Evolution of pH buffers and water homeostasis in eukaryotes: homology between humans and Acanthamoeba proteins

Papers of special note have been highlighted as: •• of considerable interest

References

• 1 Kaplan LJ, Frangos S. Clinical review: acid–base abnormalities in the intensive care unit – part II. Critical Care 9(2), 198–203 (2005).
  MedlineGoogle Scholar
• 2 Popkin BM, D'Anci KE, Rosenberg IH. Water, hydration and health. Nutr. Rev. 68(8), 439–458 (2010).
  MedlineGoogle Scholar
• 3 McKenna R, Frost SC. Overview of the carbonic anhydrase family. Subcell. Biochem. 75, 3–5 (2014).
  Medline CASGoogle Scholar
• 4 Breton S. The cellular physiology of carbonic anhydrases. JOP 2(Suppl. 4), 159–64 (2001).
  Medline CASGoogle Scholar
• 5 Elkintob JR. Symposium on regulation of the cardiovascular system in health and disease: regulation of water and electrolytes. Circulation 21, 1184–1192 (1960).
  MedlineGoogle Scholar
• 6 Ribatti D, Ranieri G, Annese T, Nico B. Aquaporins in cancer. Biochim. Biophys. Acta. 1840(5), 1550–1553 (2013).
  MedlineGoogle Scholar
• 7 Kaldenhoff R, Kai L, Uehlein N. Aquaporins and membrane diffusion of CO₂ in living organisms. Biochim. Biophys. Acta. 1840(5), 1592–1595 (2014).
  Medline CASGoogle Scholar
• 8 Finn RN, Cerdà J. Evolution and functional diversity of aquaporins. Biol. Bull. 229(1), 6–23 (2015). •• Clues toward the expanding list of chemical and molecules that permeate the central pore of aquaporins (AQPs), and the unexpected diversity of water channel genes in archaea and bacteria. Additionally, it brings attention toward major grades of AQPs in eukaryota, together with the discussion of AQPs in vertebrates.
  Medline CASGoogle Scholar
• 9 Capasso C, Supuran CT. Bacterial, fungal and protozoan carbonic anhydrases as drug targets. Expert Opin. Ther. Targets 19(12), 1689–1704 (2015). •• Refers that carbonic anhydrase (CA) is not a validated drug target in the microorganism as yet, which strengthens our rationale of targeting it in Acanthamoeba. As resistance to the clinically used anti-infective is a serious healthcare problem worldwide, inhibition of parasite CA may constitute an alternative approach for obtaining such agents with novel mechanisms of action, has been proposed in this reference.
  Medline CASGoogle Scholar
• 10 Baig AM, Rana Z, Mannan MM, Effendi V, Ahmad HR. Forte of bioinformatics computational tools in identification of targets of digitalis in unicellular eukaryotes: featuring Acanthamoeba castellanii. EC Microbiol. 6, 831–844 (2016).
  Google Scholar
• 11 Baig AM, Ahmad HR. Evidence of a M1-muscarinic GPCR homolog in unicellular eukaryotes: featuring Acanthamoeba spp bioinformatics 3D-modelling and experimentation. J. Recept. Signal Transduct. Res. 7, 1–9 (2017). •• We used the bioinformatic tools for 3D structurally homology done in this paper that is a novel way to determine the ligand-binding cleft in receptors and proteins.
  Google Scholar
• 12 Baig AM, Rana Z, Mannan MM, Sumayaaya T, Ahmad HR. Antibiotic effects of loperamide: homology of human targets of loperamide with targets in Acanthamoeba spp. Recent Pat. Antiinfect. Drug Discov. 12(1), 44–60 (2017). •• Like acetazolamide, brinzolamide and mannitol used by our study, the above papers show loperamide that is known as a USA FDA-approved drug to have covert anti-infective effects against Acanthamoeba spp.
  Medline CASGoogle Scholar
• 13 AmoebaDB: The Amoeba Genomics Resource. amoebaDB.org.
  Google Scholar
• 14 Marciano-Cabral F, Cabral G. Acanthamoeba spp. as agents of disease in humans. Clin. Microbiol. Rev. 16, 273–307 (2003).
  MedlineGoogle Scholar
• 15 Visvesvara GS, Moura H, Schuster FL. Pathogenic and opportunistic free-living amoebae: Acanthamoeba spp., Balamuthia mandrillaris, Naegleria fowleri, and Sappinia diploidea. FEMS Immunol. Med. Microbiol. 50, 1–26 (2007).
  Medline CASGoogle Scholar
• 16 Khan NA. Acanthamoeba: biology and increasing importance in human health. FEMS Microbiol. Rev. 30, 564–595 (2006). •• Our study compared the homology of pH and water homeostasis-regulating proteins and enzyme in a primitive eukaryotes. This reference shows the evolutionary distance between Acanthamoeba and human as species.
  MedlineGoogle Scholar
• 17 Baker W, van den Broek A, Camon E et al. The EMBL nucleotide sequence database. Nucleic Acids Res. 32, D27–D30 (2002).
  Google Scholar
• 18 UniProt Consortium. UniProt: a hub for protein information. Nucleic Acids Res. 43, D204–D212 (2015).
  MedlineGoogle Scholar
• 19 Kelley LA, Mezulis S, Yates CM, Wass MN, Sternberg MJ. The Phyre2 web portal for protein modeling, prediction and analysis. Nat. Protoc. 10(6), 845–858 (2015).
  Medline CASGoogle Scholar
• 20 Marco B, Stefan B, Andrew W et al. SWISS MODEL: modelling protein tertiary and quaternary structure using evolutionary information. Nucleic Acids Res. 42, W252–W258 (2014). •• This web-based tool is a very powerful source that compares the structure of protein that is desired to be compared.
  MedlineGoogle Scholar
• 21 Wass MN, Kelley LA, Sternberg MJ. 3DLigandSite: predicting ligand-binding sites using similar structures. Nucleic Acids Res. 38, W469–W473 (2010).
  Medline CASGoogle Scholar
• 22 Brunton LL, Chabner BA, Björn C. Goodman & Gilman's the Pharmacological Basis of Therapeutics (12th Edition). The McGraw-Hill Companies, Inc, NY, USA (2011).
  Google Scholar
• 23 Ganong WF, Barman SM, Barrett KE, Brooks HL, Boitano S. Ganong's Review of Medical Physiology (24th Edition). McGraw Hill Medical, New York, NY, USA (2012).
  Google Scholar
• 24 Wallace AC, Laskowski RA, Thornton JM. LIGPLOT: a program to generate schematic diagrams of protein–ligand interactions. Protein Eng. 8, 127–134 (1996).
  Google Scholar
• 25 Kumar A, Khanna R, Srivastava RK, Ali I, Wadhwani P. Mannitol an adjuvant in local anaesthetic solution: recent concept & changing trends (review). J. Clin. Diagn. Res. 8(11), GE01-4 (2014).
  Google Scholar
• 26 Boriack-Sjodin PA, Zeitlin S, Chen HH et al. Structural analysis of inhibitor binding to human carbonic anhydrase II. Protein Sci. 7(12), 2483–2489 (1998). •• It structurally analyzes structure–activity relationships, rationalizes affinity trends observed during the development of brinzolamide (Azopt®), the newest CA inhibitor approved for the treatment of glaucoma.
  Medline CASGoogle Scholar
• 27 Herkel U, Pfeiffer N. Update on topical carbonic anhydrase inhibitors. Curr. Opin. Ophthalmol. 12(2), 88–93 (2001). •• The more physiologic pH of brinzolamide appears to be advantageous when used in glaucoma.
  Medline CASGoogle Scholar
• 28 Vullo D, Franchi M, Gallori E, Antel J, Scozzafava A, Supuran CT. Carbonic anhydrase inhibitors. Inhibition of mitochondrial isozyme V with aromatic and heterocyclic sulfonamides. J. Med. Chem. 47(5), 1272–1279 (2004).
  Medline CASGoogle Scholar