Insights into the differential proteome landscape of a newly isolated Paramecium multimicronucleatum in response to cadmium stress.

Autor: Zahra I; Institute of Zoology, University of the Punjab, New Campus, Lahore 54590, Pakistan. Electronic address: itrat.phd.zool@pu.edu.pk., DeVine L; Mass Spectrometry and Proteomics Facility, Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, USA. Electronic address: LaurenDeVine@jhmi.edu., Cole R; Mass Spectrometry and Proteomics Facility, Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, USA. Electronic address: rcole@jhmi.edu., Malik HA; Bioenergy Research Center, Department of Bioinformatics and Biotechnology, Government College University Faisalabad, Faisalabad 38000, Pakistan. Electronic address: aroosainam2@gmail.com., Wu J; Department of Chemical and Biomolecular Engineering, Johns Hopkins University, Baltimore, MD, USA. Electronic address: jwu154@jhu.edu., Wen J; Department of Chemical and Biomolecular Engineering, Johns Hopkins University, Baltimore, MD, USA. Electronic address: jwen25@jhu.edu., Hedfi A; Department of Biology, College of Sciences, Taif University, POBox 11099, Taif 21944, Saudi Arabia. Electronic address: o.zaied@tu.edu.sa., Liaqat A; Institute of Zoology, University of the Punjab, New Campus, Lahore 54590, Pakistan. Electronic address: ashoo223344@gmail.com., Ijaz R; Institute of Zoology, University of the Punjab, New Campus, Lahore 54590, Pakistan. Electronic address: roohi.phd.zool@pu.edu.pk., Ramzan U; Institute of Zoology, University of the Punjab, New Campus, Lahore 54590, Pakistan. Electronic address: uzmaramzan99@gmail.com., Shakoori AR; School of Biological Sciences, University of the Punjab, New Campus, Lahore 54590, Pakistan. Electronic address: arshaksbs@yahoo.com., Shakoori FR; Institute of Zoology, University of the Punjab, New Campus, Lahore 54590, Pakistan. Electronic address: farah.zool@pu.edu.pk., Betenbaugh MJ; Department of Chemical and Biomolecular Engineering, Johns Hopkins University, Baltimore, MD, USA. Electronic address: beten@jhu.edu.
Jazyk: angličtina
Zdroj: Journal of proteomics [J Proteomics] 2024 May 30; Vol. 300, pp. 105178. Date of Electronic Publication: 2024 Apr 16.
DOI: 10.1016/j.jprot.2024.105178
Abstrakt: Employing microbial systems for the bioremediation of contaminated waters represent a potential option, however, limited understanding of the underlying mechanisms hampers the implication of microbial-mediated bioremediation. The omics tools offer a promising approach to explore the molecular basis of the bioremediation process. Here, a mass spectrometry-based quantitative proteome profiling approach was conducted to explore the differential protein levels in cadmium-treated Paramecium multimicronucleatum. The Proteome Discoverer software was used to identify and quantify differentially abundant proteins. The proteome profiling generated 7,416 peptide spectral matches, yielding 2824 total peptides, corresponding to 989 proteins. The analysis revealed that 29 proteins exhibited significant (p ≤ 0.05) differential levels, including a higher abundance of 6 proteins and reduced levels of 23 proteins in Cd 2+ treated samples. These differentially abundant proteins were associated with stress response, energy metabolism, protein degradation, cell growth, and hormone processing. Briefly, a comprehensive proteome profile in response to cadmium stress of a newly isolated Paramecium has been established that will be useful in future studies identifying critical proteins involved in the bioremediation of metals in ciliates. SIGNIFICANCE: Ciliates are considered a good biological indicator of chemical pollution and relatively sensitive to heavy metal contamination. A prominent ciliate, Paramecium is a promising candidate for the bioremediation of polluted water. The proteins related to metal resistance in Paramecium species are still largely unknown and need further exploration. In order to identify and reveal the proteins related to metal resistance in Paramecia, we have reported differential protein abundance in Paramecium multimicronucleatum in response to cadmium stress. The proteins found in our study play essential roles during stress response, hormone processing, protein degradation, energy metabolism, and cell growth. It seems likely that Paramecia are not a simple sponge for metals but they could also transform them into less toxic derivatives or by detoxification by protein binding. This data will be helpful in future studies to identify critical proteins along with their detailed mechanisms involved in the bioremediation and detoxification of metal ions in Paramecium species.
Competing Interests: Declaration of competing interest The authors declared that they have no competing interests.
(Copyright © 2023. Published by Elsevier B.V.)
Databáze: MEDLINE
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