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Bekkering, E. T.

Publications and source records attributed to Bekkering, E. T..

4 recordsLinked to original sources

A silent intergenic locus for efficient and versatile transgene expression in Plasmodium falciparum

Genetically modified Plasmodium falciparum parasites expressing transgenes such as fluorescent markers are crucial tools for malaria research. However, current reporter lines often rely on integrated transgene constructs that disrupt the coding sequence of a native gene, potentially affecting progression in the life cycle of the tool parasite line. We identified six candidate Silent Intergenic Loci (SILs): putatively editable intergenic regions without transcriptional activity, where gene insertions occurred in P. falciparum after its divergence from Plasmodium berghei and Plasmodium vivax. We characterised the largest candidate SIL on chromosome 12, SIL12, by integration of a constitutively expressed cytosolic mScarlet reporter. The resulting PfRed12 parasites progressed normally throughout the life cycle, from asexual blood-stage replication to mosquito stages and subsequent liver infection. Importantly, they infected both Anopheles stephensi and Anopheles coluzzii mosquitoes. PfRed12 parasites displayed bright fluorescence in both blood and mosquito stages, making them well suited for live visualisation of parasite transmission. In addition, we used two CRISPR-Cas9 target sites in the mScarlet cassette, one of which we purposely added, to perform efficient re-editing of the transgene. As a proof of concept, we re-edited PfRed12 parasites and integrated an apicoplast metabolic bypass construct, an inducible gametocyte producer construct, and two mNeonGreen reporter constructs. Together, our findings demonstrate that SIL12 permits stable transgene expression without compromising parasite development throughout the life cycle. We established PfRed12 as a new reporter line to study blood- and mosquito-stage development and as a versatile parental line for further genetic engineering.

microbiology↗

Plasmodium falciparum stomatin-like protein forms a putative complex with a metalloprotease in distinct mitochondrial loci

Withdrawal statementThis manuscript has been withdrawn owing to a duplicate posting of manuscript number BIORXIV/2024/604071. This was a technical error for which the authors are not responsible, and this DOI for the work should not be cited as reference. The record is retained here for purposes of transparency. If you have any questions, please contact the corresponding author. The correct preprint can be found at doi: 10.1101/2024.07.18.604071

microbiology↗

Structure of endogenous Pfs230:Pfs48/45 in complex with potent malaria transmission-blocking antibodies

The Pfs230:Pfs48/45 complex forms the basis for leading malaria transmission-blocking vaccine candidates, yet li]le 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 in vivo. 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 antibodies. Analyses of Pfs48/45-and Pfs230-targeted antibodies identify conserved epitopes on the Pfs230:Pfs48/45 complex and provides a structural paradigm for complement-dependent activity of Pfs230-targeting antibodies. Altogether, the antibody-bound Pfs230:Pfs48/45 structure presented improves our molecular understanding of this biological complex, informing the development of next-generation Plasmodium falciparum transmission-blocking interventions.

molecular biology↗

The role of stomatin-like protein (STOML) in Plasmodium falciparum

Members of the Stomatin, Prohibitin, Flotillin and HflK/C (SPFH) protein family form large membrane anchored or spanning complexes and are involved in various functions in different organelles. The human malaria causing parasite Plasmodium falciparum harbors four SPFH proteins, including prohibitin 1 and 2, prohibitin-like protein (PHBL), and stomatin-like protein (STOML), which all localize to the parasite mitochondrion. In the murine model parasite Plasmodium berghei, STOML appears essential for asexual blood-stage (ABS) development and is localized to puncta on mitochondrial branching points in oocyst stages. In this study, we show that deletion of STOML causes a significant growth defect and slower ABS development, while sexual-stage development remains unaffected. Parasites lacking STOML were not more sensitive to respiratory chain targeting drugs, rendering a function of STOML in respiratory chain assembly unlikely. Epitope tagging of endogenous STOML revealed a distinct punctate localization on branching points and endings of the ABS mitochondrial network. STOML resides in a large protein complex and pulldown experiments identified a zinc dependent metalloprotease, FtsH, as a likely interaction partner. The predicted AlphaFold2 structure of STOML shows high similarity with the bacterial HflK/C, which has been shown to form a large vault-like structure around bacterial FtsH hexamers. Combined, our results suggest that a similar STOML-FtsH complex localized to specific loci of P. falciparum mitochondria facilitate the parasites ABS development.

microbiology↗