{"id":{"repo_id":"zulu","oai_identifier":"oai:uzspace.unizulu.ac.za:10530/1587"},"canonical_url":"https://search.dev.ndltd.org/etd/zulu/oai:uzspace.unizulu.ac.za:10530/1587","repository":{"repo_id":"zulu","name":"University of Zululand","base_url":"https://uzspace.unizulu.ac.za/server/oai/request"},"display":{"title":"Structural Characterization of the interaction between divalent cations and the novel Schistosoma mansoni Universal Stress Protein G4LZI3","abstract":"Approximately 200 000 people in sub-Saharan Africa lose their lives to schistosomiasis every year. This coupled with other severe Neglected Tropical Diseases, HIV/AIDS, malaria, tuberculosis and poverty, does not make the situation any better. Vaccines targeting this disease are still yet to be discovered and current treatment is becoming a problem as drug resistance has been reported. Thus, looking for an alternative treatment regimen is fast becoming a priority. This study took an interest in Universal Stress Proteins and focused on a novel G4LZI3 USP, which has been put forward as a possible candidate vaccine. A sufficient amount (0.518mg/ml) of recombinant G4LZI3 protein was successfully expressed using 0.5mM IPTG and subjected to a Nickel-NTA column for purification. The fractions were pooled together, concentrated down and used to investigate the binding of the protein with 3 metallic divalent cations using Isothermal Titration Calorimetry (ITC). Additionally, bioinformatics was employed to predict the secondary structure of the protein, generate a 3-dimensional model of the protein and use it for docking the divalent cations. Moreover, the interacting partners of the G4LZI3 protein were determined, thus giving a clue towards the function of the protein. Bioinformatics tools assisted in confirming Ca2+, Mg2+ and Zn2+ as putative ligands and additionally identified ATP, AMP and U20 as possible molecules that interact with the G4LZI3 USP protein. However, in vivo studies only showed interaction between Mg2+ and the protein. These results provide prospects for future studies toward drug discovery for schistosomiasis.","abstract_html":"Approximately 200 000 people in sub-Saharan Africa lose their lives to schistosomiasis every year. This coupled with other severe Neglected Tropical Diseases, HIV/AIDS, malaria, tuberculosis and poverty, does not make the situation any better. Vaccines targeting this disease are still yet to be discovered and current treatment is becoming a problem as drug resistance has been reported. Thus, looking for an alternative treatment regimen is fast becoming a priority. This study took an interest in Universal Stress Proteins and focused on a novel G4LZI3 USP, which has been put forward as a possible candidate vaccine. A sufficient amount (0.518mg/ml) of recombinant G4LZI3 protein was successfully expressed using 0.5mM IPTG and subjected to a Nickel-NTA column for purification. The fractions were pooled together, concentrated down and used to investigate the binding of the protein with 3 metallic divalent cations using Isothermal Titration Calorimetry (ITC). Additionally, bioinformatics was employed to predict the secondary structure of the protein, generate a 3-dimensional model of the protein and use it for docking the divalent cations. Moreover, the interacting partners of the G4LZI3 protein were determined, thus giving a clue towards the function of the protein. Bioinformatics tools assisted in confirming Ca2+, Mg2+ and Zn2+ as putative ligands and additionally identified ATP, AMP and U20 as possible molecules that interact with the G4LZI3 USP protein. However, in vivo studies only showed interaction between Mg2+ and the protein. These results provide prospects for future studies toward drug discovery for schistosomiasis.","abstract_has_math":false,"creators":["Masamba, Priscilla"],"institution":"University of Zululand","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":["Kappo, A.P"],"committee_chairs":[],"committee_members":[],"year":2017,"date_issued":"2017","date_published":"2017","updated_at":"2026-07-24T06:17:11Z","subjects":["docking --isothermal titratiuon calorimetry --neglected tropical deisease --praziquantel --Schistosoma mansoni --universal stress protein"],"languages":[],"rights":[],"rights_urls":["https://devspace.unizulu.ac.za/bitstreams/23bada10-14a2-4a2c-988d-ddd3d502b9c4/download"],"identifier_entries":[]},"links":{"outbound_url":null,"outbound_label":null,"outbound_source":null},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Kappo, A.P"]},{"key":"dc:creator","label":"Author","values":["Masamba, Priscilla"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.issued","label":"Date","values":["2017"]},{"key":"dc:publisher.institution","label":"Dc Publisher Institution","values":["University of Zululand"]},{"key":"dc:relation.isreferencedby","label":"Dc Relation Isreferencedby","values":["http://hdl.handle.net/10530/1587"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["docking --isothermal titratiuon calorimetry --neglected tropical deisease --praziquantel --Schistosoma mansoni --universal stress protein"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:rights","label":"Dc Rights","values":["https://devspace.unizulu.ac.za/bitstreams/23bada10-14a2-4a2c-988d-ddd3d502b9c4/download"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://devspace.unizulu.ac.za/bitstreams/497c9319-3c69-43e5-807e-f3506aa7dbe7/download"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Approximately 200 000 people in sub-Saharan Africa lose their lives to schistosomiasis every year. 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Moreover, the interacting partners of the G4LZI3 protein were determined, thus giving a clue towards the function of the protein. Bioinformatics tools assisted in confirming Ca2+, Mg2+ and Zn2+ as putative ligands and additionally identified ATP, AMP and U20 as possible molecules that interact with the G4LZI3 USP protein. However, in vivo studies only showed interaction between Mg2+ and the protein. 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