La Trobe University scientists have uncovered the critical role fatty cell structures play in our body's early detection and defense against viruses. Published in Nature Communications, the discovery could open the door to a new type of antiviral strategy that harnesses the body's innate defense mechanisms rather than targeting individual viruses.

Cells are like metropolises, home to millions of molecular residents. If one were to stand atop a high-rise, trying to identify most of its inhabitants would seem an impossible task. Even with the sophisticated imaging tools currently available to scientists, it is challenging to zoom in on specific molecules and view them with a high degree of detail.

Another last-resort antibiotic has fallen victim to the rapid evolution of drug-resistant superbugs. The powerful antibiotic combination ceftazidime-avibactam (CZA), widely used to treat severe hospital-acquired infections caused by Pseudomonas aeruginosa—particularly in critically ill and immunocompromised patients—can no longer eliminate some of these infections.

Researchers at Queen Mary University of London have discovered that tiny photosynthetic bacteria band together into protective "herds" when attacked by predators—a survival strategy that could also influence how carbon is stored in the world's waters.

The nucleolus is a liquid-like cellular organelle where protein factories called ribosomes are assembled. Researchers knew of three distinct compartments within the nucleolus, but how these compartments function to drive ribosome assembly was unclear. A study from St. Jude Children's Research Hospital, published today in Molecular Cell, reveals that smaller subcompartments containing ribosome building blocks and assembly proteins spontaneously form to finish the final steps of ribosome assembly. This reveals unprecedented levels of organization behind the process and may offer insight into diseases associated with increased ribosome production, such as cancer.