Extracellular proteins enhance Cupriavidus pauculus nickel tolerance and cell aggregate formation

Mingwei Wang; Christel Vollstedt; Bente Siebels; Huang Yu; Xueling Wu; Li Shen; Jiaokun Li; Yuandong Liu; Runlan Yu; Wolfgang R Streit; Weimin Zeng

doi:10.1016/j.biortech.2023.130133

Extracellular proteins enhance Cupriavidus pauculus nickel tolerance and cell aggregate formation

Bioresour Technol. 2024 Feb:393:130133. doi: 10.1016/j.biortech.2023.130133. Epub 2023 Dec 1.

Authors

Mingwei Wang¹, Christel Vollstedt², Bente Siebels³, Huang Yu⁴, Xueling Wu⁵, Li Shen⁵, Jiaokun Li⁵, Yuandong Liu⁵, Runlan Yu⁵, Wolfgang R Streit⁶, Weimin Zeng⁷

Affiliations

¹ School of Minerals Processing and Bioengineering, Central South University, Changsha 410083, China; Department of Microbiology and Biotechnology, University of Hamburg, Hamburg 22609, Germany.
² Department of Microbiology and Biotechnology, University of Hamburg, Hamburg 22609, Germany.
³ Institute for Clinical Chemistry and Laboratory Medicine, University of Hamburg, Hamburg 20246, Germany.
⁴ Key Discipline Laboratory for National Defense for Biotechnology in Uranium Mining and Hydrometallurgy, University of South China, Hengyang 421001, China.
⁵ School of Minerals Processing and Bioengineering, Central South University, Changsha 410083, China; Key Laboratory of Biometallurgy, Ministry of Education, Changsha 410083, China.
⁶ Department of Microbiology and Biotechnology, University of Hamburg, Hamburg 22609, Germany. Electronic address: wolfgang.streit@uni-hamburg.de.
⁷ School of Minerals Processing and Bioengineering, Central South University, Changsha 410083, China; Key Laboratory of Biometallurgy, Ministry of Education, Changsha 410083, China. Electronic address: zengweimin1024@sina.com.

PMID: 38043689
DOI: 10.1016/j.biortech.2023.130133

Abstract

Heavy metal-resistant bacteria secrete extracellular proteins (e-PNs). However, the role of e-PNs in heavy metal resistance remains elusive. Here Fourier Transform Infrared Spectroscopy implied that N-H, C = O and NH₂-R played a crucial role in the adsorption and resistance of Ni²⁺ in the model organism Cuprividus pauculus 1490 (C. pauculus). Proteinase K treatment reduced Ni²⁺ resistance of C. pauculus underlining the essential role of e-PNs. Further three-dimension excitation-emission matrix fluorescence spectroscopy analysis demonstrated that tryptophan proteins as part of the e-PNs increased significantly with Ni²⁺ treatment. Proteomic and quantitative real-time polymerase chain reaction data indicated that major changes were induced in the metabolism of C. pauculus in response to Ni²⁺. Among those lipopolysaccharide biosynthesis, general secretion pathways, Ni²⁺-affiliated transporters and multidrug efflux play an essential role in Ni²⁺ resistance. Altogether the results provide a conceptual model for comprehending how e-PNs contribute to bacterial resistance and adsorption of Ni²⁺.

Keywords: Efflux pumps; Heavy metal resistance; Secretome.

MeSH terms

Cupriavidus* / metabolism
Metals, Heavy* / metabolism
Nickel
Proteomics

Substances

Nickel
Metals, Heavy

Supplementary concepts

Cupriavidus pauculus