title: Human, vector and parasite Hsp90 proteins: A comparative bioinformatics analysis.
abstract: The treatment of protozoan parasitic diseases is challenging, and thus identification and analysis of new drug targets is important. Parasites survive within host organisms, and some need intermediate hosts to complete their life cycle. Changing host environment puts stress on parasites, and often adaptation is accompanied by the expression of large amounts of heat shock proteins (Hsps). Among Hsps, Hsp90 proteins play an important role in stress environments. Yet, there has been little computational research on Hsp90 proteins to analyze them comparatively as potential parasitic drug targets. Here, an attempt was made to gain detailed insights into the differences between host, vector and parasitic Hsp90 proteins by large-scale bioinformatics analysis. A total of 104 Hsp90 sequences were divided into three groups based on their cellular localizations; namely cytosolic, mitochondrial and endoplasmic reticulum (ER). Further, the parasitic proteins were divided according to the type of parasite (protozoa, helminth and ectoparasite). Primary sequence analysis, phylogenetic tree calculations, motif analysis and physicochemical properties of Hsp90 proteins suggested that despite the overall structural conservation of these proteins, parasitic Hsp90 proteins have unique features which differentiate them from human ones, thus encouraging the idea that protozoan Hsp90 proteins should be further analyzed as potential drug targets.
authors.affiliation: Research Unit in Bioinformatics (RUBi), Department of Biochemistry and Microbiology, Rhodes University, Grahamstown 6140, South Africa.
authors.forename: Ngonidzashe
authors.initials: N
authors.lastname: Faya
authors.affiliation: Research Unit in Bioinformatics (RUBi), Department of Biochemistry and Microbiology, Rhodes University, Grahamstown 6140, South Africa.
authors.forename: David L
authors.initials: DL
authors.lastname: Penkler
authors.affiliation: Research Unit in Bioinformatics (RUBi), Department of Biochemistry and Microbiology, Rhodes University, Grahamstown 6140, South Africa.
authors.forename: Özlem
authors.initials: Ö
authors.lastname: Tastan Bishop
keywords: GRAVY, grand average of hydropathicity; Heat shock proteins; Hop, Hsp70/90 organizing protein; Hsps, heat shock proteins; M domain, middle domain; ML, Maximum Likelihood; MSA, multiple sequence analysis; Motif analysis; NJ, Neighbor Joining; Phosphorylation; Physicochemical properties; Protozoan