Document Detail


Proteomic analysis of an unculturable bacterial endosymbiont (Blochmannia) reveals high abundance of chaperonins and biosynthetic enzymes.
MedLine Citation:
PMID:  23205679     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Many insect groups have coevolved with bacterial endosymbionts that live within specialized host cells. As a salient example, ants in the tribe Camponotini rely on Blochmannia, an intracellular bacterial mutualist that synthesizes amino acids and recycles nitrogen for the host. We performed a shotgun, label-free, LC/MS/MS quantitative proteomic analysis to investigate the proteome of Blochmannia associated with Camponotus chromaiodes. We identified more than 330 Blochmannia proteins, or 54% coverage of the predicted proteome, as well as 244 Camponotus proteins. Using the average intensity of the top 3 "best flier" peptides along with spiking of a surrogate standard at a known concentration, we estimated the concentration (fmol/μg) of those proteins with confident identification. The estimated dynamic range of Blochmannia protein abundance spanned 3 orders of magnitude and covered diverse functional categories, with particularly high representation of metabolism, information transfer, and chaperones. GroEL, the most abundant protein, totaled 6% of Blochmannia protein abundance. Biosynthesis of essential amino acids, fatty acids, and nucleotides, and sulfate assimilation had disproportionately high coverage in the proteome, further supporting a nutritional role of the symbiosis. This first quantitative proteomic analysis of an ant endosymbiont illustrates a promising approach to study the functional basis of intimate symbioses.
Authors:
Yongliang Fan; J Will Thompson; Laura G Dubois; M Arthur Moseley; Jennifer J Wernegreen
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2012-12-27
Journal Detail:
Title:  Journal of proteome research     Volume:  12     ISSN:  1535-3907     ISO Abbreviation:  J. Proteome Res.     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2013-02-01     Completed Date:  2013-07-05     Revised Date:  2014-02-04    
Medline Journal Info:
Nlm Unique ID:  101128775     Medline TA:  J Proteome Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  704-18     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Amino Acids / metabolism
Animals
Ants / metabolism,  microbiology
Bacterial Proteins / isolation & purification*,  metabolism
Chromatography, Liquid
Enterobacteriaceae / genetics,  metabolism*
Fatty Acids / metabolism
Group I Chaperonins / isolation & purification*,  metabolism
Insect Proteins / isolation & purification*,  metabolism
Nucleotides / metabolism
Proteomics*
Sulfates / metabolism
Symbiosis / physiology
Tandem Mass Spectrometry
Grant Support
ID/Acronym/Agency:
R01 GM062626/GM/NIGMS NIH HHS; R01GM062626/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Bacterial Proteins; 0/Fatty Acids; 0/Insect Proteins; 0/Nucleotides; 0/Sulfates; EC 3.6.1.-/Group I Chaperonins
Comments/Corrections

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