Homologous overexpression of alkyl hydroperoxide reductase subunit C (ahpC) protects Bifidobacterium longum strain NCC2705 from oxidative stress

FangLei Zuo; Rui Yu; Gul Bahar Khaskheli; HuiQin Ma; LiLi Chen; Zhu Zeng; AiJun Mao; ShangWu Chen

doi:10.1016/j.resmic.2014.05.040

Homologous overexpression of alkyl hydroperoxide reductase subunit C (ahpC) protects Bifidobacterium longum strain NCC2705 from oxidative stress

Res Microbiol. 2014 Sep;165(7):581-9. doi: 10.1016/j.resmic.2014.05.040. Epub 2014 Jun 19.

Authors

FangLei Zuo¹, Rui Yu², Gul Bahar Khaskheli³, HuiQin Ma⁴, LiLi Chen⁵, Zhu Zeng⁶, AiJun Mao⁷, ShangWu Chen⁸

Affiliations

¹ Key Laboratory of Functional Dairy Science of Chinese Ministry of Education and Municipal Government of Beijing, Beijing Laboratory for Food Quality and Safety, College of Food Science and Nutritional Engineering, China Agricultural University, No. 17 Qinghua East Road, Haidian District, Beijing 100083, PR China. Electronic address: duruolanzi@gmail.com.
² Key Laboratory of Functional Dairy Science of Chinese Ministry of Education and Municipal Government of Beijing, Beijing Laboratory for Food Quality and Safety, College of Food Science and Nutritional Engineering, China Agricultural University, No. 17 Qinghua East Road, Haidian District, Beijing 100083, PR China. Electronic address: hardheartyr@sina.com.
³ Key Laboratory of Functional Dairy Science of Chinese Ministry of Education and Municipal Government of Beijing, Beijing Laboratory for Food Quality and Safety, College of Food Science and Nutritional Engineering, China Agricultural University, No. 17 Qinghua East Road, Haidian District, Beijing 100083, PR China. Electronic address: khaskhelig@gmail.com.
⁴ College of Agriculture and Biotechnology, China Agricultural University, No. 2 Yuanmingyuan West Road, Haidian District, Beijing 100193, PR China. Electronic address: hqma@cau.edu.cn.
⁵ Key Laboratory of Functional Dairy Science of Chinese Ministry of Education and Municipal Government of Beijing, Beijing Laboratory for Food Quality and Safety, College of Food Science and Nutritional Engineering, China Agricultural University, No. 17 Qinghua East Road, Haidian District, Beijing 100083, PR China. Electronic address: itachi.regulus@gmail.com.
⁶ Key Laboratory of Functional Dairy Science of Chinese Ministry of Education and Municipal Government of Beijing, Beijing Laboratory for Food Quality and Safety, College of Food Science and Nutritional Engineering, China Agricultural University, No. 17 Qinghua East Road, Haidian District, Beijing 100083, PR China. Electronic address: zengzhuydyxf@163.com.
⁷ Beijing Agricultural Function Microbial Engineering and Technology Center, No. 1 Li'ersi Industrial Area, Zhangjiawan Town, Tongzhou District, Beijing 101113, PR China. Electronic address: maoaijun@polo-china.com.
⁸ Key Laboratory of Functional Dairy Science of Chinese Ministry of Education and Municipal Government of Beijing, Beijing Laboratory for Food Quality and Safety, College of Food Science and Nutritional Engineering, China Agricultural University, No. 17 Qinghua East Road, Haidian District, Beijing 100083, PR China; Beijing Agricultural Function Microbial Engineering and Technology Center, No. 1 Li'ersi Industrial Area, Zhangjiawan Town, Tongzhou District, Beijing 101113, PR China. Electronic address: swchen@cau.edu.cn.

PMID: 24953679
DOI: 10.1016/j.resmic.2014.05.040

Abstract

The ability to manage reactive oxygen species (ROS) effectively is crucial for the survival of gut bifidobacteria under conditions of oxidative stress. Alkyl hydroperoxide reductase catalytic subunit C (ahpC) of Bifidobacterium longum responds to various oxidative stresses. In this study, an ahpC-overexpressing transformant of B. longum strain NCC2705 was constructed to investigate the role and function of ahpC in oxidative stresses inflicted by treatments with hydrogen peroxide (H2O2), cumene hydroperoxide, and aerobic oxygen. Results indicated that in B. longum, AhpC is the primary scavenger of endogenous H2O2 generated by aerobic metabolism, but it is unable to detoxify high concentrations of exogenous H2O2. The ahpC-overexpressing B. longum strain showed increased resistance to organic hydroperoxide killing, increased viability under aerobic growth, but decreased resistance to exogenous H2O2 in comparison to the control strain. Analysis of genes from the oxidative stress-defense pathway encoding oxygen-independent coproporphyrinogen III oxidase (HemN), NADH oxidase (Nox) and thioredoxin reductase-like protein (TrxB) showed increased transcript levels in the ahpC-overexpressing vs. control strain. These findings suggest that elevated ahpC expression facilitates or activates the different electron donor-dependent ROS-elimination pathways in B. longum's response to oxidative stress.

Keywords: Alkyl hydroperoxide reductase; Bifidobacterium longum; Oxidative stress.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Benzene Derivatives / toxicity
Bifidobacterium / drug effects
Bifidobacterium / enzymology*
Bifidobacterium / genetics
Bifidobacterium / physiology*
Hydrogen Peroxide / toxicity
Microbial Viability / drug effects
Oxidative Stress*
Oxygen / toxicity
Peroxiredoxins / biosynthesis*
Peroxiredoxins / genetics
Protein Subunits / biosynthesis
Protein Subunits / genetics
Reactive Oxygen Species / metabolism*
Reactive Oxygen Species / toxicity
Stress, Physiological*

Substances

Benzene Derivatives
Protein Subunits
Reactive Oxygen Species
Hydrogen Peroxide
Peroxiredoxins
cumene hydroperoxide
Oxygen