Document Detail


A manganese-rich environment supports superoxide dismutase activity in a Lyme disease pathogen, Borrelia burgdorferi.
MedLine Citation:
PMID:  23376276     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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 aminopeptidase. Whereas B. burgdorferi SodA has evolved in a manganese-rich, iron-poor environment, the opposite is true for Mn-SODs of organisms such as Escherichia 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 Saccharomyces 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.
Authors:
J Dafhne Aguirre; Hillary M Clark; Matthew McIlvin; Christine Vazquez; Shaina L Palmere; Dennis J Grab; J Seshu; P John Hart; Mak Saito; Valeria C Culotta
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2013-02-02
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  288     ISSN:  1083-351X     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2013 Mar 
Date Detail:
Created Date:  2013-03-25     Completed Date:  2013-05-15     Revised Date:  2014-03-26    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  8468-78     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Apoenzymes / isolation & purification,  metabolism
Bacterial Proteins / chemistry,  isolation & purification,  metabolism*
Borrelia burgdorferi / enzymology*
Catalytic Domain
Conserved Sequence
Enzyme Activation
Hydrogen Bonding
Hydrogen Peroxide
Manganese / metabolism,  physiology*
Mitochondria / enzymology
Models, Molecular
Molecular Sequence Data
Protein Transport
Saccharomyces cerevisiae
Sequence Homology, Amino Acid
Superoxide Dismutase / chemistry,  isolation & purification,  metabolism*
Grant Support
ID/Acronym/Agency:
AI078559/AI/NIAID NIH HHS; GM50016/GM/NIGMS NIH HHS; P30 ES003819/ES/NIEHS NIH HHS; R01 ES008996/ES/NIEHS NIH HHS; R01 ES08996/ES/NIEHS NIH HHS; R37 GM050016/GM/NIGMS NIH HHS; T32 GM080189/GM/NIGMS NIH HHS; T32 GM080189/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Apoenzymes; 0/Bacterial Proteins; 42Z2K6ZL8P/Manganese; BBX060AN9V/Hydrogen Peroxide; EC 1.15.1.1/Superoxide Dismutase
Comments/Corrections

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