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Dyn2 IP mass spectrometry dataset

ABSTRACT: Dyn2 IPs performed at Drexel and USF proteomics facility for "An Essential Adaptor for Apicoplast Fission and Inheritance in Malaria Parasites" paper. Associated with the additional dataset PXD062126.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Plasmodium Falciparum (ncbitaxon:5833)

SUBMITTER: Sabrina Absalon

PROVIDER: MSV000099148 | MassIVE |

SECONDARY ACCESSION(S): PXD068324

REPOSITORIES: MassIVE

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Publications

An Essential Adaptor for Apicoplast Fission and Inheritance in Malaria Parasites.

Blauwkamp James J Rajaram Krithika K Staggers Sophia R SR Harrigan Oliver O Doud Emma H EH Prigge Sean T ST Sun Stella Y SY Absalon Sabrina S

Research square 20250505

Blood-stage <i>Plasmodium falciparum</i> parasites rely on a non-photosynthetic plastid, the apicoplast, for survival, making it an attractive target for antimalarial intervention. Like the mitochondrion, the apicoplast cannot be generated <i>de novo</i> and must be inherited by daughter parasites during cell division. This inheritance relies on coordinated apicoplast positioning and fission, but the molecular mechanisms controlling these processes remain poorly understood. Here, we identify a p ...[more]

PMID: 40386403

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An Essential Factor for Apicoplast Fission and Inheritance in Malaria Parasites

Project description:Blood-stage Plasmodium falciparum parasites rely on a non-photosynthetic plastid, the apicoplast, for survival, making it an attractive target for antimalarial intervention. Like the mitochondrion, the apicoplast cannot be generated de novo and must be inherited by daughter parasites during cell division. This process relies on coordinated fission events, yet the molecular mechanisms remain poorly understood. Here, we identify a previously uncharacterized P. falciparum protein (Pf3D7_0613600), which we name PfAnchor, as a key regulator of apicoplast fission. Using Ultrastructure Expansion Microscopy (U-ExM), we show that PfAnchor localizes to the apicoplast throughout the asexual life cycle. Conditional depletion disrupts apicoplast fission, leading to incomplete cytokinesis and parasite death. Notably, loss of apicoplast branching via azithromycin treatment rescues these defects, underscoring Anchor’s specific role in apicoplast division. Immunoprecipitation further identifies an interaction with the dynamin-like GTPase PfDyn2, a key mediator of both apicoplast and mitochondrial fission, establishing PfAnchor as the first apicoplast-specific dynamin adaptor protein. Our findings define PfAnchor as an essential factor for apicoplast fission and inheritance in P. falciparum blood-stage parasites, highlighting parasite-specific organelle division as a potential vulnerability for therapeutic intervention.

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