The Discovery of New Antilisterial Proteins From Paenibacillus polymyxa Kp10 via Genome Mining and Mass Spectrometry
The inhibitory properties of novel antimicrobial proteins against food-borne pathogens such as Listeria monocytogenes offer extensive benefits to the food and medical industries. In this study, we have identified antimicrobial proteins from a milk curd–derived bacterial isolate that exhibits antilis...
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Frontiers Media S.A.
2020-07-01
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Online Access: | https://www.frontiersin.org/article/10.3389/fmicb.2020.00960/full |
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author | Nur Fadhilah Khairil Mokhtar Nur Fadhilah Khairil Mokhtar Amalia Mohd Hashim Amalia Mohd Hashim Irwan Hanish Aisyah Zulkarnain Raja Mohd Hafidz Raja Nhari Asmahani Azira Abdul Sani Sahar Abbasiliasi Arbakariya Ariff Shuhaimi Mustafa Shuhaimi Mustafa Shuhaimi Mustafa Raha Abdul Rahim Raha Abdul Rahim |
author_facet | Nur Fadhilah Khairil Mokhtar Nur Fadhilah Khairil Mokhtar Amalia Mohd Hashim Amalia Mohd Hashim Irwan Hanish Aisyah Zulkarnain Raja Mohd Hafidz Raja Nhari Asmahani Azira Abdul Sani Sahar Abbasiliasi Arbakariya Ariff Shuhaimi Mustafa Shuhaimi Mustafa Shuhaimi Mustafa Raha Abdul Rahim Raha Abdul Rahim |
author_sort | Nur Fadhilah Khairil Mokhtar |
collection | DOAJ |
description | The inhibitory properties of novel antimicrobial proteins against food-borne pathogens such as Listeria monocytogenes offer extensive benefits to the food and medical industries. In this study, we have identified antimicrobial proteins from a milk curd–derived bacterial isolate that exhibits antilisterial activity using genome mining and mass spectrometry analysis. The analysis of the draft genome sequence identified the isolate as Paenibacillus polymyxa Kp10, and predicted the presence of antimicrobial paenibacillin, paenilan, paeninodin, sactipeptides, thiazole-oxazole modified microcin, and histone-like DNA binding protein HU encoded in its genome. Interestingly, nanoLC-MS/MS analysis identified two histone-like DNA binding proteins HU as predicted in silico earlier, exhibiting antilisterial activity. Additionally, translation initiation factor IF-1 and 50S ribosomal protein L29 were also discovered by the mass spectrometry in the active fractions. The antilisterial activity of the four proteins was verified through heterologous protein expression and antimicrobial activity assay in vitro. This study has identified structural regulatory proteins from Paenibacillus possessing antilisterial activity with potential future application in the food and medical industries. |
first_indexed | 2024-12-23T04:54:46Z |
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id | doaj.art-bba3c215f5ae421f9eccb6facb48bb4e |
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issn | 1664-302X |
language | English |
last_indexed | 2024-12-23T04:54:46Z |
publishDate | 2020-07-01 |
publisher | Frontiers Media S.A. |
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series | Frontiers in Microbiology |
spelling | doaj.art-bba3c215f5ae421f9eccb6facb48bb4e2022-12-21T17:59:22ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2020-07-011110.3389/fmicb.2020.00960521464The Discovery of New Antilisterial Proteins From Paenibacillus polymyxa Kp10 via Genome Mining and Mass SpectrometryNur Fadhilah Khairil Mokhtar0Nur Fadhilah Khairil Mokhtar1Amalia Mohd Hashim2Amalia Mohd Hashim3Irwan Hanish4Aisyah Zulkarnain5Raja Mohd Hafidz Raja Nhari6Asmahani Azira Abdul Sani7Sahar Abbasiliasi8Arbakariya Ariff9Shuhaimi Mustafa10Shuhaimi Mustafa11Shuhaimi Mustafa12Raha Abdul Rahim13Raha Abdul Rahim14Department of Cell and Molecular Biology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Selangor, MalaysiaHalal Products Research Institute, Putra Infoport, Universiti Putra Malaysia, Selangor, MalaysiaHalal Products Research Institute, Putra Infoport, Universiti Putra Malaysia, Selangor, MalaysiaDepartment of Microbiology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Selangor, MalaysiaDepartment of Microbiology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Selangor, MalaysiaHalal Products Research Institute, Putra Infoport, Universiti Putra Malaysia, Selangor, MalaysiaHalal Products Research Institute, Putra Infoport, Universiti Putra Malaysia, Selangor, MalaysiaMass Spectrometry Technology Section, Malaysia Genome Institute, National Institute of Biotechnology Malaysia, Kajang, MalaysiaHalal Products Research Institute, Putra Infoport, Universiti Putra Malaysia, Selangor, MalaysiaBioprocessing and Biomanufacturing Research Centre, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Selangor, MalaysiaHalal Products Research Institute, Putra Infoport, Universiti Putra Malaysia, Selangor, MalaysiaDepartment of Microbiology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Selangor, MalaysiaBioprocessing and Biomanufacturing Research Centre, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Selangor, MalaysiaDepartment of Cell and Molecular Biology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Selangor, MalaysiaChancellory, Universiti Teknikal Malaysia Melaka, Malacca, MalaysiaThe inhibitory properties of novel antimicrobial proteins against food-borne pathogens such as Listeria monocytogenes offer extensive benefits to the food and medical industries. In this study, we have identified antimicrobial proteins from a milk curd–derived bacterial isolate that exhibits antilisterial activity using genome mining and mass spectrometry analysis. The analysis of the draft genome sequence identified the isolate as Paenibacillus polymyxa Kp10, and predicted the presence of antimicrobial paenibacillin, paenilan, paeninodin, sactipeptides, thiazole-oxazole modified microcin, and histone-like DNA binding protein HU encoded in its genome. Interestingly, nanoLC-MS/MS analysis identified two histone-like DNA binding proteins HU as predicted in silico earlier, exhibiting antilisterial activity. Additionally, translation initiation factor IF-1 and 50S ribosomal protein L29 were also discovered by the mass spectrometry in the active fractions. The antilisterial activity of the four proteins was verified through heterologous protein expression and antimicrobial activity assay in vitro. This study has identified structural regulatory proteins from Paenibacillus possessing antilisterial activity with potential future application in the food and medical industries.https://www.frontiersin.org/article/10.3389/fmicb.2020.00960/fullantilisterial proteingenome miningheterologous protein expressionmass spectrometryPaenibacillus polymyxa Kp10Listeria monocytogenes |
spellingShingle | Nur Fadhilah Khairil Mokhtar Nur Fadhilah Khairil Mokhtar Amalia Mohd Hashim Amalia Mohd Hashim Irwan Hanish Aisyah Zulkarnain Raja Mohd Hafidz Raja Nhari Asmahani Azira Abdul Sani Sahar Abbasiliasi Arbakariya Ariff Shuhaimi Mustafa Shuhaimi Mustafa Shuhaimi Mustafa Raha Abdul Rahim Raha Abdul Rahim The Discovery of New Antilisterial Proteins From Paenibacillus polymyxa Kp10 via Genome Mining and Mass Spectrometry Frontiers in Microbiology antilisterial protein genome mining heterologous protein expression mass spectrometry Paenibacillus polymyxa Kp10 Listeria monocytogenes |
title | The Discovery of New Antilisterial Proteins From Paenibacillus polymyxa Kp10 via Genome Mining and Mass Spectrometry |
title_full | The Discovery of New Antilisterial Proteins From Paenibacillus polymyxa Kp10 via Genome Mining and Mass Spectrometry |
title_fullStr | The Discovery of New Antilisterial Proteins From Paenibacillus polymyxa Kp10 via Genome Mining and Mass Spectrometry |
title_full_unstemmed | The Discovery of New Antilisterial Proteins From Paenibacillus polymyxa Kp10 via Genome Mining and Mass Spectrometry |
title_short | The Discovery of New Antilisterial Proteins From Paenibacillus polymyxa Kp10 via Genome Mining and Mass Spectrometry |
title_sort | discovery of new antilisterial proteins from paenibacillus polymyxa kp10 via genome mining and mass spectrometry |
topic | antilisterial protein genome mining heterologous protein expression mass spectrometry Paenibacillus polymyxa Kp10 Listeria monocytogenes |
url | https://www.frontiersin.org/article/10.3389/fmicb.2020.00960/full |
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