Toxic evolution: wasps and frogs mimic pain molecules to deter predators

Certain species of wasps and frogs share a pain and inflammation peptide similar to one found in vertebrates to help defend against predators—a discovery that contributes to a shifting view of how evolution works, say researchers.

Wasps and frogs independently evolved bradykinin-like peptides, structurally similar to vertebrate bradykinin, as a defense against predators. These peptides originate from toxin gene families, not from the vertebrate kininogen gene, and effectively trigger pain in predators. The findings highlight convergent evolution as a significant and predictable evolutionary process.
In vertebrates, bradykinin plays a role in wound healing and pain signaling. The research demonstrated the bradykinin‑like peptides in wasps and frogs are derived from toxin gene families, not from the vertebrate kininogen gene that produces bradykinin.

Each lineage across multiple wasp and frog families evolved these molecules separately, often multiple times, to deter predators.

Naiqi Shi et al, Repeated convergent evolution of bradykinin mimics as defensive toxins, Science (2026). DOI: 10.1126/science.adx0452

Cancer has a unique nuclear metabolic fingerprint: New discovery

More than 200 metabolic enzymes, many of which are normally tasked with producing energy in the mitochondria, are also found sitting directly on top of human DNA, according to a study published in Nature Communications. The research shows that different cell types, tissues and even cancers each have a unique pattern of metabolic enzymes compartmentalized inside the nucleus and interacting with DNA. It's the first evidence of human cells having what the authors of the study call a "nuclear metabolic fingerprint."

Though further work needs to be done to clarify whether the enzymes are catalyzing reactions, turning genes on or off or simply providing structural support, the research provides new clues for how different types of tumors grow, adapt or resist treatment.

Many of these enzymes synthesize essential building blocks of life, and their nuclear localization is associated with DNA repair. Their presence in the nucleus may therefore directly shape how cancer cells respond to genotoxic stress, a hallmark of many chemotherapeutic treatments. It's an entirely new world to explore, say the researchers of this new work.

The absence, presence and abundance of the enzymes differed by cancer type. For example, oxidative phosphorylation enzymes were common in breast cancer cells but largely absent in lung cancer cells. When they examined tumor samples from patients, the authors of the study saw a similar pattern, demonstrating the tissue and disease-specific nature of nuclear metabolism.

Scientists have been treating metabolism and genome regulation as two separate universes till now, but  this work suggests they're talking to each other, and cancer cells might be exploiting these conversations to survive.

The researchers carried out experiments to figure out what some of the metabolic enzymes are doing. They studied one group of enzymes which provide building blocks for DNA synthesis and repair and found they gather around chromatin when DNA is damaged, helping repair the genome.

During these experiments they discovered that location matters. The enzyme IMPDH2 showed completely different behavior depending on where it was. When the researchers forced it to stay only in the nucleus, it helped maintain genome stability, but when confined to the cytoplasm, it affected other pathways instead.

The discovery raises new questions about how cancer treatments work. Some drugs target a cancer's metabolic activity, while others target its DNA repair mechanisms. If the two systems are more closely linked than previously thought, it has important implications for cancer research.

It could help explain why tumors of different origins, even when carrying the same mutations, often respond very differently to chemotherapy, radiotherapy, or targeted inhibitors.

According to the authors of the study, their research is the first global evidence that the nucleus is crowded with metabolic enzymes. In the long run, mapping the location and function of the enzymes could help identify new biomarkers for diagnosis or new vulnerabilities that anti-cancer drugs could exploit.

Nature Communications (2026). DOI: 10.1038/s41467-026-69217-2

Smart combinations of antibiotics can slow down resistance

When a bacterium becomes resistant to one antibiotic, it may sometimes become more sensitive to another. This biological side-effect offers an unexpected opportunity in the fight against antibiotic resistance.

Analysis of extensive clinical data reveals that resistance to one antibiotic can coincide with increased sensitivity to another, a phenomenon known as collateral sensitivity. This effect is observed across multiple bacterial species and suggests that strategic combinations or sequencing of antibiotics could help slow the development of resistance, offering new avenues for treatment optimization.
By switching wisely between antibiotics or combining them, you can use this biological effect—known as collateral sensitivity—to reduce the chance that bacteria become resistant, and prevent treatments from failing.

Sebastian T Tandar et al, Clinical prevalence of collateral sensitivity: a systematic exploration of multicentre antimicrobial surveillance data, The Lancet Microbe (2026). DOI: 10.1016/j.lanmic.2025.101274