{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Bekkering ET"],"funding":["Dutch Research Council (NWO)","NIGMS NIH HHS"],"pubmed_abstract":["The Pfs230:Pfs48/45 complex forms the basis for leading malaria transmission-blocking vaccine candidates, yet little is known about its molecular assembly. Here, we used cryogenic electron microscopy to elucidate the structure of the endogenous Pfs230:Pfs48/45 complex bound to six potent transmission-blocking antibodies. Pfs230 consists of multiple domain clusters rigidified by interactions mediated through insertion domains. Membrane-anchored Pfs48/45 forms a disc-like structure and interacts with a short C-terminal peptide on Pfs230 that is critical for Pfs230 membrane-retention <i>in vivo</i>. Interestingly, membrane retention through this interaction is not essential for transmission to mosquitoes, suggesting that complex disruption is not a mode of action for transmission-blocking ant"],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2025.02.14.638310"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11844449"],"repository":["biostudies-literature"],"pubmed_title":["Structure of endogenous Pfs230:Pfs48/45 in complex with potent malaria transmission-blocking antibodies."],"pmcid":["PMC11844449"],"funding_grant_id":["R01 GM129325","VI.Veni.222.381"],"pubmed_authors":["Jansen PWTC","Takashima E","Heide F","Jore MM","Proellochs NI","Bekkering ET","Maeda A","Ivanochko D","Vermeulen M","Yuguchi T","Jackman M","Inklaar MR","Yoo R","van Daalen RC","Rubinstein JL","Julien JP","Stoter R","Wanders OT","van Gemert GJ","Andrade CM","Bousema T","Hailemariam S","Kooij TWA"],"additional_accession":[]},"is_claimable":false,"name":"Structure of endogenous Pfs230:Pfs48/45 in complex with potent malaria transmission-blocking antibodies.","description":"The Pfs230:Pfs48/45 complex forms the basis for leading malaria transmission-blocking vaccine candidates, yet little is known about its molecular assembly. Here, we used cryogenic electron microscopy to elucidate the structure of the endogenous Pfs230:Pfs48/45 complex bound to six potent transmission-blocking antibodies. Pfs230 consists of multiple domain clusters rigidified by interactions mediated through insertion domains. Membrane-anchored Pfs48/45 forms a disc-like structure and interacts with a short C-terminal peptide on Pfs230 that is critical for Pfs230 membrane-retention <i>in vivo</i>. Interestingly, membrane retention through this interaction is not essential for transmission to mosquitoes, suggesting that complex disruption is not a mode of action for transmission-blocking ant","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jun","modification":"2026-07-03T03:25:40.123Z","creation":"2025-04-07T07:50:03.757Z"},"accession":"S-EPMC11844449","cross_references":{"pubmed":["39990443"],"doi":["10.1101/2025.02.14.638310"]}}