Antimicrobial resistance has emerged as a global threat that requires urgent attention. In a new study, published in Frontiers in Microbiology, researchers investigated how the antibiotic epilancin 15X kills bacteria.

Over the past few decades, bacteria have increasingly been able to mutate, allowing them to resist the effect of antibiotics. Coupled with the fact that antibiotics are hard to develop, this situation can soon prove to be catastrophic.

Aquatic birds, especially ducks, can carry influenza viruses but they don’t often become severely ill, leading scientists to wonder how their immune systems act as a reservoir for a highly infectious and pathogenic virus, but the birds remain relatively unharmed. Additionally, could the immune system be engineered to thwart transmission to other animals and humans, ultimately preventing future pandemics?

Many of the drugs we utilize in modern medicine are naturally produced by microbes. Penicillin, an antibiotic derived from certain molds, is one of the most notable natural products due to its recognition as one of the biggest advances in medicine and human health. As DNA sequencing has become cheaper and faster, scientists now have access to hundreds of thousands of microbial genomes and the natural products they produce.

Although Enterococcus faecalis is usually an innocuous member of the bacterial community in the human gut, it can also cause several infections, including liver disorders. The bacteria produce cytolysins, which are molecules that destroy cells. In a new study, researchers have uncovered how they do so.

Researchers from the Carl R. Woese Institute for Genomic Biology in collaboration with scientists at Oxford University have published a paper in Cell reporting the function of LanCL proteins. These proteins are found in eukaryotic cells but their function was previously unknown. The study is the first step towards understanding the importance of these ubiquitous proteins. 

Wilfred van der Donk (MMG), the Richard E. Heckert Endowed Chair in Chemistry and director of graduate studies in chemistry at Illinois, was elected to the National Academy of Sciences, one of the highest professional honors a scientist can receive.

Microbes are master chefs of the biomolecular world; collectively, they harbor the ability to produce a vast array of unknown substances, some of which may have therapeutic or other useful properties. In searching for useful products, a team of chemists at Illinois have discovered a whole new class of microbial recipes.

The mid-20th century was the golden age of natural product discovery. Scientists discovered groundbreaking drugs, like penicillin and tetracycline, from sources in nature.

But as the search for natural products continued, pharmaceutical companies kept finding the same products over and over again. By the early 2000s, most of these companies shut down their natural product discovery programs.

Bacteria are master engineers of small, biologically useful molecules. A new study in Nature Communications (DOI: 10.1038/s41467-018-06083-7) has revealed one of the tricks of this microbial trade: synthesizing and then later inserting a nitrogen-nitrogen bond, like a prefabricated part, into a larger molecule.

Researchers say they can now produce a vast library of unique cyclic compounds, some with the capacity to interrupt specific protein-protein interactions that play a role in disease. The new compounds have cyclic structures that give them stability and enhance their ability to bind to their targets.  

The study, reported in the journal Nature Chemical Biology, also revealed that one of the newly generated compounds interferes with the binding of an HIV protein to a human protein, an interaction vital to the virus’s life cycle.