William Metcalf

The world around us contains many chemicals that are useful for medicines, crop protection, and animal health. These chemicals—known as natural products—have typically been discovered by sheer luck. Unsurprisingly, traditional techniques often find the same products, like antibiotics, repeatedly thus creating a need for new technologies. To address this growing demand, William Metcalf (MMG leader), a professor of microbiology, co-founded the company MicroMGx in 2015.

Scientists have labored for decades to find antibiotics that work against Gram-negative bacteria, which cause some of the deadliest infections in hospital settings and are most likely to be resistant to treatment with existing antibiotics. In a study reported in the journal Chemical Science, researchers developed a new method to determine how antibiotics with specific chemical properties thread their way through tiny pores in the otherwise impenetrable cell envelopes of Gram-negative bacteria.

Since 1983, the bacteria Pantoea ananatis has been known to infect several important crops including onions, rice, and corn. It was unclear, however, what molecules were involved. A new study, published in mBio, has identified one of the culprits: pantaphos. Intriguingly, the researchers have discovered that pantaphos can also act as an herbicide and it is toxic to glioblastoma cells, making it an exciting candidate for agricultural and biomedical applications.

Microbes are well-known among biologists as master engineers of useful small molecules, and there are many tricks of their trade. When researchers at the University of Illinois took a closer look at how a known microbe makes a known so-called natural product, they were rewarded with the discovery of a completely unknown biochemical trick.

By proving a theory that was first proposed almost 40 years ago, researchers at the IGB have confirmed a new way that cells conserve energy.

An unexpected discovery has given scientists a greater understanding of an important methane-producing enzyme.

A team of IGB researchers published a paper in eLife that outlined their findings on an enzyme called methyl-coenzyme M reductase, or MCR.

Their findings overturn what was previously believed to be true in the field: that a set of unique modifications present in MCR were essential to how the enzyme functions.