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Researchers unveil molecular details of how bacteria propagate antibiotic resistance
Date:7/26/2012

bacterium to a recipient).

Before the plasmid gene for drug resistance can be passed, it must be processed for the transfer. This occurs when a protein called the Nicking Enzyme of Staphylococci, or NES, binds with its active area, known as the relaxase region, to the donor cell plasmid. NES then cuts, or "nicks," one strand of the double helix so that it separates into two single strands of DNA. One moves into the recipient cell while the other remains with the donor. After the two strands are replicated, NES reforms the plasmid in both cells, creating two drug-resistant Staph that are ready to spread their misery further.

Using x-ray crystallography, Edwards, Redinbo and their colleagues defined the structure of both ends of the VRSA NES protein, the N-terminus where the relaxase region resides and the molecule's opposite end known as the C-terminus. They noticed that the N-terminus structure included a region with two distinct protein loops. Suspecting that this area might play a critical role in the VRSA plasmid transfer process, the researchers cut out the loops. This kept the NES relaxase region from clamping onto or staying bound to the plasmid DNA.

Biochemical assays showed that the function of the loops was indeed to keep the relaxase region attached to the plasmid until nicking occurred. This took place, the researchers learned, in the minor groove of a specific DNA sequence on the plasmid.

"We realized that a compound that could block this groove, prevent the NES loops from attaching and inhibit the cleaving of the plasmid DNA into single strands could potentially stop conjugal transfer of drug resistance altogether," Edwards says.

To test their theory in the laboratory, the researchers used a Hoechst compounda blue fluorescent dye used to stain DNAthat could bind to the minor groove. As predicted, blocking the grove prevented nicking of the plasmid DNA sequence.

Redinbo says that this "proof of conce
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Contact: Catherine Meyers
cmeyers@aip.org
301-209-3088
American Institute of Physics
Source:Eurekalert

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