In mapping the structure of short-lived bacterial 'switches,' biochemist may find novel answer to antibiotic resistance

WALTHAM, Mass. -- Atom by atom, a Brandeis University researcher and her colleagues have unmasked the structure of ephemeral protein "switches" that play a critical role in transforming mild-mannered bacteria into lethal parasites. The finding, reported in the Dec. 23 issue of the journal Nature, raises the prospect of a novel kind of antibiotic to fill the void left by growing resistance among many bacteria to traditional drugs.

The research, led by Brandeis biochemist Dorothee Kern, also involved scientists from the University of Wisconsin, Lawrence Berkeley National Laboratory, and the University of California at Berkeley.

Current-generation antibiotics, which kill off normal strains of bacteria while leaving resistant ones unaffected, essentially select for the survival of resistant strains, sometimes inducing resistance in as little as six months. The protein family Kern describes in the Nature paper represents a potential target for a whole new class of antibiotics to specifically prevent pathogenic bacteria from becoming virulent and attacking the body's cells.

"Most conventional antibiotics work by inhibiting processes essential to cell viability, such as DNA translation or the assembly of cell membranes," says Kern, an assistant professor of biochemistry at Brandeis. "Few attempts have been made to target the mechanisms by which pathogenic bacteria become virulent and infect host cells."

Part of a two-component system that dominates signal transduction in bacteria, the phosphate-juggling protein switch mapped out by Kern and her colleagues works by snatching a single phosphate ion from the amino acid histidine. The phosphorylated protein then binds to bacterial DNA, turning on genes such as those that instigate infection. These protein switches are ubiquitous in bacteria, but aren't found in humans -- making them an ideal target for antibiotics.

The protein switch studied by Kern is part of

Contact: Steve Bradt
Brandeis University

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