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Heinberg, A.

Publications and source records attributed to Heinberg, A..

2 recordsLinked to original sources

Targeting the 3 splice site by a decoy oligonucleotide attenuates U2AF1 splicing activity and inhibits leukemia

Recurrent mutations in spliceosomal genes are a hallmark of myeloid malignancies, with SF3B1, SRSF2, U2AF1 and ZRSR2 among the most frequently affected. These alterations are typically heterozygous, mutually exclusive missense mutations targeting highly conserved residues, reflecting a selective pressure to maintain a dysregulated yet essential splicing machinery. This constraint suggests that leukemic cells remain dependent on residual splicing activity, exposing a potential therapeutic vulnerability that extends beyond genetically defined subsets. For example, a previously developed therapeutic, Pladienolide B, is a potent cancer cell growth inhibitor targeting the SF3B1 subunit of the spliceosome1,2. Here we present an RNA decoy-based strategy to disrupt 3' splice site recognition by competitively engaging components of the spliceosomal machinery. We engineered a chemically stabilized RNA decoy that mimics the 3 splice site (3'SS decoy), thereby sequestering proteins involved in 3 splice site recognition from endogenous pre-mRNA targets. Although the decoy is expected to engage multiple components of the 3' splice site recognition complex, U2AF1 was used as the primary molecular readout to assess target engagement and downstream effects. To enable intracellular delivery, decoys were encapsulated in lipid nanoparticles (LNPs), facilitating efficient uptake in leukemic systems. We show that LNP-encapsulated decoys are efficiently delivered into leukemic cells, including established cell lines and patient-derived blasts, and directly engage components of the splicing machinery. Decoy treatment induces widespread alterations in RNA splicing programs and impairs leukemic cell fitness in vitro. Importantly, systemic administration of the 3SS decoy significantly reduces leukemia burden in an in vivo xenograft model. Notably, these effects are observed independently of spliceosomal mutational status, supporting a broader dependency of leukemic cells on intact splicing factor function. Together, our findings establish decoy-mediated disruption of splicing factor activity as a mechanistically targeted therapeutic strategy and identify LNPs as an effective platform for the delivery of RNA-based modulators of essential RNA-protein interactions in myeloid malignancies.

molecular biology↗

Phosphorylation of the canonical histone H2A marks foci of damaged DNA in malaria parasite

Plasmodium falciparum parasites proliferate within circulating red blood cells and are responsible for the deadliest form of human malaria. These parasites are exposed to numerous intrinsic and external sources that could cause DNA damage, therefore, they have evolved efficient mechanisms to protect their genome integrity and allow them to proliferate in such conditions. In higher eukaryotes, double strand breaks rapidly lead to phosphorylation of the core histone variant H2A.X which marks the site of damaged DNA. We show that in P. falciparum that lacks the H2A.X variant, the canonical PfH2A is phosphorylated on serine 121 upon exposure to sources of DNA damage in a dose dependent manner. We further demonstrate that phosphorylated PfH2A is recruited to foci of damaged chromatin shortly after exposure to sources of damage, while the non-phosphorylated PfH2A remains spread throughout the nucleoplasm. In addition, we found that PfH2A phosphorylation is dynamic and as the parasite repairs its DNA over time, this phosphorylation is removed. We also demonstrate that these phosphorylation dynamics could be used to establish a novel and direct DNA repair assay in P. falciparum. ImportancePlasmodium falciparum is the deadliest human parasite that causes malaria when it reaches the blood stream and begins proliferating inside red blood cells where the parasites are particularly prone to DNA damage. The molecular mechanisms that allow these pathogens to maintain their genome integrity under such condition are also the driving force for acquiring genome plasticity that enable them to create antigenic variation and become resistant to essentially all available drugs. However, mechanisms of DNA damage response and repair have not been extensively studied in these parasites. The paper addresses our recent discovery, that P. falciparum that lacks the histone variant H2A.X, phosphorylates its canonical core histone PfH2A in response to exposure to DNA damage. The process of DNA repair in Plasmodium was mostly studied indirectly. Our findings enabled us to establish a direct DNA repair assay for P. falciparum similar to assays that are widely used in model organisms.

microbiology↗