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Last Updated: Nov 17th, 2006 - 22:35:04

Tuberculosis Channel
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Latest Research : Infectious Diseases : Tuberculosis

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Structure of resuscitation promoting factor (Rpf) unveiled
Feb 28, 2005, 21:28, Reviewed by: Dr.

“The discovery of Rpf in the TB bacteria could allow the development of methods to ‘wake-up’ all dormant bacteria in a patient allowing antibiotics to kill the bacteria and cure the disease.”

 
UCL scientists have found a protein that could unlock the secret to quicker, more effective treatment of TB by waking TB bacteria in the body. Once the TB bacteria are active again, the disease becomes treatable using common drugs like antibiotics. Scientists believe that uncovering the molecular structure of this protein will lead the way to designing drugs which enable treatment of dormant and multidrug resistant TB.

In England and Wales around 400 people die each year from the disease. The top challenge for TB control in the European region is multidrug-resistant TB (MDR-TB). Eight per cent of the bacteria causing TB in patients are resistant to one or more drugs and one per cent show multidrug resistance. Left untreated, a person with infectious TB of the lungs infects around 10 to 15 people every year.

In a study published on 1st March 2005 in Nature Structural & Molecular Biology, a combined team discovered the structure of a protein known as resuscitation promoting factor (Rpf). Five versions of the Rpf protein exist in TB bacteria. The paper’s unveiling of the molecular structure of Rpf could be crucial to the treatment of TB in the future.

Dr John Ward, Dept of Biochemistry and Molecular Biology at UCL, said: “The discovery of Rpf in the TB bacteria could allow the development of methods to ‘wake-up’ all dormant bacteria in a patient allowing antibiotics to kill the bacteria and cure the disease.”

 

- published on 1st March 2005 in Nature Structural & Molecular Biology
 

‘The structure of a resuscitation-promoting factor domain from Mycobacterium tuberculosis shows homology to lysozymes’published in the 1st March addition of Nature Structural & Molecular Biology is available online

 
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The team includes Prof Brian Henderson at the UCL Eastman Dental Institute, Nicholas Keep from Birkbeck, University of London, and John Ward at UCL as well as researchers from INSERM Montpellier.

1. ‘The structure of a resuscitation-promoting factor domain from Mycobacterium tuberculosis shows homology to lysozymes’published in the 1st March addition of Nature Structural & Molecular Biology is available online at http://www.nature.com/cgi-taf/DynaPage.taf?file=/nsmb/journal/vaop/ncurrent/abs/nsmb905.html&dynoptions=doi1109067205 2. The top challenge for TB control in the European region, according to the World Health Organisation (WHO), is” multidrug-resistant TB (MDR-TB), HIV-related TB and TB control in prisons” More Information on the challenges of TB control can be found at the WHO website: http://www.euro.who.int/tuberculosis/issues/20030312_1
3. A table of figures for multidrug resistance can be found at: http://www.hpa.org.uk/infections/topics_az/tb/epidemiology/table18.htm
4. More detailed information on TB can be found on the WHO website at: http://www.who.int/mediacentre/factsheets/fs104/en/
5. In England and Wales around 400 people die each year from the disease according to the Health Protection Agency: http://www.hpa.org.uk/infections/topics_az/tb/epidemiology/table11.htm


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