{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Marothia M"],"funding":["Science and Engineering Research Board","Indian Council of Medical Research","Ministry of Education and Science of the Russian Federation","Department of Biotechnology, Ministry of Science and Technology, India"],"pagination":["109918"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11134565"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["27(6)"],"pubmed_abstract":["Malaria parasite invasion to host erythrocytes is mediated by multiple interactions between merozoite ligands and erythrocyte receptors that contribute toward the development of disease pathology. Here, we report a novel antigen <i>Plasmodium</i> prohibitin \"<i>Pf</i>PHB2\" and identify its cognate partner \"Hsp70A1A\" in host erythrocyte that plays a crucial role in mediating host-parasite interaction during merozoite invasion. Using small interfering RNA (siRNA)- and glucosamine-6-phosphate riboswitch (glmS) ribozyme-mediated approach, we show that loss of Hsp70A1A in red blood cells (RBCs) or <i>Pf</i>PHB2 in infected red blood cells (iRBCs), respectively, inhibit <i>Pf</i>PHB2-Hsp70A1A interaction leading to invasion inhibition. Antibodies targeting <i>Pf</i>PHB2 and monoclonal antibody t"],"journal":["iScience"],"pubmed_title":["Targeting <i>Pf</i>Prohibitin 2-Hu-Hsp70A1A complex as a unique approach towards malaria vaccine development."],"pmcid":["PMC11134565"],"funding_grant_id":["IRHPA IPA/2020/000007","075-15-2022-301"],"pubmed_authors":["Kumari G","Biswas S","Saini M","Ramalingam S","Shoaib R","Anand S","Bhowmick IP","Abdulhameed Almuqdadi HT","Ranganathan A","Marothia M","Kahlon AK","Shevtsov M","Maurya P","Garg S","Behl A","Goswami B","Munjal A","Singh S","Gupta P"],"additional_accession":[]},"is_claimable":false,"name":"Targeting <i>Pf</i>Prohibitin 2-Hu-Hsp70A1A complex as a unique approach towards malaria vaccine development.","description":"Malaria parasite invasion to host erythrocytes is mediated by multiple interactions between merozoite ligands and erythrocyte receptors that contribute toward the development of disease pathology. Here, we report a novel antigen <i>Plasmodium</i> prohibitin \"<i>Pf</i>PHB2\" and identify its cognate partner \"Hsp70A1A\" in host erythrocyte that plays a crucial role in mediating host-parasite interaction during merozoite invasion. Using small interfering RNA (siRNA)- and glucosamine-6-phosphate riboswitch (glmS) ribozyme-mediated approach, we show that loss of Hsp70A1A in red blood cells (RBCs) or <i>Pf</i>PHB2 in infected red blood cells (iRBCs), respectively, inhibit <i>Pf</i>PHB2-Hsp70A1A interaction leading to invasion inhibition. Antibodies targeting <i>Pf</i>PHB2 and monoclonal antibody t","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jun","modification":"2026-07-15T07:52:15.909Z","creation":"2026-07-01T03:07:53.248Z"},"accession":"S-EPMC11134565","cross_references":{"pubmed":["38812541"],"doi":["10.1016/j.isci.2024.109918"]}}