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Research provides new leads in the case against drug-resistant biofilms
Date:11/10/2010

ers of other genes that are important for biofilm formation," Page said. "This is the only known toxin-antitoxin system that is capable of doing this."

An odd bird

The MqsA antitoxin is as unusual as it is influential, Page's team reports. For one thing, the protein, which resembles a bird with wide flapping wings Page likens it to a Klingon "Bird of Prey" ship from Star Trek needs the metal zinc on each wing tip to keep it stable. When it's bound to its partner toxin and DNA, the antitoxin also keeps a very tight lid on the toxin's ability to operate on mRNA, squeezing key parts, or active sites, so close together (about 1 billionth of a meter) that the mRNA simply can't enter.

Because the toxin's activity is key to the health and welfare of persister and biofilm cells, the properties of the toxin-antitoxin binding that regulate them give rise to some potential drug development strategies, Page said. For most of the time, the toxin is bound by the antitoxin, allowing cells to grow. Under other conditions, the antitoxin is destroyed and the toxin is free to cleave, or disable, mRNA. That shuts off existing persister and biofilm cells from further growth, and instead keeps them in a dormant state well-protected from things like antibiotics. If that cleaving goes on too long, however, the cells will die.

So two approaches for drug development, Page said, might be to find compounds that can either keep the toxin-antitoxin pair associated all the time (so that the toxin is inactive and thus that no cleaving occurs), or keep them separated all the time (so that the toxin is active and cleaving always occurs). The zinc on the antitoxin may also prove to be a target.

The investigation is ongoing, but the word is now out on the street that for MqsA and MqsR, the heat is on.


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Contact: David Orenstein
david_orenstein@brown.edu
401-863-1862
Brown University
Source:Eurekalert

Page: 1 2

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