Structural and functional diversity of Entamoeba histolytica calcium-binding proteins
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REVIEW
Structural and functional diversity of Entamoeba histolytica calcium-binding proteins Sanjeev Kumar 1,2 & Shalini Mishra 3 & S. Gourinath 3 Received: 17 June 2020 / Accepted: 9 October 2020 # International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag GmbH Germany, part of Springer Nature 2020
Abstract Entamoeba histolytica (E. histolytica) is an etiological agent of human amoebic colitis, and it causes a high level of morbidity and mortality worldwide, particularly in developing countries. Ca2+ plays a pivotal role in amoebic pathogenesis, and Ca2+-binding proteins (CaBPs) of E. histolytica appear to be a major determinant in this process. E. histolytica has 27-EF-hand containing CaBPs, suggesting that this organism has complex Ca2+ signaling cascade. E. histolytica CaBPs share (29–47%) sequence identity with ubiquitous Ca2+binding protein calmodulin (CaM); however, they do not show any significant structural similarity, indicating lack of a typical CaM in this organism. Structurally, these CaBPs are very diverse among themselves, and perhaps such diversity allows them to recognize different cellular targets, thereby enabling them to perform a range of cellular functions. The presence of such varied signaling molecules helps parasites to invade host cells and advance in disease progression. In the past two decades, tremendous progress has been made in understanding the structure of E. histolytica CaBPs by using the X-ray or NMR method. To gain greater insight into the structural and functional diversity of these amoebic CaBPs, we analyzed and compiled all the available literature. Most of the CaBPs has about 150 amino acids with 4-EF hand or EF-hand-like sequences, similar to CaM. In a few cases, all the EF-hand motifs are not capable of binding Ca2+, suggesting them to be pseudo EF-hand motifs. The CaBPs perform diverse cellular signaling that includes cytoskeleton remodeling, phagocytosis, cell proliferation, migration of trophozoites, and GTPase activity. Overall, the structural and functional diversity of E. histolytica CaBPs compiled here may offer a basis to develop an efficient drug to counter its pathogenesis. Keywords Ca2+ . Signaling . CaM . CaBPs . Entamoeba histolytica
Introduction Ca2+ is a ubiquitous secondary messenger, involved in several intracellular processes (for example, cell division,
Sanjeev Kumar and Shalini Mishra contributed equally to this work. * Sanjeev Kumar [email protected] * S. Gourinath [email protected] Shalini Mishra [email protected] 1
Present address: Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC 29425, USA
2
Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA
3
School of Life Science Jawaharlal Nehru University, New Delhi 110067, India
differentiation, motility, contraction, secretion, and such), in almost all kinds of living organisms. The involvement of Ca2+ signaling has been observed in several human protozoan parasi
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