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Future Microbiol. 2018 Feb;13:195-207. doi: 10.2217/fmb-2017-0116. Epub 2018 Jan 11.

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

Author information

1
Department of Biological & Biomedical Sciences, Aga Khan University, Sindh, Stadium Road, Karachi, 78400 Sindh, Pakistan.
2
Dr Panjwani Center for Molecular Medicine & Drug Research, University of Karachi, 75270, Sindh, Pakistan.

Abstract

AIM:

This study intended to trace the evolution of acid-base buffers and water homeostasis in eukaryotes. Acanthamoeba castellanii  was selected as a model unicellular eukaryote for this purpose. Homologies of proteins involved in pH and water regulatory mechanisms at cellular levels were compared between humans and A. castellanii.

MATERIALS & METHODS:

Amino acid sequence homology, structural homology, 3D modeling and docking prediction were done to show the extent of similarities between carbonic anhydrase 1 (CA1), aquaporin (AQP), band-3 protein and H+ pump. Experimental assays were done with acetazolamide (AZM), brinzolamide and mannitol to observe their effects on the trophozoites of  A. castellanii.

RESULTS:

The human CA1, AQP, band-3 protein and H+-transport proteins revealed similar proteins in Acanthamoeba. Docking showed the binding of AZM on amoebal AQP-like proteins.  Acanthamoeba showed transient shape changes and encystation at differential doses of brinzolamide, mannitol and AZM.  Conclusion: Water and pH regulating adapter proteins in Acanthamoeba and humans show significant homology, these mechanisms evolved early in the primitive unicellular eukaryotes and have remained conserved in multicellular eukaryotes.

KEYWORDS:

Acanthamoeba castellanii; aquaporin; carbonic anhydrase; evolution of acid–base buffers in eukaryotes; water homeostasis

PMID:
29322818
DOI:
10.2217/fmb-2017-0116
[Indexed for MEDLINE]

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