Chiral separation of d/l-arginine with whole cells through an engineered FhuA nanochannel

2019 ◽  
Vol 55 (38) ◽  
pp. 5431-5434 ◽  
Author(s):  
Deepak Anand ◽  
Gaurao V. Dhoke ◽  
Julia Gehrmann ◽  
Tayebeh M. Garakani ◽  
Mehdi D. Davari ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Chiral Separation ◽  
Protein A ◽  
Cell System ◽  
Membrane Channel ◽  
Whole Cell ◽  
Whole Cells ◽  
Channel Protein ◽  
Ferric Hydroxamate ◽  
Outer Membrane Channel

Development of a novel whole cell system for chiral separation of arginine enantiomers through an engineered outer membrane channel protein ferric hydroxamate uptake protein A (FhuA).

scholarly journals The Mycobacterium tuberculosis Outer Membrane Channel Protein CpnT Confers Susceptibility to Toxic Molecules

2015 ◽  
Vol 59 (4) ◽  
pp. 2328-2336 ◽  
Author(s):  
Olga Danilchanka ◽  
David Pires ◽  
Elsa Anes ◽  
Michael Niederweis
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Membrane Permeability ◽  
Nutrient Uptake ◽  
Outer Membrane ◽  
Membrane Channel ◽  
Content Type ◽  
Channel Protein ◽  
Outer Membrane Channel ◽  
Outer Membrane Permeability ◽  
Slow Growing

ABSTRACTMycobacterium tuberculosis, the causative agent of tuberculosis, is protected from toxic solutes by an effective outer membrane permeability barrier. Recently, we showed that the outer membrane channel protein CpnT is required for efficient nutrient uptake byM. tuberculosisandMycobacterium bovisBCG. In this study, we found that thecpnTmutant ofM. bovisBCG is more resistant than the wild type to a large number of drugs and antibiotics, including rifampin, ethambutol, clarithromycin, tetracycline, and ampicillin, by 8- to 32-fold. Furthermore, thecpnTmutant ofM. bovisBCG was 100-fold more resistant to nitric oxide, a major bactericidal agent required to controlM. tuberculosisinfections in mice. Thus, CpnT constitutes the first outer membrane susceptibility factor in slow-growing mycobacteria. The dual functions of CpnT in uptake of nutrients and mediating susceptibility to toxic molecules are reflected in macrophage infection experiments: while loss of CpnT was detrimental forM. bovisBCG in macrophages that enable bacterial replication, presumably due to inadequate nutrient uptake, it conferred a survival advantage in macrophages that mount a strong bactericidal response. Importantly, thecpnTgene showed a significantly higher density of nonsynonymous mutations in drug-resistant clinicalM. tuberculosisstrains, indicating that CpnT is under selective pressure in human tuberculosis and/or during chemotherapy. Our results indicate that the CpnT channel constitutes an outer membrane gateway controlling the influx of nutrients and toxic molecules into slow-growing mycobacteria. This study revealed that reducing protein-mediated outer membrane permeability might constitute a new drug resistance mechanism in slow-growing mycobacteria.

scholarly journals Molecular dynamics simulation of outer membrane channel protein, maltoporin of E.coli

2003 ◽  
Vol 43 (supplement) ◽  
pp. S49
Author(s):  
K. Seki ◽  
A. Suenaga ◽  
T. Narumi ◽  
M. Taiji ◽  
C. Danelon ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulation ◽  
Outer Membrane ◽  
Dynamics Simulation ◽  
Membrane Channel ◽  
Channel Protein ◽  
Outer Membrane Channel

scholarly journals An outer membrane channel protein of Mycobacterium tuberculosis with exotoxin activity

2014 ◽  
Vol 111 (18) ◽  
pp. 6750-6755 ◽  
Author(s):  
O. Danilchanka ◽  
J. Sun ◽  
M. Pavlenok ◽  
C. Maueroder ◽  
A. Speer ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Outer Membrane ◽  
Membrane Channel ◽  
Channel Protein ◽  
Outer Membrane Channel

scholarly journals The Salmonella Enteritidis TolC outer membrane channel is essential for egg white survival

2019 ◽  
Vol 98 (5) ◽  
pp. 2281-2289 ◽  
Author(s):  
R. Raspoet ◽  
V. Eeckhaut ◽  
K. Vermeulen ◽  
L. De Smet ◽  
Y. Wen ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Salmonella Enteritidis ◽  
Egg White ◽  
Membrane Channel ◽  
Outer Membrane Channel
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