Picture a bacteria cell like a balloon. Puncture the wall of the balloon, and it bursts. That’s how some antibiotics work: in bacteria, the cell wall is made of a molecule called peptidoglycan, and by interfering with production of peptidoglycan, the antibiotic kills the bacteria.
Associate professor of chemistry Michael VanNieuwenhze says that for 50 years, researchers inferred that the bacteria chlamydia had peptidoglycan in its cell wall, but, “It was difficult to find because the bacterial cell was actually hidden inside of a host cell. So you have to, if you will, parse the cellular machinery of two different cells to get at the peptidoglycan, if in fact it existed,” VanNieuwenhze says.
Biochemistry graduate student Erkin Kuru led the research team that discovered a way to confirm the existence of peptidoglycan in chlamydia. Kuru’s team developed a molecular probe that incorporated itself into peptidoglycan and lit up in a specific way when bombarded with light photons.
Now that the existence of peptidoglycan has been confirmed in chlamydia, Kuru says research can move forward on diagnosis techniques and possible new treatments.
“One advantage of inhibiting peptidoglycan in bacteria is, our cells do not have peptidoglycan cell walls. And any drug that would be specific to this peptidoglycan molecule would be basically nontoxic to the humans,” Kuru says.
VanNieuwenhze says that means researchers can now come up with a new antibiotic specific to kill chlamydia, hitting it on its peptidoglycan cell walls.
The research team published their paper in Nature this month, and Kuru says reception in the scientific community has been positive.