Proteomic analysis of Lactobacillus casei in response to different pHs using two-dimensional electrophoresis and MALDI TOF mass spectroscopy
Background and Objectives: Lactobacillus casei, an acid-resistant bacterium, has a protective role against the pathogens. So we aimed to determine the proteome of Lactobacillus casei ATCC39392 strain in response to different pHs of 5 and 7 using proteomic analysis. Materials and Methods: Supernatan...
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Tehran University of Medical Sciences
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doaj-fc28dbef0ffb46abb6a371464ce124a02020-12-02T06:37:13ZengTehran University of Medical SciencesIranian Journal of Microbiology2008-32892008-44472020-10-0112510.18502/ijm.v12i5.4604Proteomic analysis of Lactobacillus casei in response to different pHs using two-dimensional electrophoresis and MALDI TOF mass spectroscopyNarges Dadfarma0Golgis Karimi1Jamileh Nowroozi2Naser Nejadi3Bahram Kazemi4Mojgan Bandehpour5Department of Microbiology, North Tehran Branch, Islamic Azad University, Tehran, IranCellular and Molecular Biology Research Center, Shahid Beheshti University of Medical Sciences, Tehran, IranDepartment of Microbiology, North Tehran Branch, Islamic Azad University, Tehran, IranProteomics Research Center, School of Paramedical Sciences, Shahid Beheshti University of Medical Sciences, Tehran, IranCellular and Molecular Biology Research Center, Shahid Beheshti University of Medical Sciences, Tehran, IranDepartment of Medical Biotechnology, School of Advanced Technologies in Medicine, Shahid Beheshti University of Medical Sciences, Tehran, Iran Background and Objectives: Lactobacillus casei, an acid-resistant bacterium, has a protective role against the pathogens. So we aimed to determine the proteome of Lactobacillus casei ATCC39392 strain in response to different pHs of 5 and 7 using proteomic analysis. Materials and Methods: Supernatant and bacterial extraction of Lactobacillus casei ATCC39392 adapts at pHs 5 and 7 were isolated using sodium dodecyl sulfate–polyacrylamide gel and two-dimensional gel electrophoresis. The comparison of results showed that 7 protein spots were seen in pH 5 but not in pH 7. Afterward, they were excised and sent for Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry (MALDI-TOF MS) to be identified. Results: Seven different proteins (four secretory and three structural) with different roles in human body health were identified. Prescribed proteins include putative cell wall associated Hydrolase, Glycoside Hydrolase, beta-N-Acetyl hexosaminidase, Histidine Kinase, Chaperonin, metal dependent Hydrolase and Lysozyme. Conclusion: Seven isolated proteins with anti-cancer and digestive impresses are proper subjects in therapy or drug delivery approaches especially oral drug usage for protection against stomach acidic area. https://ijm.tums.ac.ir/index.php/ijm/article/view/2643Lactobacillus casei;Acid tolerance;Anti-cancer;Digestive impresses;Two-dimensional gel;Mass spectrometry |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Narges Dadfarma Golgis Karimi Jamileh Nowroozi Naser Nejadi Bahram Kazemi Mojgan Bandehpour |
spellingShingle |
Narges Dadfarma Golgis Karimi Jamileh Nowroozi Naser Nejadi Bahram Kazemi Mojgan Bandehpour Proteomic analysis of Lactobacillus casei in response to different pHs using two-dimensional electrophoresis and MALDI TOF mass spectroscopy Iranian Journal of Microbiology Lactobacillus casei; Acid tolerance; Anti-cancer; Digestive impresses; Two-dimensional gel; Mass spectrometry |
author_facet |
Narges Dadfarma Golgis Karimi Jamileh Nowroozi Naser Nejadi Bahram Kazemi Mojgan Bandehpour |
author_sort |
Narges Dadfarma |
title |
Proteomic analysis of Lactobacillus casei in response to different pHs using two-dimensional electrophoresis and MALDI TOF mass spectroscopy |
title_short |
Proteomic analysis of Lactobacillus casei in response to different pHs using two-dimensional electrophoresis and MALDI TOF mass spectroscopy |
title_full |
Proteomic analysis of Lactobacillus casei in response to different pHs using two-dimensional electrophoresis and MALDI TOF mass spectroscopy |
title_fullStr |
Proteomic analysis of Lactobacillus casei in response to different pHs using two-dimensional electrophoresis and MALDI TOF mass spectroscopy |
title_full_unstemmed |
Proteomic analysis of Lactobacillus casei in response to different pHs using two-dimensional electrophoresis and MALDI TOF mass spectroscopy |
title_sort |
proteomic analysis of lactobacillus casei in response to different phs using two-dimensional electrophoresis and maldi tof mass spectroscopy |
publisher |
Tehran University of Medical Sciences |
series |
Iranian Journal of Microbiology |
issn |
2008-3289 2008-4447 |
publishDate |
2020-10-01 |
description |
Background and Objectives: Lactobacillus casei, an acid-resistant bacterium, has a protective role against the pathogens. So we aimed to determine the proteome of Lactobacillus casei ATCC39392 strain in response to different pHs of 5 and 7 using proteomic analysis.
Materials and Methods: Supernatant and bacterial extraction of Lactobacillus casei ATCC39392 adapts at pHs 5 and 7 were isolated using sodium dodecyl sulfate–polyacrylamide gel and two-dimensional gel electrophoresis. The comparison of results showed that 7 protein spots were seen in pH 5 but not in pH 7. Afterward, they were excised and sent for Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry (MALDI-TOF MS) to be identified.
Results: Seven different proteins (four secretory and three structural) with different roles in human body health were identified. Prescribed proteins include putative cell wall associated Hydrolase, Glycoside Hydrolase, beta-N-Acetyl hexosaminidase, Histidine Kinase, Chaperonin, metal dependent Hydrolase and Lysozyme.
Conclusion: Seven isolated proteins with anti-cancer and digestive impresses are proper subjects in therapy or drug delivery approaches especially oral drug usage for protection against stomach acidic area.
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topic |
Lactobacillus casei; Acid tolerance; Anti-cancer; Digestive impresses; Two-dimensional gel; Mass spectrometry |
url |
https://ijm.tums.ac.ir/index.php/ijm/article/view/2643 |
work_keys_str_mv |
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