Search bioRxiv⌕ Search

bioRxiv · 10.64898/2026.01.21.700814

A versatile, marker-free platform for life cycle-wide imaging in Plasmodium falciparum via integration of an exogenous gene cassette into a conserved intergenic locus

Abstract

The development of a transgenic Plasmodium falciparum line that exhibits robust fluorescence throughout its life cycle in cultured cells and mosquito hosts is valuable for live imaging, tissue localization studies, and quantitative evaluations of parasite infectivity. In this study, we utilized Plasmodium-optimized genome editing to integrate an mCherry expression cassette into a specific intergenic locus without gene disruption; thereby successfully minimizing the physiological impact of exogenous gene introduction. The resulting transgenic parasite line, NF54-mCh, exhibited intense fluorescence across all developmental stages; including intraerythrocytic asexual and sexual blood stages; mosquito ookinete, oocyst, and sporozoite stages; and liver stages. Cultured NF54-mCh exhibited normal intraerythrocytic proliferation, gametocytogenesis, and gametocyte maturation, with efficient transmission to mosquito vectors. The marker brightness in salivary gland sporozoites allowed for visual, non-invasive identification of infected mosquitoes, thus facilitating dissection. Sporozoites dissected from salivary glands were highly infectious to livers in humanized mice; and allowed completion of the full life cycle, as evidenced by the appearance of ring-stage parasites in inoculated human erythrocytes. NF54-mCh serves as a parental line for performing additional genetic modifications, because the CRISPR/Cas9-based genome editing method is free of introduced drug resistance markers. The broader applicability of this strategy was validated by generating fluorescence reporter lines for use in the rodent malaria parasite model systems, Plasmodium berghei and Plasmodium yoelii. In summary, NF54-mCh represents a unique, versatile platform that will accelerate fundamental research and support the future development of innovative malaria control strategies, including studies on new vaccines and drug efficacy. IMPORTANCEA detailed understanding of the molecular and cellular biology of the human malaria parasite Plasmodium falciparum, particularly during infection processes, is essential for efforts in malaria control and elimination. In this study, we generated a marker-free transgenic P. falciparum line which exhibits constitutive, robust fluorescence throughout its developmental stages in erythrocytes, mosquitoes, and hepatocytes, without impairing parasite growth or fitness. The fluorescence marker gene was inserted into an intergenic locus and thus no genes were disrupted. The pfs47 gene is intact, which allows the parasites to evade the mosquito innate system; therefore, the parasite retains the ability for pfs47-dependent infection of refractory Anopheles strains. The transgenic parasites do not contain drug resistance markers, and thus there are no limitations for further genetic manipulation. This transgenic parasite line provides a powerful tool for the study of fundamental parasite infection mechanisms and for the molecular analysis of host-parasite interactions.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Sekine, T., Shinzawa, N., Kubota, R., Kobayashi, D., Okubo, Y., Itokawa, K., Isawa, H., Amino, H., Ishino, T.. 2026-01-21. A versatile, marker-free platform for life cycle-wide imaging in Plasmodium falciparum via integration of an exogenous gene cassette into a conserved intergenic locus. https://doi.org/10.64898/2026.01.21.700814

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related preprints

Cryo-EM Structure of Mycobacteriophage D29 Reveals a Specialized Portal-Capsid Junction and a Unique 13-Subunit Baseplate Collar

Mycobacteriophages are promising agents against drug-resistant mycobacterial infections, yet their structural organization and host-recognition mechanisms remain poorly understood. Here, we determined cryo-EM structures of the capsid, connector, tail tube, and baseplate of the lytic, broad-host-range mycobacteriophage D29, revealing a near-complete virion architecture. At the capsid-portal interface, five copies of the previously uncharacterized protein gp19.1 bridge adjacent capsid subunits around the dodecameric portal, potentially reinforcing the symmetry-mismatched vertex. At the baseplate, 13 copies of gp6 assemble into a collar surrounding the sixfold-symmetric gp23-gp27 core. Remarkably, this 6:13 symmetry mismatch is accommodated through six distinct gp6- gp27 interfaces involving 12 gp6 subunits, leaving one subunit largely disengaged from the core. This asymmetric organization produces a tilted, outward-flaring collar that presents an extensive surface with the potential to engage the host cell. Whole-cell binding and plaque-competition assays further implicate the gp6 collar and the flexible trimeric central fiber gp31 in host recognition. Together, these findings reveal distinct structural adaptations at symmetry-mismatched interfaces and provide a structural framework for understanding mycobacteriophage assembly and host engagement.

microbiology↗

A Luciferase Reporter of Ester Prodrug Delivery to the Cytosol of Intracellular Mycobacteria

The bacterial cell envelope restricts access to cytoplasmic targets and is a principal reason that otherwise potent antibacterial compounds fail in cells. Masking an anionic carboxylic acid as an ester is a common way to cross that barrier, but the strategy succeeds only if the target organism also hydrolyzes the ester once the compound arrives. These two requirements, permeation and intracellular unmasking, are rarely measured together in live bacterial cells, and existing reporters cannot specify where unmasking occurred. Here we describe a bioluminescent platform that resolves both steps in real time in live mycobacteria using carboxylate esters of D-luciferin. Luciferase requires that an ester both reach the bacterial cytoplasm and be hydrolyzed there, which makes light a compartment-specific readout of productive delivery. Across a series of alkyl esters in Mycobacterium smegmatis, chain length governed permeation while branching adjacent to the carbonyl governed esterase processing, indicating that the two parameters can be tuned independently. The n-butyl ester gave the strongest signal in broth, in infected macrophages, and in the pathogen Mycobacterium avium, whereas the tert-butyl ester was inert in Mycobacterium avium and unmasking of the whole series was attenuated at phagosomal pH. Ester activation is therefore both species- and compartment-dependent, and masking groups are best selected in the organism and environment in which they must act.

microbiology↗

Flexible phosphorus allocation to the phosphoproteome underpins diatom regulatory adaptations to fluctuating phosphate supply

Diatoms are major drivers of marine phosphorus (P) cycling and are highly adapted to cope with variable P supply. P-starved diatoms can sense increases in P availability within seconds, accumulating this limiting resource through luxury polyphosphate (polyP) storage. Yet, how diatoms coordinate such responses is unknown. Protein phosphorylation is a core mechanism for environmental signal transduction in eukaryotes, but how cells balance investment in protein phosphorylation against competing physiological demands during P limitation is poorly understood. Here, we characterise system-wide remodelling of the Phaeodactylum tricornutum phosphoproteome in response to P deficiency and subsequent resupply. We identify widespread proteome dephosphorylation across 44% of phosphosites, revealing a previously unrecognised P-sparing strategy in marine phytoplankton. Following P resupply, diatoms orchestrate extensive phosphoproteome reprogramming within minutes. We characterise previously unrecognized components for early recovery from P limitation, including a novel environmentally prevalent intracellular H+/phosphate transporter strongly conserved in diverse diatoms. We also identify a vacuolar Ca2+-dependent protein kinase (CDPK) associated with polyP-storage granules. Mutant and inhibitor analyses demonstrate a role for Ca2+- and CDPK-signalling in the regulation of luxury polyP accumulation. Our findings reveal that recovery from P starvation is mediated by rapid phosphoregulatory control of intracellular P trafficking, organellar ATP generation coupled with luxury P storage, enabling diatoms to exploit newly available P and thrive in fluctuating P regimes. Collectively, our study uncovers the phosphoproteome as a flexible intracellular P reservoir and establishes mechanistic links between intracellular P budgeting, signalling and the marine P cycle.

microbiology↗