bims-toxgon Biomed News
on Toxoplasma gondii metabolism
Issue of 2026–01–11
seven papers selected by
Lakesh Kumar, BITS Pilani



  1. Int J Biol Macromol. 2026 Jan 02. pii: S0141-8130(25)10544-8. [Epub ahead of print]339(Pt 2): 149987
      The ubiquitin-like protein UBL5 plays conserved roles in pre-mRNA splicing across eukaryotes, yet its biological functions in the apicomplexan parasite Toxoplasma gondii remain unknown. Here, Our findings characterize TgUBL5 as an important regulator contributing to parasite proliferation, invasion, and acute virulence. Conditional depletion of TgUBL5 severely impairs tachyzoite growth, gliding motility, and host cell invasion, while abolishing pathogenicity during acute infection in BALB/c mice under IAA treatment. Co-immunoprecipitation assays reveal a direct interaction between TgUBL5 and the U5 snRNP-associated splicing factor TgSART1, whose degradation similarly disrupts parasite viability and virulence. RNA-seq profiling demonstrates that TgSART1 ablation triggers genome-wide splicing defects, predominantly intron retention, concomitant with transcriptional downregulation of key virulence effectors (ROP, MIC, RON, and SRS families). This SART1-dependent splicing defect phenocopies the invasion defect and virulence attenuation seen upon TgUBL5 depletion, suggesting that while TgSART1 directly regulates essential splicing, the virulence phenotype involves both factors, with TgUBL5 potentially stabilizing TgSART1. Our study uncovers a link between splicing regulation involving ubiquitin-like proteins and parasite infectivity.
    Keywords:  SART1; Splicing factor; Toxoplasma gondii; UBL5; Virulence
    DOI:  https://doi.org/10.1016/j.ijbiomac.2025.149987
  2. Trends Parasitol. 2026 Jan 08. pii: S1471-4922(25)00376-9. [Epub ahead of print]
      Recent studies by Romano et al. and Mehra et al. reveal that Toxoplasma gondii actively connects its parasitophorous vacuole to the host endoplasmic reticulum. Through a parasitic secretory relay involving dense granule and rhoptry effectors, the parasite establishes membrane contact sites that enable metabolic exchange without compromising vacuolar integrity.
    Keywords:  ROP1; Toxoplasma gondii; VIP1; membrane contact sites
    DOI:  https://doi.org/10.1016/j.pt.2025.12.009
  3. Acta Trop. 2026 Jan 06. pii: S0001-706X(26)00003-3. [Epub ahead of print] 107969
      Leishmaniasis is a protozoan disease prevalent in subtropical regions. Its treatment is expensive, especially the liposomal formulation, and parasite resistance must sometimes be overcome. The Sirtuins are a family of NAD-dependent histone deacetylases that have been identified as promising targets for anti-parasitic drugs due to their essential roles in organisms such as Leishmania. There are three known sirtuins in Leishmania infantum: SIR2-related protein 1 (LiSIR2rp1) present in the cytoplasm and nuclei, and LiSIR2rp2-3 present in mitochondria. While a truncated version of the LiSIR2rp1 has already been crystallized, the complete molecular structure remains unresolved. Our study presents a structural computational characterization of the full-length LiSIR2rp1, the non-mitochondrial sirtuin homologous to human sirtuin SIRT2. We generated and validated molecular models for the full-length LiSIR2rp1 using computational tools. The protein presented a highly conserved catalytic core, and the molecular dynamics simulations (MDS) revealed structural stability of this core, similar to that of human sirtuins. However, the LiSIR2rp1 highly flexible central intrinsically disordered region (IDR) simulated an overall MDS instability. These results suggest that the IDR conformational freedom plays a critical role in the functioning of LiSIR2rp1, with a similar loop in hSIRT2. Our findings contribute to a better understanding of LiSIR2rp1's structural patterns and compare it to its human homolog, thus offering insights into its behaviour. Knowledge about this L. infantum enzyme, a potential target for drug development, could enhance the prospects for future therapeutic strategies against leishmaniasis.
    Keywords:  Leishmania infantum; SIRT; histone deacetylase; intrinsic disordered region; molecular dynamics; protein modeling; sirtuin
    DOI:  https://doi.org/10.1016/j.actatropica.2026.107969
  4. Toxicol Appl Pharmacol. 2026 Jan 02. pii: S0041-008X(26)00002-5. [Epub ahead of print] 117706
      In this research, we mainly focus on the mechanism of histone deacetylase sirtuin 2 (SIRT2) affecting the growth and metastasis of tongue cancer using in vitro and in vivo experiments. Human tongue cancer cells SCC-25, SCC-9, CAL-27, CAL-33 and human oral epithelial cells were cultured for cell line selection. In vitro, SCC-25 cells were manipulated with pcDNA3.1-SIRT2, pcDNA3.1-FZD1, pcDNA3.1-NC, or/and Wnt/β-catenin pathway inhibitor (MSAB) or activator (SKL2001), while CAL-33 cells were treated with siRNA-SIRT2, siRNA-NC or MSAB. The levels of H3K27ac, β-catenin (nuclear, cytoplasmic and total protein), and Wnt1/3a/7a were detected using WB. Based on data from the ENCODE database, the enrichment level of H3K27ac in the FZD1 promoter region was examined by ChIP experiment. Finally, an orthotopic xenograft tumor model in nude mice was constructed for in vivo validation. Re-expression of SIRT2 impaired the proliferative, invasive, and migratory behaviors of tongue cancer cells, while strengthening their apoptosis. Furthermore, SIRT2 decreased H3K27 acetylation, resulting in increased cytoplasmic β-catenin and decreased expression of FZD1, Wnt1/3a/7a, and nuclear β-catenin. FZD1 overexpression or the Wnt/β-catenin pathway activation partially compromised the inhibitory impacts of SIRT2 on the aforementioned behaviors of human tongue cancer cells. The in vivo validation suggested that SIRT2 played a regulatory role in FZD1 expression and Wnt/β-catenin pathway, thereby hindering the growth and metastasis of the orthotopic tongue cancer xenograft model. SIRT2 inhibits the transcriptional expression of FZD1 through H3K27 deacetylation to block the Wnt/β-catenin pathway, consequently suppressing the growth and metastasis of tongue cancer.
    Keywords:  Frizzled-1; H3K27ac; Metastasis; Proliferation; Sirtuin 2; Tongue cancer; Wnt Pathway; β-Catenin
    DOI:  https://doi.org/10.1016/j.taap.2026.117706
  5. Discov Oncol. 2026 Jan 07.
      Histone deacetylase 6 (HDAC6) is the sole member of the histone deacetylase (HDAC) family predominantly localized in the cytoplasm, characterized by dual catalytic domains and an ubiquitin-binding domain. In recent years, it has garnered substantial attention due to its critical role in tumor initiation and progression. This review delineates the unique structural features and core biological functions of HDAC6, while further exploring its expression patterns and prognostic significance in tumors. Additionally, it elaborates on the regulatory roles of HDAC6 in key biological behaviors of tumor cells, including promoting proliferation, suppressing apoptosis, enhancing migratory and invasive potentials, and inducing epithelial-mesenchymal transition (EMT). Concomitantly, the review analyzes the impacts of HDAC6 on the tumor immune microenvironment, its modulation of tumor metabolism, and its association with tumor drug resistance. To date, research on HDAC6 in tumors has firmly established its value as a potential therapeutic target, with specific inhibitors (e.g., ACY-1215 and Tubastatin A) demonstrating significant antitumor activity in preclinical studies and several clinical trials. Focused on the implications of HDAC6 in tumors, this review not only highlights its distinct functions compared to other HDAC family members but also integrates previously unreported mechanisms of action (e.g., HDAC6 cooperates with NEDD8/p62 to sustain proteostasis) and clinical translation perspectives. Collectively, it presents an innovative review that provides valuable references for subsequent basic research and clinical practice of HDAC6-targeted tumor therapy.
    Keywords:  Cancer therapy; HDAC6; HDAC6 inhibitors; Signaling pathways; Tumor immunity; Tumor microenvironment; Tumorigenesis
    DOI:  https://doi.org/10.1007/s12672-026-04391-9
  6. Adv Sci (Weinh). 2026 Jan 05. e12532
      Intestinal epithelial cells (IEC) are crucial for regulating intestinal local immunity to potentiate mucosal barrier function, but the mechanism remains unclear. In this study, we showed that the nicotinamide adenine dinucleotide (NAD+)-dependent enzyme SIRT3 in IECs is required for local T cell differentiation in colorectal cancer and colitis. Modest IEC SIRT3 overexpression reduces the secretion of proinflammatory cytokine IL-1β and inhibits IFNγ-producing CD4+T cells (TH1) and cytotoxic T lymphocytes (CTLs) differentiation. IEC SIRT3 deficiency enhances the production of IL-1β and promotes local TH1 and CTL differentiation in limiting colorectal cancer growth and aggravating colitis. Mechanistically, SIRT3 deficiency promotes IEC functions through quinolinic acid (QA)-mediated NAD+ synthesis for limiting tumor growth. Microbiota-derived 3-hydroxyaminobenzoic acid is the source of intracellular QA in IECs. IL-1β-IL-1R1 signaling is required for IEC SIRT3 deficiency-induced TH1 and CTL differentiation in cancer. Thus, our findings showed that microbiota-derived QA is used as an alternative source of replenishing the intracellular NAD+ pool induced by SIRT3 deficiency to regulate IEC and T cell function, which has implications for targeting IECs as an approach to the treatment of immune-associated diseases, including colorectal cancer and colitis.
    Keywords:  IL‐1R1 signaling; SIRT3; T cell differentiation; T helper cells; colorectal cancer; intestinal epithelial cells
    DOI:  https://doi.org/10.1002/advs.202512532
  7. Cells. 2025 Dec 26. pii: 51. [Epub ahead of print]15(1):
      Many cellular processes, including gene expression regulation, DNA replication and repair, as well as proper condensation and segregation of chromosomes, require highly coordinated remodeling of chromatin. Cohesin and condensins, the structural maintenance of chromosomes (SMC) protein complexes that function as ATP-powered loop extrusion motors, are key determinants of chromatin structure. The genetic loss of their function is lethal, whereas inducible degradation approaches enable rapid, robust analysis of the depletion phenotype. In this review, we discuss new insights into chromatin folding through each cell cycle phase from the auxin-inducible degradation (AID) system. We review the mechanisms by which condensins and cohesins contribute to the helical organization of mitotic chromosomes and to the maintenance of chromosome territories in interphase. Additionally, we discuss studies examining the roles of TOP2A, KIF4A, and SRBD during mitosis using the AID system. We then outline emerging principles of the mitotic-to-interphase transition and how targeted degradation of chromatin proteins reshapes this process. Finally, we highlight and discuss new advances in understanding interphase chromatin organization revealed by AID-based studies.
    Keywords:  3D genome; CTCF; SMC complexes; auxin-inducible degradation
    DOI:  https://doi.org/10.3390/cells15010051