biostudies-literatureMarothia MScience and Engineering Research BoardIndian Council of Medical ResearchMinistry of Education and Science of the Russian FederationDepartment of Biotechnology, Ministry of Science and Technology, India109918https://www.ebi.ac.uk/biostudies/studies/S-EPMC11134565biostudies-literatureUnknown27(6)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 tiScienceTargeting <i>Pf</i>Prohibitin 2-Hu-Hsp70A1A complex as a unique approach towards malaria vaccine development.PMC11134565IRHPA IPA/2020/000007075-15-2022-301Kumari GBiswas SSaini MRamalingam SShoaib RAnand SBhowmick IPAbdulhameed Almuqdadi HTRanganathan AMarothia MKahlon AKShevtsov MMaurya PGarg SBehl AGoswami BMunjal ASingh SGupta PfalseTargeting <i>Pf</i>Prohibitin 2-Hu-Hsp70A1A complex as a unique approach towards malaria vaccine development.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 t2024-01-01T00:00:00Z2024 Jun2026-07-15T07:52:15.909Z2026-07-01T03:07:53.248ZS-EPMC111345653881254110.1016/j.isci.2024.109918