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A Comparative Approach to Characterize the Landscape of Host-Pathogen Protein-Protein Interactions
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Human, vector and parasite Hsp90 proteins: A comparative bioinformatics analysis.

Ngonidzashe Faya1, David L Penkler1, Özlem Tastan Bishop1

  • 1Research Unit in Bioinformatics (RUBi), Department of Biochemistry and Microbiology, Rhodes University, Grahamstown 6140, South Africa.

FEBS Open Bio
|January 22, 2016
PubMed
Summary

Protozoan parasitic diseases are difficult to treat. This study identified unique features in parasitic heat shock protein 90 (Hsp90) compared to human Hsp90, suggesting Hsp90 as a potential drug target.

Keywords:
GRAVY, grand average of hydropathicityHeat shock proteinsHop, Hsp70/90 organizing proteinHsps, heat shock proteinsM domain, middle domainML, Maximum LikelihoodMSA, multiple sequence analysisMotif analysisNJ, Neighbor JoiningPhosphorylationPhysicochemical propertiesProtozoan

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Area of Science:

  • Bioinformatics
  • Parasitology
  • Drug Discovery

Background:

  • Protozoan parasitic diseases pose significant treatment challenges.
  • Heat shock proteins (Hsps), particularly Hsp90, are crucial for parasite survival under stress.
  • Limited comparative computational research exists on parasitic Hsp90 as drug targets.

Purpose of the Study:

  • To perform a large-scale bioinformatics analysis of Hsp90 proteins from hosts, vectors, and parasites.
  • To identify unique features of parasitic Hsp90 proteins that differentiate them from human Hsp90.
  • To evaluate the potential of parasitic Hsp90 as novel drug targets.

Main Methods:

  • Collected and analyzed 104 Hsp90 protein sequences.
  • Classified sequences based on cellular localization (cytosolic, mitochondrial, ER) and parasite type (protozoa, helminth, ectoparasite).
  • Conducted primary sequence analysis, phylogenetic tree calculations, motif analysis, and physicochemical property assessment.

Main Results:

  • Parasitic Hsp90 proteins exhibit unique characteristics compared to human Hsp90.
  • Despite overall structural conservation, distinct features were identified in parasitic Hsp90.
  • Analysis supported the potential of Hsp90 as a viable drug target in parasitic infections.

Conclusions:

  • Comparative bioinformatics analysis reveals unique features in parasitic Hsp90 proteins.
  • These unique features highlight parasitic Hsp90 as a promising target for novel anti-parasitic drug development.
  • Further investigation into protozoan Hsp90 is warranted for therapeutic strategies.