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Team makes discovery in search for new antibiotic

A Taiwanese research team made a breakthrough in the development of a new class of antibiotic that can give humans new leverage in their never-ending battle with bacteria, a statement released by Academia Sinica said on Friday.

The research team, led by Alex Ma (馬徹), an assistant research fellow at the research institute’s Genomics Research Center, developed a complete three-dimensional model structure of the membrane protein that resides on the surface of the Escherichia coli bacteria, or E. coli.

This marks the first time a mechanism that holds the key to bacterial cell wall formation has been modeled in detail and could lead to the development of a new generation of antibiotocs, the statement said.

Bacteria construct cell walls as they divide and multiply, and antibiotics are effective because they block certain key enzymes that help bacteria build those walls. By deciphering the membrane protein — in this case penicillin-binding protein (PBP1b) — Ma’s team can better figure out how to block it.

The study was published on Tuesday in the online version of the US National Academy of Sciences journal — the Proceedings of the National Academy of Sciences.

Since the discovery of penicillin 80 years ago, at least 1,000 kinds of antibiotic have been developed to fight bacterial infections, about 150 of which are commonly used to treat infections.

The rise of drug-resistant bacteria in recent years has seriously challenged medical science, making the need for new antibacterial agents more urgent.

Ma started his research five years ago as part of a project led by Academia Sinica President Wong Chi-huey (翁啟惠) to solve the mystery of bacteria cell wall synthesis and to address the issue of drug-resistant bacteria.

Initially, Ma and his colleagues studied the activity of PBPs. The team then focused on discovering exactly how PBP1b conducts the task of making bacteria cell walls.

After five years of work, the team managed to obtain its three-dimensional structure by coaxing the purified membrane protein PMP1b into crystals and using X-ray crystallography.

The resulting model gives a clear picture of how PBP1b binds a substance called lipid II and performs a kind of a knitting job to finally make a new skin when the bacteria divides, the research institute’s statement said.
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