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Comparison of Proteins Secreted into Extracellular Space of Pathogenic and Non-pathogenic Acanthamoeba castellanii

  • Moon, Eun-Kyung (Department of Medical Zoology, Kyung Hee University School of Medicine) ;
  • Choi, Hyun-Seo (Department of Medical Zoology, Kyung Hee University School of Medicine) ;
  • Park, So-Min (Department of Biomedical Science, Graduate School, Kyung Hee University) ;
  • Kong, Hyun-Hee (Department of Parasitology, Dong-A University College of Medicine) ;
  • Quan, Fu-Shi (Department of Medical Zoology, Kyung Hee University School of Medicine)
  • Received : 2018.09.07
  • Accepted : 2018.10.31
  • Published : 2018.12.31

Abstract

Pathogenic Acanthamoeba spp. cause granulomatous amoebic encephalitis and keratitis. Acanthamoeba keratitis (AK) is a rare but serious ocular infection that can result in permanent visual impairment or blindness. However, pathogenic factors of AK remain unclear and treatment for AK is arduous. Expression levels of proteins secreted into extracellular space were compared between A. castellanii pathogenic (ACP) and non-pathogenic strains. Two-dimensional polyacrylamide gel electrophoresis revealed 123 differentially expressed proteins, including 34 increased proteins, 7 qualitative increased proteins, 65 decreased proteins, and 17 qualitative decreased proteins in ACP strain. Twenty protein spots with greater than 5-fold increase in ACP strain were analyzed by liquid chromatography triple quadrupole mass spectrometry. These proteins showed similarity each to inosine-uridine preferring nucleoside hydrolase, carboxylesterase, oxygen-dependent choline dehydrogenase, periplasmic-binding protein proteinases and hypothetical proteins. These proteins expressed higher in ACP may provide some information to understand pathogenicity of Acanthamoeba.

Keywords

References

  1. Marciano-Cabral F, Cabral G. Acanthamoeba spp. as agents of disease in humans. Clin Microbiol Rev 2003; 16: 273-307. https://doi.org/10.1128/CMR.16.2.273-307.2003
  2. Jones DB, Visvesvara GS, Robinson NM. Acanthamoeba polyphaga keratitis and Acenthamoeba uveitis associated with fatal meningoencephalitis. Trans Ophthalmol Soc UK 1975; 95: 221-232.
  3. Verani JR, Lorick SA, Yoder JS, Beach MJ, Braden CR, Roberts JM, Conover CS, Chen S, McConnell KA, Chang DC, Park BJ, Jones DB, Visvesvara GS, Roy SL. National outbreak of Acanthamoeba keratitis associated with use of a contact lens solution, United States. Emerg Infect Dis 2009; 15: 1236-1242. https://doi.org/10.3201/eid1508.090225
  4. Awwad ST, Petroll WM, McCulley JP, Cavanagh HD. Updates in Acanthamoeba keratitis. Eye Contact Lens 2007; 33: 1-8. https://doi.org/10.1097/ICL.0b013e31802b64c1
  5. Garate M, Marchant J, Cubillos I, Cao Z, Khan NA, Panjwani N. In vitro pathogenicity of Acanthamoeba is associated with the expression of the mannose-binding protein. Invest Ophthalmol Vis Sci 2006; 47: 1056-1062. https://doi.org/10.1167/iovs.05-0477
  6. Serrano-Luna Jde J, Cervantes-Sandoval I, Calderon J, Navarro-Garcia F, Tsutsumi V, Shibayama M. Protease activities of Acanthamoeba polyphaga and Acanthamoeba castellanii. Can J Microbiol 2006; 52: 16-23. https://doi.org/10.1139/w05-114
  7. Reed S, Bouvier J, Pollack AS, Engel JC, Brown M, Hirata K, Que X, Eakin A, Hagblom P, Gillin F. Cloning of a virulence factor of Entamoeba histolytica. Pathogenic strains possess a unique cysteine proteinase gene. J Clin Invest 1993; 91: 1532-1540. https://doi.org/10.1172/JCI116359
  8. Moncada D, Keller K, Chadee K. Entamoeba histolytica-secreted products degrade colonic mucin oligosaccharides. Infect Immun 2005; 73: 3790-3793. https://doi.org/10.1128/IAI.73.6.3790-3793.2005
  9. Ringqvist E, Palm JE, Skarin H, Hehl AB, Weiland M, Davids BJ, Reiner DS, Griffiths WJ, Eckmann L, Gillin FD, Svard SG. Release of metabolic enzymes by Giardia in response to interaction with intestinal epithelial cells. Mol Biochem Parasitol 2008; 159: 85-91. https://doi.org/10.1016/j.molbiopara.2008.02.005
  10. Kucknoor AS, Mundodi V, Alderete JF. The proteins secreted by Trichomonas vaginalis and vaginal epithelial cell response to secreted and episomally expressed AP65. Cell Microbiol 2007; 9: 2586-2597. https://doi.org/10.1111/j.1462-5822.2007.00979.x
  11. Lorenzo-Morales J, Ortega-Rivas A, Foronda P, Abreu-Acosta N, Ballart D, Martinez E, Valladares B. RNA interference (RNAi) for the silencing of extracellular serine proteases genes in Acanthamoeba: molecular analysis and effect on pathogenecity. Mol Biochem Parasitol 2005; 144: 10-15. https://doi.org/10.1016/j.molbiopara.2005.07.001
  12. Na BK, Cho JH, Song CY, Kim TS. Degradation of immunoglobulins, protease inhibitors and interleukin-1 by a secretory proteinase of Acanthamoeba castellanii. Korean J Parasitol 2002; 40: 93-99. https://doi.org/10.3347/kjp.2002.40.2.93
  13. Huang JM, Lin WC, Li SC, Shih MH, Chan WC, Shin JW, Huang FC. Comparative proteomic analysis of extracellular secreted proteins expressed by two pathogenic Acanthamoeba castellanii clinical isolates and a non-pathogenic ATCC strain. Exp Parasitol 2016; 166: 60-67. https://doi.org/10.1016/j.exppara.2016.03.018
  14. Bahk YY, Kim SA, Kim JS, Euh HJ, Bai GH, Cho SN, Kim YS. Antigens secreted from Mycobacterium tuberculosis: identification by proteomics approach and test for diagnostic marker. Proteomics 2004; 4: 3299-3307. https://doi.org/10.1002/pmic.200400980
  15. Gobom J, Nordhoff E, Mirgorodskaya E, Ekman R, Roepstorff P. Sample purification and preparation technique based on nanoscale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry. J Mass Spectrom 1999; 34: 105-116. https://doi.org/10.1002/(SICI)1096-9888(199902)34:2<105::AID-JMS768>3.0.CO;2-4
  16. Quiocho FA. Atomic structures of periplasmic binding proteins and the high-affinity active transport systems in bacteria. Philos Trans R Soc Lond B Biol Sci 1990; 326: 341-351. https://doi.org/10.1098/rstb.1990.0016
  17. Tam R, Saier MH Jr. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol Rev 1993; 57: 320-346.
  18. Kervella M, Pages JM, Pei Z, Grollier G, Blaser MJ, Fauchere JL. Isolation and characterization of two Campylobacter glycine-extracted proteins that bind to HeLa cell membranes. Infect Immun 1993; 61: 3440-3448.
  19. Lun S, Bishai WR. Characterization of a novel cell wall-anchored protein with carboxylesterase activity required for virulence in Mycobacterium tuberculosis. J Biol Chem 2007; 282: 18348-18356. https://doi.org/10.1074/jbc.M700035200
  20. Hyde JE. Targeting purine and pyrimidine metabolism in human apicomplexan parasites. Curr Drug Targets 2007; 8: 31-47. https://doi.org/10.2174/138945007779315524
  21. Park S, Choi SG, Yoo SM, Son JH, Jung YK. Choline dehydrogenase interacts with SQSTM1/p62 to recruit LC3 and stimulate mitophagy. Autophagy 2014; 10: 1906-1920. https://doi.org/10.4161/auto.32177

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