Lyme disease bugs use manganese to evade immune system

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Lyme disease bugs use manganese to evade immune system

Postby NHE » Sat Mar 23, 2013 7:38 pm

Weird Way Lyme Disease Bugs Avoid Immune System
http://www.livescience.com/28120-lyme-d ... anese.html

The bacterium that causes Lyme Disease substitutes manganese for iron in its diet, a new study finds. The pathogen is the first known organism to live without iron.

This talent helps the pathogen evade the immune system, which often acts against foreign invaders by starving them of iron.
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Re: Lyme disease bugs use manganese to evade immune system

Postby CuriousRobot » Sun Mar 24, 2013 1:54 pm

A Manganese-Rich Environment Supports Superoxide Dismutase Activity in a Lyme Disease Pathogen, Borrelia burgdorferi.
The Lyme disease pathogen Borrelia burgdorferi represents a novel organism in which to study metalloprotein biology in that this spirochete has uniquely evolved with no requirement for iron. Not only is iron low, but we show here that B. burgdorferi has the capacity to accumulate remarkably high levels of manganese. This high manganese is necessary to activate the SodA superoxide dismutase (SOD) essential for virulence. Using a metalloproteomic approach, we demonstrate that a bulk of B. burgdorferi SodA directly associates with manganese and a smaller pool of inactive enzyme accumulates as apoprotein. Other metalloproteins may have similarly adapted to using manganese as co-factor including the BB0366 amino-peptidase. While B. burgdorferi SodA has evolved in a manganese-rich, iron-poor environment, the opposite is true for Mn-SODs of organisms such as E. coli and bakers yeast. These Mn-SODs still capture manganese in an iron-rich cell, and we tested whether the same is true for Borrelia SodA. When expressed in the iron-rich mitochondria of S. cerevisiae, B. burgdorferi SodA was inactive. Activity was only possible when cells accumulated extremely high levels of manganese that exceeded cellular iron. Moreover, there was no evidence for iron inactivation of the SOD. B. burgdorferi SodA shows strong overall homology with other members of the Mn-SOD family, but computer assisted modeling revealed some unusual features of the hydrogen bonding network near the enzyme's active site. The unique properties of B. burgdorferi SodA may represent adaptation to expression in the manganese-rich and iron-poor environment of the spirochete.
http://www.ncbi.nlm.nih.gov/pubmed/23376276

Neat.
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