bims-toxgon Biomed News
on Toxoplasma gondii metabolism
Issue of 2026–01–18
five papers selected by
Lakesh Kumar, BITS Pilani



  1. Microb Cell. 2025 ;12 299-313
      Post-translational modifications of microtubules regulate their stability and dynamics. Acetylation of α tubulin at lysine 40 (K40) by α -acetyltransferase ( α TAT) occurs on the luminal side of microtubules, stabilizes their structure, and plays essential roles in various cellular processes across eukaryotes. Apicomplexan parasites include the malaria-causing Plasmodium species and Toxoplasma gondii, both of which possess unusually stable subpellicular microtubules, a set of cytoskeletal filaments underlying the parasite's inner membrane complex. Interestingly, while Toxoplasma gondii and human-infecting Plasmodium species retain both K40 and α TAT, rodent-infecting Plasmodium species have lost α TAT, and K40 has been replaced by glutamine (Q40), a residue that can mimic acetylated lysine. Here, we investigate the role of microtubule acetylation in apicomplexan parasites by generating and characterizing genetic mutants in Plasmodium berghei and Toxoplasma gondii. In Plasmodium berghei, introduction of a Q40K mutation in α 1 tubulin did not affect parasite development or infectivity, suggesting that the absence of K40 acetylation is not detrimental. In Toxoplasma gondii, we confirmed that α TAT is responsible for microtubule acetylation but, contrary to previous reports, its deletion had no impact on parasite growth in vitro. Together, these results indicate that luminal K40 acetylation is not essential for microtubule function in either species, pointing to functional redundancy and highlighting the plasticity of cytoskeletal regulation in apicomplexan parasites.
    Keywords:  K40 acetylation; apicomplexan parasites; microtubule acetylation; parasite cytoskeleton; tubulin modifications
    DOI:  https://doi.org/10.15698/mic2025.12.863
  2. Life Sci Alliance. 2026 Apr;pii: e202503522. [Epub ahead of print]9(4):
      Apicomplexan parasites such as Plasmodium spp. and Toxoplasma gondii possess unique tubulin-based structures, including subpellicular microtubules and apical polar rings, which are essential for parasite motility, host cell invasion, and replication. Apicortin, a microtubule-associated protein, contains a doublecortin (DC) domain and a partial tubulin polymerization-promoting protein (TPPP) domain, both implicated in microtubule binding and stabilization. How tubulin-based structures are maintained is poorly understood, but it may involve Apicortin, so far found only in apicomplexans and the placozoan Trichoplax adhaerens Here, we investigated the location and function of Apicortin in Plasmodium berghei Live-cell imaging of a transgenic parasite line expressing GFP-tagged Apicortin showed its location at the apical end of invasive parasite stages within the mosquito vector. Super-resolution and expansion microscopy revealed that Apicortin forms a distinct ringlike structure in the apical complex region at the apical end. However, deletion of the Apicortin gene had no effect on parasite development, indicating that this protein is not essential. This suggests that there may be redundancy or compensatory functions in the mechanisms that stabilize the apical complex.
    DOI:  https://doi.org/10.26508/lsa.202503522
  3. bioRxiv. 2026 Jan 08. pii: 2026.01.08.698415. [Epub ahead of print]
      The apical polar ring (APR) is a defining cytoskeletal structure in apicomplexan parasites, critical for parasite morphology and host cell invasion. However, its molecular composition and function remain elusive in Plasmodium falciparum . Here, we identify and characterize PfAPR1 as an APR-resident protein. Conditional knockout of PfAPR1 reveals its essential role in asexual replication. Using iterative ultrastructure expansion microscopy (iU-ExM), we show that PfAPR1 predominantly localizes to the basal APR ring. Loss of PfAPR1 causes defects in daughter cell segmentation and subpellicular microtubules organization, while IMC formation and apical polarity are largely preserved. PfAPR1-KO parasites contact host red blood cells but fail to form a tight junction, resulting in a complete block in invasion. Using PfAPR1 as molecular bait, we identify additional APR proteins and delineate APR biogenesis with U-ExM. These findings define the molecular architecture and function of the APR in P. falciparum, highlighting it as a promising antimalarial target.
    DOI:  https://doi.org/10.64898/2026.01.08.698415
  4. mBio. 2026 Jan 13. e0344425
      Toxoplasma gondii exploits host phagocytes to disseminate systemically and establish infection in the central nervous system (CNS). Yet, the mechanisms governing the interaction between parasitized phagocytes and the brain endothelium remain elusive. Here, we show that T. gondii infection, but not parasite lysates, robustly induces transcriptional and secretory upregulation of the chemokine C-C motif ligand 5 (CCL5/RANTES) in primary brain endothelial cells and dendritic cells (DCs). This response was triggered by the parasite effector GRA15 through NF-κB signaling, while the effector TEEGR counteracted CCL5 induction in an MYR-translocon-dependent manner. In response to recombinant CCL5, infected DCs displayed increased hypermotility, chemotaxis toward CCL5 gradients, and enhanced transmigration across polarized endothelial monolayers. Intraperitoneally infected mice rapidly upregulated CCL5 in the blood and Ccl5 expression in the cerebral microvasculature, thereby increasing the adhesion of parasitized DCs and cerebral parasite loads. Pretreatment of mice with recombinant CCL5 dramatically elevated the sequestration of infected DCs, while treatment with the selective chemokine receptor 5 (CCR5) antagonist Maraviroc reverted sequestration. Together, these findings reveal that T. gondii co-opts the host CCL5/CCR5 axis via GRA15-mediated signaling to promote leukocyte-dependent dissemination and early colonization of the CNS.
    IMPORTANCE: The intracellular parasite Toxoplasma gondii invades immune cells to spread through the circulatory system, eventually reaching the brains of humans and animals. It is not well understood how parasitized immune cells interact with blood vessel walls, a process that ultimately helps Toxoplasma colonize the brain tissue. We found that when Toxoplasma infects the cells lining the blood vessels (endothelium), these produce C-C motif chemokine ligand 5 (CCL5), a potent signaling and attractant molecule. CCL5 production was triggered by a parasite-derived secreted protein, GRA15. CCL5 activated and attracted infected immune cells. In mice, the levels of CCL5 increased quickly in the brain microvasculature after infection, helping the infected immune cells adhere to brain vessels. When the effect of CCL5 was pharmacologically blocked, fewer infected cells sequestered in the brain vessels, lowering the parasite loads. These findings reveal a mechanism through which Toxoplasma manipulates host cells to produce factors that facilitate its colonization of the brain.
    Keywords:  (MeSH): host-pathogen; blood-brain barrier; central nervous system protozoal infections; chemokines; intracellular parasitism; leukocyte chemotaxis
    DOI:  https://doi.org/10.1128/mbio.03444-25
  5. Nucleic Acids Res. 2026 Jan 14. pii: gkaf1517. [Epub ahead of print]54(2):
      We report that Aurora B kinase-mediated phosphorylation is essential for BubR1 acetylation at lysine 250 (K250), a modification required to preserve the mitotic checkpoint complex (MCC) and ensure accurate chromosome segregation. This Aurora B-BubR1 acetylation axis provides a mechanistic explanation for how kinetochore-microtubule attachment status is transduced to spindle assembly checkpoint (SAC) activity. Aurora B phosphorylates BubR1 at Serine 39 (and Ser16) in response to unattachment, and this phosphorylation is indispensable for subsequent K250 acetylation. Using a monoclonal anti-AcK250 antibody in structured illumination microscopy, we demonstrate that BubR1 acetylation sustains the fibrous corona, as shown by the crescent-shaped expansion of ZW10 and MAD2 surrounding kinetochores. Loss of either CENP-E or BubR1 acetylation abolishes fibrous corona, indicating that the interaction between acetylated BubR1 and CENP-E connects lateral attachment with the prevention of premature corona disassembly until proper end-on attachment is achieved. Disruption of Aurora B-mediated phosphorylation compromises K250 acetylation, fibrous corona maintenance, and MCC stability, whereas expression of a K250 acetylation-mimetic BubR1 rescues these defects in S16A/S39A phosphorylation-deficient mutants. Together, our findings establish a phosphorylation-acetylation cascade in BubR1 as a critical SAC signaling pathway and identify this axis as a promising therapeutic target in cancers driven by chromosomal instability.
    DOI:  https://doi.org/10.1093/nar/gkaf1517