasitology, pp 285–324: Springer
Kong HH, Kim TH, Chung DI (2000) Purification and characterization of a secretory serine proteinase of Acanthamoeba healyi isolated from GAE. J Parasitol 86:12–17. https://doi.org/10.1645/0022-3395(2000)086[0012:PACOAS]2.0.CO;2
doi: 10.1645/0022-3395(2000)086[0012:PACOAS]2.0.CO;2
pubmed: 10701557
La Scola B, Raoult D (2001) Survival of Coxiella burnetii within free-living amoeba Acanthamoeba castellanii. Clin Microbiol Infect 7:75–79. https://doi.org/10.1046/j.1469-0691.2001.00193.x
doi: 10.1046/j.1469-0691.2001.00193.x
pubmed: 11298146
Leher H, Silvany R, Alizadeh H, Huang J, Niederkorn JY (1998) Mannose induces the release of cytopathic factors from Acanthamoeba castellanii. Infect Immun 66:5–10. https://doi.org/10.1128/IAI.66.1.5-10.1998
doi: 10.1128/IAI.66.1.5-10.1998
pubmed: 9423832
pmcid: 107851
Leitsch D, Köhsler M, Marchetti-Deschmann M, Deutsch A, Allmaier G, Duchêne M, Walochnik J (2010) Major role for cysteine proteases during the early phase of Acanthamoeba castellanii encystment. Eukaryot Cell 9:611–618. https://doi.org/10.1128/EC.00300-09
doi: 10.1128/EC.00300-09
pubmed: 20190073
pmcid: 2863413
Lorenzo-Morales J, Lindo JF, Martinez E, Calder D, Figueruelo E, Valladares B, Ortega-Rivas A (2005) Pathogenic Acanthamoeba strains from water sources in Jamaica, West Indies. Ann Trop Med Parasitol 99:751–758. https://doi.org/10.1179/136485905X65215
doi: 10.1179/136485905X65215
pubmed: 16297288
Lorenzo-Morales J, Khan NA, Walochnik J (2015) An update on Acanthamoeba keratitis: diagnosis, pathogenesis and treatment. Parasite 22:10. https://doi.org/10.1051/parasite/2015010
doi: 10.1051/parasite/2015010
pubmed: 25687209
pmcid: 4330640
Ly TMC, Müller HE (1990) Ingested Listeria monocytogenes survive and multiply in protozoa. J Med Microbiol 33:51–54. https://doi.org/10.1099/00222615-33-1-51
doi: 10.1099/00222615-33-1-51
pubmed: 2121990
Magliano AC, da Silva FM, Teixeira MM, Alfieri SC (2009) Genotyping, physiological features and proteolytic activities of a potentially pathogenic Acanthamoeba sp. isolated from tap water in Brazil. Exp Parasitol 123:231–235. https://doi.org/10.1016/j.exppara.2009.07.006
doi: 10.1016/j.exppara.2009.07.006
pubmed: 19646440
Mahdavi Poor B, Dalimi A, Ghafarifar F, Khoshzaban F, Abdolalizadeh J (2017) Characterization of extracellular proteases of Acanthamoeba genotype T4 isolated from different sources in Iran. Parasitol, Res 116:3373–3380. https://doi.org/10.1007/s00436-017-5656-y
doi: 10.1007/s00436-017-5656-y
pubmed: 29075925
Marciano-Cabral F, Cabral G (2003) Acanthamoeba spp. as agents of disease in humans. Clin Microbiol Rev 16:273–307. https://doi.org/10.1128/CMR.16.2.273-307.2003
doi: 10.1128/CMR.16.2.273-307.2003
pubmed: 12692099
pmcid: 153146
McKerrow JH, Caffrey C, Kelly B, Loke P, Sajid M (2006) Proteases in parasitic diseases. Annu Rev Pathol 1:497–536. https://doi.org/10.1146/annurev.pathol.1.110304.100151
doi: 10.1146/annurev.pathol.1.110304.100151
pubmed: 18039124
Michalek M, Sönnichsen FD, Wechselberger R, Dingley AJ, Hung CW, Kopp A, Wienk H, Simanski M, Herbst R, Lorenzen I, Marciano-Cabral F (2013) Structure and function of a unique pore-forming protein from a pathogenic Acanthamoeba. Nat Hem Bio 9:37–42. https://doi.org/10.1038/nchembio.1116
doi: 10.1038/nchembio.1116
Michel R, Burghardt H, Bergmann H (1995) Acanthamoeba, naturally intracellularly infected with Pseudomonas aeruginosa, after their isolation from a microbiologically contaminated drinking water system in a hospital. Zentralbl Hyg Umweltmed 196:532–544
pubmed: 7619202
Mitra MM, Alizadeh H, Gerard RD, Niederkorn JY (1995) Characterization of a plasminogen activator produced by Acanthamoeba castellanii. Mol Biochem Parasitol 73:157–164. https://doi.org/10.1016/0166-6851(94)00109-z
doi: 10.1016/0166-6851(94)00109-z
pubmed: 8577323
Mitro K, Bhagavathiammai A, Zhou OM, Bobbett G, McKerrow JH, Chokshi R, Chokshi B, James ER (1994) Partial characterization of the proteolytic secretions of Acanthamoeba polyphaga. Exp Parasitol 78:377–385. https://doi.org/10.1006/expr.1994.1041
doi: 10.1006/expr.1994.1041
pubmed: 8206136
Moon EK, Chung DI, Hong YC, Kong HH (2008) Characterization of a serine proteinase mediating encystation of Acanthamoeba. Eukaryot Cell 7:1513–1517. https://doi.org/10.1128/EC.00068-08
doi: 10.1128/EC.00068-08
pubmed: 18676958
pmcid: 2547060
Moon EK, Xuan YH, Chung DI, Hong Y, Kong HH (2011) Microarray analysis of differentially expressed genes between cysts and trophozoites of Acanthamoeba castellanii. Korean J Parasitol 49:341–347. https://doi.org/10.3347/kjp.2011.49.4.341
doi: 10.3347/kjp.2011.49.4.341
pubmed: 22355200
pmcid: 3279671
Moon EK, Hong Y, Chung DI, Kong HH (2012) Cysteine protease involving in autophagosomal degradation of mitochondria during encystation of Acanthamoeba. Mol Biochem Parasitol 185:121–126. https://doi.org/10.1016/j.molbiopara.2012.07.008
doi: 10.1016/j.molbiopara.2012.07.008
pubmed: 22917557
Moon EK, Hong Y, Lee HA, Quan FS, Kong HH (2017) DNA Methylation of Gene Expression in Acanthamoeba castellanii Encystation. Korean J Parasitol 55:115–120
doi: 10.3347/kjp.2017.55.2.115
pubmed: 28506032
pmcid: 5450953
Mortazavi PN, Keisary E, Loh LN, Jung SY, Khan NA (2011) Possible roles of phospholipase A2 in the biological activities of Acanthamoeba castellanii (T4 genotype). Protist 162:168–176. https://doi.org/10.1016/j.protis.2010.03.005
doi: 10.1016/j.protis.2010.03.005
pubmed: 20650684
Morton LD, McLaughlin GL, Whiteley HE (1991) Effects of temperature, amebic strain, and carbohydrates on Acanthamoeba adherence to corneal epithelium in vitro. Infect Immun 59:3819–3822
doi: 10.1128/iai.59.10.3819-3822.1991
pubmed: 1894379
pmcid: 258957
Na BK, Kim JC, Song CY (2001) Characterization and pathogenetic role of proteinase from Acanthamoeba castellanii. Microb Pathog 30:39–48. https://doi.org/10.1006/mpat.2000.0403
doi: 10.1006/mpat.2000.0403
pubmed: 11162184
Page FC (1981) A Light-and Electron-Microscopical Study of Protacanthamoeba caledonican. sp., Type-Species of Protacanthamoebang (Amoebida, Acanthamoebidae). J Protozool 28:70–78
doi: 10.1111/j.1550-7408.1981.tb02807.x
Park MK, Cho MK, Kang SA, Park HK, Kim DH, Yu HS (2014) Acanthamoeba protease activity promotes allergic airway inflammation via protease-activated receptor 2. PLoS ONE 9:e92726. https://doi.org/10.1371/journal.pone.0092726
doi: 10.1371/journal.pone.0092726
pubmed: 24658532
pmcid: 3962434
Pellegrin JL, Ortega-Barria E, Barza M, Baum J, Pereira ME (1991) Neuraminidase activity in Acanthamoeba species trophozoites and cysts. Invest Ophthalmol vis Sci 32:3061–3066
pubmed: 1938282
Poor BM, Dalimi A, Ghafarifar F, Khoshzaban F, Abdolalizadeh J (2018) Contamination of swimming pools and hot tubs biofilms with Acanthamoeba. Acta Parasitol 63:147–153. https://doi.org/10.1515/ap-2018-0016
doi: 10.1515/ap-2018-0016
pubmed: 29351066
Proca-Ciobanu M, Lupascu GH, Petrovici A, Ionescu MD (1975) Electron microscopic study of a pathogenic Acanthamoeba castellani strain: the presence of bacterial endosymbionts. Int J Parasitol 5:49–56. https://doi.org/10.1016/0020-7519(75)90097-1
doi: 10.1016/0020-7519(75)90097-1
pubmed: 803475
Pussard M, Pons R (1977) Morphologie de la paroi kystiqueet taxonomie du genre Acanthamoeba (Protozoa, Amoebida). Protistologica 8:557–598
Putaporntip C, Kuamsab N, Nuprasert W, Rojrung R, Pattanawong U, Tia T, Yanmanee S, Jongwutiwes S (2021) Analysis of Acanthamoeba genotypes from public freshwater sources in Thailand reveals a new genotype, T23 Acanthamoeba bangkokensis sp. nov. Sci Rep 11:17290. https://doi.org/10.1038/s41598-021-96690-0
doi: 10.1038/s41598-021-96690-0
pubmed: 34453084
pmcid: 8397737
Qvarnstrom Y, Da Silva AJ, Schuster FL, Gelman BB, Visvesvara GS (2009) Molecular confirmation of Sappinia pedata as a causative agent of amoebic encephalitis. J Infect Dis 199:1139–1142. https://doi.org/10.1086/597473
doi: 10.1086/597473
pubmed: 19302010
Ramirez-Rico G, Martinez-Castillo M, de la Garza M, Shibayama M, Serrano-Luna J (2015) Acanthamoeba castellanii Proteases are Capable of Degrading Iron-Binding Proteins as a Possible Mechanism of Pathogenicity. J Eukaryot Microbiol 62:614–622. https://doi.org/10.1111/jeu.12215
doi: 10.1111/jeu.12215
pubmed: 25737266
Rowbotham TJ (1980) Preliminary report on the pathogenicity of Legionella pneumophila for freshwater and soil amoebae. J Clin Pathol 33:1179–1183. https://doi.org/10.1136/jcp.33.12.1179
doi: 10.1136/jcp.33.12.1179
pubmed: 7451664
pmcid: 1146371
Sarath G, De La Motte R, Wagner F (1989) Protease assay methods. In: Beynon R, Bond J (eds) Proteolytic enzymes: a practical approach. University Press UK, Oxford, pp 25–56
Schuster FL, Visvesvara GS (2004) Free-living amoebae as opportunistic and non-opportunistic pathogens of humans and animals. Int J Parasitol 34:1001–1027. https://doi.org/10.1016/j.ijpara.2004.06.004
doi: 10.1016/j.ijpara.2004.06.004
pubmed: 15313128
Serrano-Luna J, Cervantes-Sandoval I, Calderon J, Navarro-Garcia F, Tsutsumi V, Shibayama M (2006) Protease activities of Acanthamoeba polyphaga and Acanthamoeba castellanii. Can J Microbiol 52:16–23. https://doi.org/10.1139/w05-114
doi: 10.1139/w05-114
pubmed: 16541155
Siddiqui R, Khan NA (2012) Biology and pathogenesis of Acanthamoeba. Parasit Vectors 5:6
doi: 10.1186/1756-3305-5-6
pubmed: 22229971
pmcid: 3284432
Sissons J, Alsam S, Goldsworthy G, Lightfoot M, Jarroll EL, Khan NA (2006) Identification and properties of proteases from an Acanthamoeba isolate capable of producing granulomatous encephalitis. BMC Microbiol 6:42. https://doi.org/10.1186/1471-2180-6-42
doi: 10.1186/1471-2180-6-42
pubmed: 16672059
pmcid: 1464133
Stothard DR, Schroeder-Diedrich JM, Awwad MH, Gast RJ, Ledee DR, Rodriguez-Zaragoza S, Dean CL, Fuerst PA, Byers TJ (1998) The evolutionary history of the genus Acanthamoeba and the identification of eight new 18S rRNA gene sequence types. J Eukaryot Microbiol 45:45–54. https://doi.org/10.1111/j.1550-7408.1998.tb05068.x
doi: 10.1111/j.1550-7408.1998.tb05068.x
pubmed: 9495032
pmcid: 7194170
Tawfeek GM, Bishara SA, Sarhan RM, ElShabrawi Taher E, ElSaady Khayyal A (2016) Genotypic, physiological, and biochemical characterization of potentially pathogenic Acanthamoeba isolated from the environment in Cairo. Egypt Parasitol Res 115:1871–1881. https://doi.org/10.1007/s00436-016-4927-3
doi: 10.1007/s00436-016-4927-3
pubmed: 26841771
Thom S, Warhurst D, Drasar BS (1992) Association of Vibrio cholerae with fresh water amoebae. J Med Mocrobiol 36:303–306. https://doi.org/10.1099/00222615-36-5-303
doi: 10.1099/00222615-36-5-303
Tice AK, Shadwick LL, Fiore-Donno AM, Geisen S, Kang S, Schuler GA, Spiegel FW, Wilkinson KA, Bonkowski M, Dumack K, Lahr DJ (2016) Expansion of the molecular and morphological diversity of Acanthamoebidae (Centramoebida, Amoebozoa) and identification of a novel life cycle type within the group. Biol Direct 11:1–21. https://doi.org/10.1186/s13062-016-0171-0
doi: 10.1186/s13062-016-0171-0
Trabelsi H, Dendana F, Sellami A, Sellami H, Cheikhrouhou F, Neji S, Makni F, Ayadi A (2012) Pathogenic free-living amoebae: Epidemiology and clinical review. Pathol Biol (paris) 60:399–405. https://doi.org/10.1016/j.patbio.2012.03.002
doi: 10.1016/j.patbio.2012.03.002
pubmed: 22520593
Vandooren J, Geurts N, Martens E, Van den Steen PE, Opdenakker G (2013) Zymography methods for visualizing hydrolytic enzymes. Nat Method 10:211–220. https://doi.org/10.1038/nmeth.2371
doi: 10.1038/nmeth.2371
Visvesvara GS, Schuster FL, Martinez AJ (1993) Balamuthia mandrillaris, NG, N. Sp., agent of amebic meningoencephalitis in humans and other animals. J Eukaryot Microbiol 40:504–514. https://doi.org/10.1111/j.1550-7408.1993.tb04943.x
doi: 10.1111/j.1550-7408.1993.tb04943.x
pubmed: 8330028
Walochnik J, Haller-Schober EM, Kolli H, Picher O, Obwaller A, Aspock H (2000) Discrimination between clinically relevant and nonrelevant Acanthamoeba strains isolated from contact lens-wearing keratitis patients in Austria. J Clin Microbiol 38:3932–3936. https://doi.org/10.1128/JCM.38.11.3932-3936.2000
doi: 10.1128/JCM.38.11.3932-3936.2000
pubmed: 11060047
pmcid: 87520
Walochnik J, Sommer K, Obwaller A, Haller-Schober EM, Aspöck H (2004) Characterisation and differentiation of pathogenic and non-pathogenic Acanthamoeba strains by their protein and antigen profiles. Parasitol Res 92:289–298. https://doi.org/10.1007/s00436-003-1041-0
doi: 10.1007/s00436-003-1041-0
pubmed: 14722757
Wang Z, Wu D, Tachibana H, Feng M, Cheng XJ (2020) Identification and biochemical characterisation of Acanthamoeba castellanii cysteine protease 3. Parasit Vectors 13:592. https://doi.org/10.1186/s13071-020-04474-8
doi: 10.1186/s13071-020-04474-8
pubmed: 33228764
pmcid: 7685649
Wang Y, Jiang L, Zhao Y, Ju X, Wang L, Jin L, Fine RD, Li M (2023) Biological characteristics and pathogenicity of Acanthamoeba. Front Microbiol 14:1147077
doi: 10.3389/fmicb.2023.1147077
pubmed: 37089530
pmcid: 10113681
Wilkesman J, Kurz L (2009) Protease analysis by zymography: a review on techniques and patents. Recent Pat Biotechnol 3:175–184. https://doi.org/10.2174/187220809789389162
doi: 10.2174/187220809789389162
pubmed: 19954417
Winiecka-Krusnell J, Wreiber K, Euler AV, Engstrand L, Linder E (2002) Free-living amoebae promote growth and survival of Helicobacter pylori. Scand J Infect Dis. 34:253–256. https://doi.org/10.1080/00365540110080052
doi: 10.1080/00365540110080052
pubmed: 12064686
Xuan YH, Yu HS, Jeong HJ, Seol SY, Chung DI, Kong HH (2007) Molecular characterization of bacterial endosymbionts of Acanthamoeba isolates from infected corneas of Korean patients. Korean J Parasitol 45:1–9. https://doi.org/10.3347/kjp.2007.45.1.1
doi: 10.3347/kjp.2007.45.1.1
pubmed: 17374972
pmcid: 2526339