Identification of Lactobacillus acidophilus proteins by using 2-D Gel electrophoresis and MALDI- TOF under the influence of Sodium Fluoride

  • Unique Paper ID: 207706
  • Volume: 13
  • Issue: 3
  • PageNo: 2233-2237
  • Abstract:
  • Proteomics, the large-scale study of proteins, is an effective approach for understanding the molecular mechanisms and physiological responses of probiotic bacteria under stress conditions. Although proteomic investigations of probiotics are relatively recent, they have become increasingly important for elucidating bacterial metabolism, adaptation, and survival. In the present study, the proteomic response of Lactobacillus acidophilus to sodium fluoride treatment was investigated using two-dimensional gel electrophoresis (2D-GE). Protein profiles of treated and untreated cells were analyzed with Image Master 2D Platinum 6.0 software. A total of 170 protein spots were clearly resolved and detected on the gels. Among these, 12 protein spots exhibited significant differential expression in response to sodium fluoride exposure. Five protein spots were found to be upregulated, whereas seven were downregulated when compared with the control. The differentially expressed protein spots were excised and subjected to matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) for protein identification and functional characterization. The identified proteins were associated with diverse cellular processes, including metabolism, stress response, protein synthesis, and cellular adaptation. These findings provide insights into the molecular mechanisms employed by L. acidophilus to cope with fluoride-induced stress and enhance our understanding of the physiological adaptations of probiotic bacteria under adverse environmental conditions. This study demonstrates the utility of proteomic analysis in identifying stress-responsive proteins and contributes to the broader understanding of probiotic bacterial biology.

Copyright & License

Copyright © 2026 Authors retain the copyright of this article. This article is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

BibTeX

@article{207706,
        author = {Dr. P. Sandya Priya and Dr. P. Mohan and Dr. M. Aruna Kumari and Dr. Sujana Papani},
        title = {Identification of Lactobacillus acidophilus proteins by using 2-D Gel electrophoresis and MALDI- TOF under the influence of Sodium Fluoride},
        journal = {International Journal of Innovative Research in Technology},
        year = {2026},
        volume = {13},
        number = {3},
        pages = {2233-2237},
        issn = {2349-6002},
        url = {https://ijirt.org/article?manuscript=207706},
        abstract = {Proteomics, the large-scale study of proteins, is an effective approach for understanding the molecular mechanisms and physiological responses of probiotic bacteria under stress conditions. Although proteomic investigations of probiotics are relatively recent, they have become increasingly important for elucidating bacterial metabolism, adaptation, and survival. In the present study, the proteomic response of Lactobacillus acidophilus to sodium fluoride treatment was investigated using two-dimensional gel electrophoresis (2D-GE). Protein profiles of treated and untreated cells were analyzed with Image Master 2D Platinum 6.0 software. A total of 170 protein spots were clearly resolved and detected on the gels. Among these, 12 protein spots exhibited significant differential expression in response to sodium fluoride exposure. Five protein spots were found to be upregulated, whereas seven were downregulated when compared with the control. The differentially expressed protein spots were excised and subjected to matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) for protein identification and functional characterization. The identified proteins were associated with diverse cellular processes, including metabolism, stress response, protein synthesis, and cellular adaptation. These findings provide insights into the molecular mechanisms employed by L. acidophilus to cope with fluoride-induced stress and enhance our understanding of the physiological adaptations of probiotic bacteria under adverse environmental conditions. This study demonstrates the utility of proteomic analysis in identifying stress-responsive proteins and contributes to the broader understanding of probiotic bacterial biology.},
        keywords = {Proteomics, Lactobacillus acidophilus, Sodium fluoride, 2D gel electrophoresis, MALDI-TOF MS, Differential protein expression, Stress response.},
        month = {August},
        }

Cite This Article

Priya, D. P. S., & Mohan, D. P., & Kumari, D. M. A., & Papani, D. S. (2026). Identification of Lactobacillus acidophilus proteins by using 2-D Gel electrophoresis and MALDI- TOF under the influence of Sodium Fluoride. International Journal of Innovative Research in Technology (IJIRT), 13(3), 2233–2237.

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