Abstract
Acanthamoebae are ubiquitous free-living amoebae that occur abundantly in water and soil worldwide, being among the most versatile protozoan organisms. They generally do not need a host, but when they accidentally have contact to the human eye, lung or skin, they can cause severe disease. They are the causative agents of Acanthamoeba keratitis (AK), on the one hand, and of several disseminating infections in the immunocompromised host eventually leading to granulomatous amoebic encephalitis (GAE), on the other hand. The infective and invasive form of Acanthamoeba is the trophozoite; nevertheless, the cyst plays an important role in the distribution of the amoebae as well as in the course of disease. Acanthamoebae can form cysts within the host tissue, and these cysts are resistant against treatment and also often lead to reinfections.
Altogether, around 25 different species divided into three morphological groups have been described; however, the validity of many species has been challenged by molecular analyses. Currently, the genus is divided into 20 genotypes based on 18S rDNA sequencing, but the number of genotypes is growing constantly. Genotype T4 seems to be the most abundant one in most habitats and also the most common genotype in human infections; however, a classification into virulent and non-virulent genotypes is not possible. Acanthamoebae pathogenicity depends on cell-cell contact, the cytolytic event being triggered by an intimate contact between the amoebae with the target cells, established primarily via lectin-like amoebic adherence molecules. The ability of acanthamoebae to lyse cells is mainly based on lysosomal hydrolases and phospholipases.
In 2013, a first genome has become available revealing a significant number of genes presumably acquired by lateral gene transfer and a rather complex cell communication repertoire. However, the genetics of Acanthamoeba spp. is far from being fully elucidated. Fact is that acanthamoebae have unusually broad metabolic and biosynthetic capabilities, being able to synthesise most amino acids (even multiple steps), co-factors and vitamins and nucleotides de novo. Moreover, they can digest a wide range of nutrients, they are among the few protozoa with a cellulase, and they are the only protozoans known to date with an alginate lyase. Although acanthamoebae generally divide by binary fission and there is no convincing evidence for genetic recombination, even their asexual nature has been challenged recently.
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Abbreviations
- AA:
-
Arachidonic acid (AA)
- AcAtg:
-
Acanthamoeba autophagy-related proteins
- AIF:
-
Apoptosis-inducing factor
- AK:
-
Acanthamoeba keratitis
- AOX:
-
Alternative oxidase
- aPA:
-
Acanthamoeba plasminogen activator
- cAMP:
-
Cyclic adenosine monophosphate
- CPE:
-
Cytopathic effect
- CRD:
-
Carbohydrate recognition domains
- CSCP:
-
Cyst-specific cysteine protease
- CXCL2:
-
Chemokine (C-X-C motif) ligand 2
- cPLA:
-
Cytosolic phospholipase A
- DAG:
-
Diacylglycerol
- DH:
-
Dehydrogenase
- ECM:
-
Extracellular matrix
- ERMES:
-
ER-mitochondria encounter structure
- EST:
-
Expressed sequence tag
- ETC:
-
Electron transport chain
- FFA:
-
Free fatty acid
- GAE:
-
Granulomatous amoebic encephalitis
- GMP:
-
Guanosine monophosphate
- GPCR:
-
G protein-coupled receptors
- HBMEC:
-
Human brain microvascular endothelial cells
- HCE:
-
Human corneal epithelial cells
- HNE:
-
4-Hydroxy-2-nonenal
- ICL:
-
Isocitrate lyase
- LBP:
-
Laminin-binding protein
- LGT:
-
Lateral gene transfer
- MalS:
-
Malate synthase
- MAPK:
-
Mitogen-activated protein kinase
- MBP:
-
Mannose-binding protein
- MIP:
-
Mannose-induced protein
- MMP:
-
Matrix metalloprotease
- ORF:
-
Open reading frame
- PAR:
-
Protease-activated receptor
- PDH:
-
Pyruvate dehydrogenase
- PHB:
-
Polyhydroxybutyrate
- PI3K:
-
Phosphatidylinositol 3-kinase
- PKC:
-
Protein kinase C-like gene
- PMN:
-
Polymorphonuclear leukocyte
- PN:
-
Purine nucleotide
- pTyr:
-
Phosphotyrosine
- ROS:
-
Reactive oxygen species
- SAPLIP:
-
Saposin-like protein
- TCA:
-
Tricarboxylic acid
- TLR:
-
Toll-like receptors (TLR)
- UCP:
-
Uncoupling protein
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Further Reading (Examples)
Clarke DW, Niederkorn JY (2006a) The immunobiology of Acanthamoeba keratitis. Microbes Infect 8(5):1400–1405
Clarke DW, Niederkorn JY (2006b) The pathophysiology of Acanthamoeba keratitis. Trends Parasitol 22(4):175–180
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Ferrante A (1991b) Free-living amoebae: pathogenicity and immunity. Parasite Immunol 13(1):31–47
Ferreira GA, Magliano AC, Pral EM, Alfieri SC (2009) Elastase secretion in Acanthamoeba polyphaga. Acta Trop 112(2):156–163
Khan NA (2015) Acanthamoeba: Biology and Pathogenesis, 2nd edn. Caister Academic Press, Norfolk, 334p
Khan NA (2007) Acanthamoeba invasion of the central nervous system. Int J Parasitol 37(2):131–138
Lloyd D (2014) Encystment in Acanthamoeba castellanii: a review. Exp Parasitol 145(Suppl):S20–S27
Lorenzo-Morales J, Khan NA, Walochnik J (2015) An update on Acanthamoeba keratitis: diagnosis, pathogenesis and treatment. Parasite 22:10
Marciano-Cabral F, Cabral G (2003) Acanthamoeba spp. as agents of disease in humans. Clin Microbiol Rev 16(2):273–307
Page FC (1987b) The classification of the naked amoebae (Phylum Rhizopoda). Arch Protist 133:199–217
Page FC (1988) A new key to freshwater and soil gymnamoebae. Freshwater Biol. Ass., Ambleside
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Rondanelli EG (ed) (1987) Amphizoic amoebae. Human pathology. Infectious diseases color atlas monographs. Piccin Nuova Libraria, Padua, 279 p
Siddiqui R, Khan NA (2012) Biology and pathogenesis of Acanthamoeba. Parasit Vectors 5:6
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Acknowledgements
The authors wish to thank Michael Duchêne for critically reading the manuscript. Moreover, we would like to thank the Acanthamoeba community for all the excellent studies that have been performed, without which we would not have been able to write this chapter.
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Köhsler, M., Mrva, M., Walochnik, J. (2016). Acanthamoeba . In: Walochnik, J., Duchêne, M. (eds) Molecular Parasitology. Springer, Vienna. https://doi.org/10.1007/978-3-7091-1416-2_10
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