Human, vector and parasite Hsp90 proteins: A comparative bioinformatics analysis
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 a...
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| Format: | Article |
| Language: | English |
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Wiley
2015-01-01
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| Series: | FEBS Open Bio |
| Subjects: | |
| Online Access: | https://doi.org/10.1016/j.fob.2015.11.003 |
| _version_ | 1811186255004696576 |
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| author | Ngonidzashe Faya David L. Penkler Özlem Tastan Bishop |
| author_facet | Ngonidzashe Faya David L. Penkler Özlem Tastan Bishop |
| author_sort | Ngonidzashe Faya |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-11T13:42:25Z |
| format | Article |
| id | doaj.art-dba2b382955f4dea825026a3e7f4f50e |
| institution | Directory Open Access Journal |
| issn | 2211-5463 |
| language | English |
| last_indexed | 2024-04-11T13:42:25Z |
| publishDate | 2015-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | FEBS Open Bio |
| spelling | doaj.art-dba2b382955f4dea825026a3e7f4f50e2022-12-22T04:21:12ZengWileyFEBS Open Bio2211-54632015-01-015191692710.1016/j.fob.2015.11.003Human, vector and parasite Hsp90 proteins: A comparative bioinformatics analysisNgonidzashe Faya0David L. Penkler1Özlem Tastan Bishop2Research Unit in Bioinformatics (RUBi), Department of Biochemistry and Microbiology, Rhodes University, Grahamstown 6140, South AfricaResearch Unit in Bioinformatics (RUBi), Department of Biochemistry and Microbiology, Rhodes University, Grahamstown 6140, South AfricaResearch Unit in Bioinformatics (RUBi), Department of Biochemistry and Microbiology, Rhodes University, Grahamstown 6140, South AfricaThe 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.https://doi.org/10.1016/j.fob.2015.11.003Heat shock proteinsPhysicochemical propertiesMotif analysisPhosphorylationProtozoan |
| spellingShingle | Ngonidzashe Faya David L. Penkler Özlem Tastan Bishop Human, vector and parasite Hsp90 proteins: A comparative bioinformatics analysis FEBS Open Bio Heat shock proteins Physicochemical properties Motif analysis Phosphorylation Protozoan |
| title | Human, vector and parasite Hsp90 proteins: A comparative bioinformatics analysis |
| title_full | Human, vector and parasite Hsp90 proteins: A comparative bioinformatics analysis |
| title_fullStr | Human, vector and parasite Hsp90 proteins: A comparative bioinformatics analysis |
| title_full_unstemmed | Human, vector and parasite Hsp90 proteins: A comparative bioinformatics analysis |
| title_short | Human, vector and parasite Hsp90 proteins: A comparative bioinformatics analysis |
| title_sort | human vector and parasite hsp90 proteins a comparative bioinformatics analysis |
| topic | Heat shock proteins Physicochemical properties Motif analysis Phosphorylation Protozoan |
| url | https://doi.org/10.1016/j.fob.2015.11.003 |
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