Resistance to antibiotics has been on scientists' and researchers' minds, as they look for alternative solutions for treatments and cures of multiple antibiotic-reliant diseases. One such group of researchers may have found a new option.
Having deconstructed the crystal structure of the enzyme that creates obafluorin - a broad-spectrum antibiotic agent that comes from a strain of soil bacteria - the team has discovered what could be our next generation of antibiotics.
Led by a group of researchers from the Washington University in St. Louis, and the University of Buffalo, the findings were published on July 31st, in Nature Communications.
The search for uncontaminated antibiotics
"In the long term, we really need new structural classes of antibiotics that have never been contaminated by clinical resistance from established antibiotic classes," said Timothy Wencewicz, assistant professor of Chemistry in Arts and Sciences.
Wencewicz continued: "Obafluorin has a novel structure compared to all FDA-approved antibiotics."
What the team has found could be used as the next phase of antibiotics. This is desperately needed as more and more people are developing immunity to current antibiotics, mostly from overuse over the years.
Nature as the main provider
Obafluorin, in particular, comes from a fluorescent strain of soil bacteria, which creates a biofilm on the roots of plants. The enzyme, nonribosomal peptide synthetase, with its highly reactive beta-lactone ring, is what's accountable for obafluorin's antimicrobial structure.
First discovered in 1984, it wasn't until 2017 that Wenecewicz figured out the genetic blueprint of the enzyme. His findings allow a beta-lactone forming enzyme (obafluorin) which is available in nature to be made from scratch in a laboratory for the first time.
“We need new structural classes of antibiotics that have never been contaminated by clinical resistance from established antibiotic classes.” #WashU experts study obafluorin, a promising compound that may give rise to a new generation of antibiotics. https://t.co/1EKxIRdh91— Washington University in St. Louis (@WUSTL) August 1, 2019
Thanks to this new research however, it is now easier and faster to create analogs of the natural product in a lab environment.
For Wencewicz, the research is not over yet, as he said: "Given the structural diversity of known beta-lactone natural products, we believe that novel beta-lactone synthases remain to be discovered."