4.7 Article

Integration of transcriptomic and proteomic reveals the toxicological molecular mechanisms of decabromodiphenyl ethane (DBDPE) on Pleurotus ostreatus

Journal

ENVIRONMENTAL POLLUTION
Volume 314, Issue -, Pages -

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.envpol.2022.120263

Keywords

Decabromodiphenyl ethane (DBDPE); New brominated flame retardants (NBFRs); White rot fungus; Transcriptomic; Proteomic

Funding

  1. Natural Science Foundation of Heilongjiang Province, China [LH 2020D010]
  2. Open Project of State Key Laboratory of Urban Water Resource and Environment, Harbin Institute of Technology,Harbin , China [ESK202207]
  3. Heilongjiang Key Laboratory of Ozone Application Technology and Equipment Development (Harbin Institute of Technology) [OZO20210x]

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This study investigated the toxicological molecular mechanisms of Pleurotus ostreatus during the biodegradation of Decabromodiphenyl ethane (DBDPE). Transcriptome and proteome analysis revealed differentially expressed genes and proteins involved in cellular processes, metabolic processes, oxidation-reduction processes, and membrane-related functions. Key enzymes associated with oxidative phosphorylation and the tricarboxylic acid cycle were down-regulated by DBDPE exposure. Cytochrome P450 enzymes and stress proteins were induced to participate in DBDPE degradation and resist its toxicity. These findings contribute to a better understanding of the effects of DBDPE on P. ostreatus and provide insights for improving DBDPE removal.
Decabromodiphenyl ethane (DBDPE), as one of the most widely used new brominated flame retardants (NBFRs), can pose a potential threat to human health and the environment. An integrated transcriptome and proteome was performed for investigating the toxicological molecular mechanisms of Pleurotus ostreatus (P. ostreatus) during the biodegradation of DBDPE at the concentrations of 5 and 20 mg/L. A total of 1193/1018 and 92/126 differentially expressed genes/proteins (DEGs/DEPs) were found, respectively, with DBDPE exposure at 5 and 20 mg/L. These DEGs and DEPs were mainly involved in the cellular process as well as metabolic process. DEPs for oxidationreduction process and hydrolase activity were up-regulated, and those for membrane, lipid metabolic process and transmembrane transport were down-regulated. The DEGs and DEPs related to some key enzymes were down-regulated, such as NADH dehydrogenase/oxidoreductase, succinate dehydrogenase, cytochrome C1 protein, cytochrome-c oxidase/reductase and ATP synthase, which indicated that DBDPE affected the oxidative phosphorylation as well as tricarboxylic acid (TCA) cycle. Cytochrome P450 enzymes (CYPs) might be involved in DBDPE degradation through hydroxylation and oxidation. Some stress proteins were induced to resist DBDPE toxicity, including major facilitator superfamily (MFS) transporter, superoxide dismutase (SOD), molecular chaperones, heat shock proteins (HSP20, HSP26, HSP42), 60S ribosomal protein and histone H4. The findings help revealing the toxicological molecular mechanisms of DBDPE on P. ostreatus, aiming to improve the removal of DBDPE.

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