Protein study gives fresh impetus in fight against superbugs

ScienceDaily (Jan. 31, 2012) ? Scientists have shed light on the way superbugs such as MRSA are able to become resistant to antibiotics. Researchers have mapped the complex molecular structure of an enzyme found in many bacteria.

These molecules -- known as restriction enzymes -- control the speed at which bacteria can acquire resistance to drugs and eventually become superbugs.

Infectious bacteria

The study, carried out by an international team including scientists from the University of Edinburgh, focused on E. coli.

However, the results would apply to many other infectious bacteria.

After prolonged treatment with antibiotics, bacteria may evolve to become resistant to many drugs, as is the case with superbugs such as MRSA.

Enzyme activity

Bacteria become resistant by absorbing DNA -- usually from other bugs or viruses -- which contains genetic information enabling the bacteria to block the action of drugs.

Restriction enzymes can slow or halt this absorption process.

Enzymes that work in this way are believed to have evolved as a defense mechanism for bacteria.

DNA reaction

The researchers also studied the enzyme in action by reacting it with DNA from another organism.

They were able to model the mechanism by which the enzyme disables foreign DNA, while safeguarding the bacteria's own genetic material.

Restriction enzymes' ability to sever genetic material is widely applied by scientists to cut and paste strands of DNA in genetic engineering.

The study was carried out in collaboration with the Universities of Leeds and Portsmouth with partners in Poland and France.

It was supported by the Biotechnology and Biological Sciences Research Council and the Wellcome Trust and published in Genes and Development journal.

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Story Source:

The above story is reprinted from materials provided by University of Edinburgh.

Note: Materials may be edited for content and length. For further information, please contact the source cited above.

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Journal Reference:

1. C. K. Kennaway, J. E. Taylor, C. F. Song, W. Potrzebowski, W. Nicholson, J. H. White, A. Swiderska, A. Obarska-Kosinska, P. Callow, L. P. Cooper, G. A. Roberts, J.-B. Artero, J. M. Bujnicki, J. Trinick, G. G. Kneale, D. T. F. Dryden. Structure and operation of the DNA-translocating type I DNA restriction enzymes. Genes & Development, 2012; 26 (1): 92 DOI: 10.1101/gad.179085.111

Note: If no author is given, the source is cited instead.

Disclaimer: This article is not intended to provide medical advice, diagnosis or treatment. Views expressed here do not necessarily reflect those of ScienceDaily or its staff.

Source: http://www.sciencedaily.com/releases/2012/01/120131102521.htm

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