Article (Scientific journals)
Overexpression of a monomeric form of the bovine odorant-binding protein protects Escherichia coli from chemical-induced oxidative stress.
Macedo-Marquez, Alain; Vazquez-Acevedo, Miriam; Ongay-Larios, Laura et al.
2014In Free Radical Research, 48 (7), p. 814-822
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Keywords :
lipocalins; lipid peroxidation; 4-hydroxy-2-nonenal; reactive oxygen species; unsaturated fatty acids
Abstract :
[en] Mammalian odorant-binding proteins (OBPs) are soluble lipocalins produced in the nasal mucosa and in other epithelial tissues of several animal species, where they are supposed to serve as scavengers for small structurally unrelated hydrophobic molecules. These would include odorants and toxic aldehydes like 4-hydroxy-2-nonenal (HNE), which are end products of lipid peroxidation; therefore OBP might physiologically contribute to preserve the integrity of epithelial tissues under oxidative stress conditions by removing toxic compounds from the environment and, eventually, driving them to the appropriate degradative pathways. With the aim of developing a biological model based on a living organism for the investigation of the antioxidant properties of OBP, here we asked whether the overexpression of the protein could confer protection from chemical-induced oxidative stress in Escherichia coli. To this aim, bacteria were made to overexpress either GCC-bOBP, a redesigned monomeric mutant of bovine OBP, or its amino-terminal 6-histidine-tagged version 6H-GCC-bOBP. After inducing overexpression for 4 h, bacterial cells were diluted in fresh culture media, and their growth curves were followed in the presence of hydrogen peroxide (H2O2) and tert-Butyl hydroperoxide (tBuOOH), two reactive oxygen species whose toxicity is mainly due to lipid peroxidation, and menadione, a redox-cycling drug producing the superoxide ion. GCC-bOBP and 6H-GCC-bOBP were found to protect bacterial cells from the insulting agents H2O2 and tBuOOH but not from menadione. The obtained data led us to hypothesize that the presence of overexpressed OBP may contribute to protect bacterial cells against oxidative stress probably by sequestering toxic compounds locally produced during the first replication cycles by lipid peroxidation, before bacteria activate their appropriate enzyme-based antioxidative mechanisms.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Macedo-Marquez, Alain
Vazquez-Acevedo, Miriam
Ongay-Larios, Laura
Miranda Astudillo, Héctor Vicente ;  Université de Liège - ULiège > Département des sciences de la vie > Génétique et physiologie des microalgues
Hernandez-Munoz, Rodolfo
Gonzalez-Halphen, Diego
Grolli, S.
Ramoni, R.
Language :
English
Title :
Overexpression of a monomeric form of the bovine odorant-binding protein protects Escherichia coli from chemical-induced oxidative stress.
Publication date :
28 March 2014
Journal title :
Free Radical Research
ISSN :
1071-5762
eISSN :
1029-2470
Publisher :
Taylor & Francis, United Kingdom
Volume :
48
Issue :
7
Pages :
814-822
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 19 December 2017

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