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Molecular regulation of universal stress proteins in environmentally mediated schistosomiasis parasites

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dc.contributor.advisor Isokpehi, R.D.
dc.contributor.advisor Awofolu, Omotayo Rafiu Mbah, Andreas Nji 2014-04-24T12:15:21Z 2014-04-24T12:15:21Z 2014-04-24
dc.identifier.citation Mbah, Andreas Nji (2014) Molecular regulation of universal stress proteins in environmentally mediated schistosomiasis parasites, University of South Africa, Pretoria, <> en
dc.description.abstract Human schistosomiasis popularly known as bilharzias in many regions of Africa is a freshwater snail-transmitted disease caused by parasitic flatworms known as schistosomes. The growth and development of schistosomes typically requires developmental stages in multiple hosts and transmission stages in freshwater. These life cycle environments present a plethora of stressors. Certain gene families including heat shock proteins (HSPs/Hsps) and universal stress proteins (USPs) help schistosomes to respond to unfavourable conditions. The availability of genomes sequences information for Schistosoma japonicum, Schistosoma mansoni and Schistosoma haematobium provide unique research resources to apply bioinformatics analysis of its associated USPs to predict regulatory features from sequence analysis. The objectives of the research were to (i) Infer the biochemical and environmental regulation of universal stress proteins of Schistosoma species; (ii) Identify biological function relevant protein sequence and structure features for prioritized universal stress proteins from Schistosoma species; (iii) Determine the distinctive structural features of a predicted regulator of Schistosoma adenylate cyclase activity that has possible influence on the functioning of universal stress proteins. The findings revealed that (i) schistosomes USPs are hydrophilic and very reactive in the water environment or in aqueous phase, which seems adaptive with their immediate environment and developmental stages; (ii) The functions of Smp_076400 and Sjp_0058490 (Q86DW2) are regulated by conserved binding site residues and metallic ions ligands (Ca2+, Mg2+ and Zn2+), particularly Ca2+ predicted to bind to both USPs; (iii) The S. mansoni life cycle and stress resistance pathway protein (Smp_059340.1) is regulated by Ser53, Thr188, Gly210 and Asp207 residues. The overall scope has highlighted the role of bioinformatics in predicting exploitable regulatory features of schistosome universal stress proteins and biological pathways that might lead to identification of putative functional biomarkers of common environmental diseases. The findings of this research can be applicable to other areas of environmental health and environmental genomics. en
dc.format.extent 1 online resource (xxii, 141 leaves) :col. ill.
dc.language.iso en en
dc.subject Adenylate cyclase en
dc.subject ATP binding protein en
dc.subject Calcium en
dc.subject Chemical ligands en
dc.subject Environmental stressors en
dc.subject Biomolecular regulators en
dc.subject Praziquantel en
dc.subject Schistosoma en
dc.subject Schistosomiasis en
dc.subject Universal stress proteins en
dc.subject.ddc 614.43
dc.subject.lcsh Heat shock proteins
dc.subject.lcsh Schistosomatidae--Control
dc.subject.lcsh Schistosomatidae--Molecular aspects
dc.title Molecular regulation of universal stress proteins in environmentally mediated schistosomiasis parasites en
dc.type Thesis en
dc.description.department Environmental Sciences en (D. Litt et Phil. (Environmental Sciences)

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