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Extracellular proteins enhance Cupriavidus pauculus nickel tolerance and cell aggregate formation

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Extracellular proteins enhance Cupriavidus pauculus nickel tolerance and cell aggregate formation. / Wang, Mingwei; Vollstedt, Christel; Siebels, Bente; Yu, Huang; Wu, Xueling; Shen, Li; Li, Jiaokun; Liu, Yuandong; Yu, Runlan; Streit, Wolfgang R; Zeng, Weimin.

In: BIORESOURCE TECHNOL, Vol. 393, 02.2024, p. 130133.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Wang, M, Vollstedt, C, Siebels, B, Yu, H, Wu, X, Shen, L, Li, J, Liu, Y, Yu, R, Streit, WR & Zeng, W 2024, 'Extracellular proteins enhance Cupriavidus pauculus nickel tolerance and cell aggregate formation', BIORESOURCE TECHNOL, vol. 393, pp. 130133. https://doi.org/10.1016/j.biortech.2023.130133

APA

Wang, M., Vollstedt, C., Siebels, B., Yu, H., Wu, X., Shen, L., Li, J., Liu, Y., Yu, R., Streit, W. R., & Zeng, W. (2024). Extracellular proteins enhance Cupriavidus pauculus nickel tolerance and cell aggregate formation. BIORESOURCE TECHNOL, 393, 130133. https://doi.org/10.1016/j.biortech.2023.130133

Vancouver

Wang M, Vollstedt C, Siebels B, Yu H, Wu X, Shen L et al. Extracellular proteins enhance Cupriavidus pauculus nickel tolerance and cell aggregate formation. BIORESOURCE TECHNOL. 2024 Feb;393:130133. https://doi.org/10.1016/j.biortech.2023.130133

Bibtex

@article{dbd433d776174b6d8ef12f15605fefa1,
title = "Extracellular proteins enhance Cupriavidus pauculus nickel tolerance and cell aggregate formation",
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 = "Nickel, Proteomics, Metals, Heavy/metabolism, Cupriavidus/metabolism",
author = "Mingwei Wang and Christel Vollstedt and Bente Siebels and Huang Yu and Xueling Wu and Li Shen and Jiaokun Li and Yuandong Liu and Runlan Yu and Streit, {Wolfgang R} and Weimin Zeng",
note = "Copyright {\textcopyright} 2023 Elsevier Ltd. All rights reserved.",
year = "2024",
month = feb,
doi = "10.1016/j.biortech.2023.130133",
language = "English",
volume = "393",
pages = "130133",
journal = "BIORESOURCE TECHNOL",
issn = "0960-8524",
publisher = "Elsevier Limited",

}

RIS

TY - JOUR

T1 - Extracellular proteins enhance Cupriavidus pauculus nickel tolerance and cell aggregate formation

AU - Wang, Mingwei

AU - Vollstedt, Christel

AU - Siebels, Bente

AU - Yu, Huang

AU - Wu, Xueling

AU - Shen, Li

AU - Li, Jiaokun

AU - Liu, Yuandong

AU - Yu, Runlan

AU - Streit, Wolfgang R

AU - Zeng, Weimin

N1 - Copyright © 2023 Elsevier Ltd. All rights reserved.

PY - 2024/2

Y1 - 2024/2

N2 - 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+.

AB - 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+.

KW - Nickel

KW - Proteomics

KW - Metals, Heavy/metabolism

KW - Cupriavidus/metabolism

U2 - 10.1016/j.biortech.2023.130133

DO - 10.1016/j.biortech.2023.130133

M3 - SCORING: Journal article

C2 - 38043689

VL - 393

SP - 130133

JO - BIORESOURCE TECHNOL

JF - BIORESOURCE TECHNOL

SN - 0960-8524

ER -