Scientists have found a way to combat harmful gram-negative bacteria.
In the last few years, health care officials have contended with the growing scourge of a superbug, gram-negative bacteria. As the U.S. Centers for Disease Control and Prevention explained, this unique bacteria is resistant to most readily available antibiotics, and causes ailments like bloodstream infections, pneumonia and most surgical site infections. In 2010, researchers from Massachusetts General Hospital revealed that these bacteria cause about 30 percent of all hospital-acquired infections.
However, there could be a new way to fight these microbial menaces. In a recent study published in the journal Nature, scientists may have found an effective way to stop these superbugs right in their tracks.
Hitting back hard
For the study, researchers from the U.K.’s University of East Anglia posed a simple question: What is it that makes these gram-negative bacteria so resistant to most treatment methods? The answer, they found, is the outer membrane. According to the Online Textbook of Bacteriology, the outer membrane is the bacteria’s knight in shining armor. It not only serves to protect the cell’s inner RNA, but assists with directing the flow of valuable nutrients and proteins. For the outer membrane to be able to communicate effectively with the inner membrane, the cells uses OMPs, or outer membrane proteins. As Phys.org explained, OMPs are powerful receptors, and they’re responsible for managing what components come into a bacteria’s cells.
But how does the bacteria know which OMPs belong in the cell walls to properly control traffic? As the Washington Post reported, the OMPs have a unique mechanism called BamA, or the beta-barrel assembly machinery. It’s the BAM that controls the gates in and out of a cell, and are responsible for keeping harmful toxins away. Several studies, including a 2011 review published in the Journal of Bacteriology, have outlined the inner workings of BAM. Until now, though, scientists had little insight into the exact mechanisms behind how BamA operated.
So, researchers with the Nature study set about how to better understand BamA and BamD. BamD is akin to BamA’s tag team partner, according to UniProt Consortium, and helps assemble the proteins. During their experiments, the research team found that BamA and BamD have two states: inward-open and lateral-open.
By adjusting the tilt of the entire BAM complex, scientists were able to better understand how these cell structures moved between an open and closed state. With that knowledge, the team can find ways to deliver drugs beyond the protective outer membrane and into the heart of the gram-negative bacteria. In fact, the team is already developing a designer molecule that interrupts communication between BamA and BamD.
Beyond the work with gram-negative bacteria, the scientists from East Anglia hope to tackle other diseases. For instance, Parkinson’s and diabetes are linked to issues with mitochondria (also referred to as the cell’s “engine”) which also have complicated outer membranes.
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