home   genetic news   bioinformatics   biotechnology   literature   journals   ethics   positions   events   sitemap
 
  HUM-MOLGEN -> Genetic News | search  
 

Combating The Legionnaires' Pathogen

 
  September, 5 2001 19:17
your information resource in human molecular genetics
 
     
In 1976, 152 people contracted a severe respiratory disease while attending an American Legion convention in Philadelphia; 22 of the patients died. The culprit of this disease - called the Legionnaires' disease because of the outbreak at the convention - is a rod-shaped bacterium called Legionella pneumophila. The bacteria live in warm stagnant water sources, such as in air conditioning cooling towers, shower heads or humidifiers, and are transmitted to humans through inhaling the water droplets generated by these devices. Because ~70% of the cases of the Legionnaires' disease are in epidemic form, both prevention and development of treatment against the disease are important tasks.

At the early stage of L. pneumophila infection, the bacteria multiply inside human lung cells. This capability is enhanced by a bacterial protein called macrophage infectivity potentiator protein (Mip). Mip has an enzyme activity that speeds up the protein folding reaction, although it is not yet known if this activity is involved in L. pneumophila infection. To begin to understand the role of Mip in L. pneumophila infection, Hilgenfeld and coworkers at the Institute of Molecular Biotechnology, Germany, have determined the crystal structure of Mip (Nature Structural Biology, Vol. 8, No. 9, pages 779-783).

The molecular architecture of Mip is a V-shaped dimer. At the diverging ends of the V are two domains that can bind FK506, a compound that inhibits the enzyme activity of Mip. By also determining the structure of Mip in complex with FK506, the authors have provided details of how this compound binds to the protein. Because FK506 is an immunsuppressant, it is not an appropriate drug for treating L. pneumophila infection. Nonetheless, these results represent a starting point from which rational searches for host cell protein(s) that interact with Mip, as well as drugs that specifically target Mip, can be initiated.

Contact information:

Professor Rolf Hilgenfeld
Institute of Molecular Biotechnology
Structural Biology & Crystallography
Beutenbergstr, 11
P.O. Box 100813
D-07745 Jena
Germany
Telephone: 49 3641 65 6061
Fax: 49 3641 65 6062
E-mail: hilgenfd@imb-jena.de

(C) Nature Structural Biology press release.


Message posted by: Trevor M. D'Souza

print this article mail this article
Bookmark and Share this page (what is this?)

Social bookmarking allows users to save and categorise a personal collection of bookmarks and share them with others. This is different to using your own browser bookmarks which are available using the menus within your web browser.

Use the links below to share this article on the social bookmarking site of your choice.

Read more about social bookmarking at Wikipedia - Social Bookmarking

Latest News
Variants Associated with Pediatric Allergic Disorder

Mutations in PHF6 Found in T-Cell Leukemia

Genetic Risk Variant for Urinary Bladder Cancer

Antibody Has Therapeutic Effect on Mice with ALS

Regulating P53 Activity in Cancer Cells

Anti-RNA Therapy Counters Breast Cancer Spread

Mitochondrial DNA Diversity

The Power of RNA Sequencing

‘Pro-Ageing' Therapy for Cancer?

Niche Genetics Influence Leukaemia

Molecular Biology: Clinical Promise for RNA Interference

Chemoprevention Cocktail for Colon Cancer

more news ...

Generated by News Editor 2.0 by Kai Garlipp
WWW: Kai Garlipp, Frank S. Zollmann.
7.0 © 1995-2016 HUM-MOLGEN. All rights reserved. Liability, Copyright and Imprint.