Difference between revisions of "PMID:28559299"
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| + | !align=left align='left' bgcolor='#CCCCFF' |Citation | ||
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| + | '''Meehan, BM, Landeta, C, Boyd, D and Beckwith, J''' (2017) The Disulfide Bond Formation Pathway Is Essential for Anaerobic Growth of Escherichia coli. ''J. Bacteriol.'' '''199''' | ||
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| + | !align=left align='left' bgcolor='#CCCCFF' |Abstract | ||
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| + | Disulfide bonds are critical to the stability and function of many bacterial proteins. In the periplasm of , intramolecular disulfide bond formation is catalyzed by the two-component disulfide bond forming (DSB) system. Inactivation of the DSB pathway has been shown to lead to a number of pleotropic effects, although cells remain viable under standard laboratory conditions. However, we show here that strains of reversibly filament under aerobic conditions and fail to grow anaerobically unless a strong oxidant is provided in the growth medium. These findings demonstrate that the background disulfide bond formation necessary to maintain the viability of strains is oxygen dependent. LptD, a key component of the lipopolysaccharide transport system, fails to fold properly in strains exposed to anaerobic conditions, suggesting that these mutants may have defects in outer membrane assembly. We also show that anaerobic growth of mutants can be restored by suppressor mutations in the disulfide bond isomerization system. Overall, our results underscore the importance of proper disulfide bond formation to pathways critical to viability under conditions where oxygen is limited. While the disulfide bond formation (DSB) system of has been studied for decades and has been shown to play an important role in the proper folding of many proteins, including some associated with virulence, it was considered dispensable for growth under most laboratory conditions. This work represents the first attempt to study the effects of the DSB system under strictly anaerobic conditions, simulating the environment encountered by pathogenic strains in the human intestinal tract. By demonstrating that the DSB system is essential for growth under such conditions, this work suggests that compounds inhibiting Dsb enzymes might act not only as antivirulents but also as true antibiotics. | ||
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| + | [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=28559299 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5527382 PMC5527382] | ||
| + | Online version:[http://dx.doi.org/10.1128/JB.00120-17 10.1128/JB.00120-17] | ||
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| + | !align=left align='left' bgcolor='#CCCCFF' |Keywords | ||
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| + | Anaerobiosis; Culture Media/chemistry; Disulfides/metabolism; Escherichia coli/cytology; Escherichia coli/growth & development; Escherichia coli/metabolism; Gene Deletion; Microbial Viability; Oxidants/metabolism | ||
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| + | ==Main Points of the Paper == | ||
| + | {{LitSignificance}} | ||
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| + | == Materials and Methods Used == | ||
| + | {{LitMaterials}} | ||
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| + | ==Phenotype Annotations== | ||
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| + | !|Phenotype of!!Taxon Information!!Genotype Information (if known)!!Condition Information!!OMP ID!!OMP Term Name!!ECO ID!!ECO Term Name!!Notes!!Status | ||
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| + | ==Notes== | ||
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| + | ==References== | ||
| + | {{RefHelp}} | ||
| + | <references/> | ||
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| + | [[Category:Publication]] | ||
Latest revision as of 00:01, 3 February 2019
| Citation |
Meehan, BM, Landeta, C, Boyd, D and Beckwith, J (2017) The Disulfide Bond Formation Pathway Is Essential for Anaerobic Growth of Escherichia coli. J. Bacteriol. 199 |
|---|---|
| Abstract |
Disulfide bonds are critical to the stability and function of many bacterial proteins. In the periplasm of , intramolecular disulfide bond formation is catalyzed by the two-component disulfide bond forming (DSB) system. Inactivation of the DSB pathway has been shown to lead to a number of pleotropic effects, although cells remain viable under standard laboratory conditions. However, we show here that strains of reversibly filament under aerobic conditions and fail to grow anaerobically unless a strong oxidant is provided in the growth medium. These findings demonstrate that the background disulfide bond formation necessary to maintain the viability of strains is oxygen dependent. LptD, a key component of the lipopolysaccharide transport system, fails to fold properly in strains exposed to anaerobic conditions, suggesting that these mutants may have defects in outer membrane assembly. We also show that anaerobic growth of mutants can be restored by suppressor mutations in the disulfide bond isomerization system. Overall, our results underscore the importance of proper disulfide bond formation to pathways critical to viability under conditions where oxygen is limited. While the disulfide bond formation (DSB) system of has been studied for decades and has been shown to play an important role in the proper folding of many proteins, including some associated with virulence, it was considered dispensable for growth under most laboratory conditions. This work represents the first attempt to study the effects of the DSB system under strictly anaerobic conditions, simulating the environment encountered by pathogenic strains in the human intestinal tract. By demonstrating that the DSB system is essential for growth under such conditions, this work suggests that compounds inhibiting Dsb enzymes might act not only as antivirulents but also as true antibiotics. |
| Links |
PubMed PMC5527382 Online version:10.1128/JB.00120-17 |
| Keywords |
Anaerobiosis; Culture Media/chemistry; Disulfides/metabolism; Escherichia coli/cytology; Escherichia coli/growth & development; Escherichia coli/metabolism; Gene Deletion; Microbial Viability; Oxidants/metabolism |
Main Points of the Paper
Please summarize the main points of the paper.
Materials and Methods Used
Please list the materials and methods used in this paper (strains, plasmids, antibodies, etc).
Phenotype Annotations
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| Phenotype of | Taxon Information | Genotype Information (if known) | Condition Information | OMP ID | OMP Term Name | ECO ID | ECO Term Name | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|
Notes
References
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