Proteomic dataset of Listeria monocytogenes exposed to sublethal concentrations of free and nanoencapsulated nisin
The cellular proteins of L. monocytogenes exposed to free and liposome-encapsulated nisin at sublethal concentration were hydrolyzed by trypsin and examined by tandem mass spectrometry (MS/MS) to obtain proteomic data. In the present study, we use the STRING v11.05 database analyze the interactions...
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| Format: | Article |
| Language: | English |
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Elsevier
2022-08-01
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| Series: | Data in Brief |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2352340922005455 |
| _version_ | 1811216319978143744 |
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| author | Cristian Mauricio Barreto Pinilla Paolo Stincone Adriano Brandelli |
| author_facet | Cristian Mauricio Barreto Pinilla Paolo Stincone Adriano Brandelli |
| author_sort | Cristian Mauricio Barreto Pinilla |
| collection | DOAJ |
| description | The cellular proteins of L. monocytogenes exposed to free and liposome-encapsulated nisin at sublethal concentration were hydrolyzed by trypsin and examined by tandem mass spectrometry (MS/MS) to obtain proteomic data. In the present study, we use the STRING v11.05 database analyze the interactions among the 78 upregulated proteins from L. monocytogenes obtained after treatment with sublethal concentrations of free and nanoliposome-encapsulated nisin. As result, from the upregulated proteins by free nisin was determined a network with 140 edges with two relevant nodes, containing ribosomal proteins and transmembrane transport proteins (SecD and ABC transport system). These two sets of proteins present biological connection as a group, with strong interactions and are related to detoxification and other Listeria response mechanisms. In addition, a high amount of membrane proteins was identified in the free nisin treatment. On the other hand, in the interaction analysis of upregulated proteins by liposome-loaded nisin, was found 156 edges with a single protein network, the same observed in free nisin, related to ribosomal proteins. Therefore, according with this analysis, the encapsulation of nisin into liposomes cause upregulation of ribosomal and decrease of L. monocytogenes response proteins as compared with free nisin. |
| first_indexed | 2024-04-12T06:37:12Z |
| format | Article |
| id | doaj.art-b86bcf7dc22b4d588c0287563e28a1e2 |
| institution | Directory Open Access Journal |
| issn | 2352-3409 |
| language | English |
| last_indexed | 2024-04-12T06:37:12Z |
| publishDate | 2022-08-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Data in Brief |
| spelling | doaj.art-b86bcf7dc22b4d588c0287563e28a1e22022-12-22T03:43:51ZengElsevierData in Brief2352-34092022-08-0143108343Proteomic dataset of Listeria monocytogenes exposed to sublethal concentrations of free and nanoencapsulated nisinCristian Mauricio Barreto Pinilla0Paolo Stincone1Adriano Brandelli2Centro de Tecnologia de Lacticínios (TECNOLAT), Instituto de Tecnologia de Alimentos, Campinas, SP 13070-178, BrazilCMFI Cluster of Excellence, Interfaculty Institute of Microbiology and Medicine, University of Tübingen, Tübingen 72076, GermanyLaboratório de Bioquímica e Microbiologia Aplicada, Departamento de Ciência de Alimentos, Universidade Federal do Rio Grande do Sul, Porto Alegre 91501-970, Brazil; Corresponding author.The cellular proteins of L. monocytogenes exposed to free and liposome-encapsulated nisin at sublethal concentration were hydrolyzed by trypsin and examined by tandem mass spectrometry (MS/MS) to obtain proteomic data. In the present study, we use the STRING v11.05 database analyze the interactions among the 78 upregulated proteins from L. monocytogenes obtained after treatment with sublethal concentrations of free and nanoliposome-encapsulated nisin. As result, from the upregulated proteins by free nisin was determined a network with 140 edges with two relevant nodes, containing ribosomal proteins and transmembrane transport proteins (SecD and ABC transport system). These two sets of proteins present biological connection as a group, with strong interactions and are related to detoxification and other Listeria response mechanisms. In addition, a high amount of membrane proteins was identified in the free nisin treatment. On the other hand, in the interaction analysis of upregulated proteins by liposome-loaded nisin, was found 156 edges with a single protein network, the same observed in free nisin, related to ribosomal proteins. Therefore, according with this analysis, the encapsulation of nisin into liposomes cause upregulation of ribosomal and decrease of L. monocytogenes response proteins as compared with free nisin.http://www.sciencedirect.com/science/article/pii/S2352340922005455ProteomeTandem mass spectroscopyBacteriaprotein analysisAntimicrobialNisin |
| spellingShingle | Cristian Mauricio Barreto Pinilla Paolo Stincone Adriano Brandelli Proteomic dataset of Listeria monocytogenes exposed to sublethal concentrations of free and nanoencapsulated nisin Data in Brief Proteome Tandem mass spectroscopy Bacteria protein analysis Antimicrobial Nisin |
| title | Proteomic dataset of Listeria monocytogenes exposed to sublethal concentrations of free and nanoencapsulated nisin |
| title_full | Proteomic dataset of Listeria monocytogenes exposed to sublethal concentrations of free and nanoencapsulated nisin |
| title_fullStr | Proteomic dataset of Listeria monocytogenes exposed to sublethal concentrations of free and nanoencapsulated nisin |
| title_full_unstemmed | Proteomic dataset of Listeria monocytogenes exposed to sublethal concentrations of free and nanoencapsulated nisin |
| title_short | Proteomic dataset of Listeria monocytogenes exposed to sublethal concentrations of free and nanoencapsulated nisin |
| title_sort | proteomic dataset of listeria monocytogenes exposed to sublethal concentrations of free and nanoencapsulated nisin |
| topic | Proteome Tandem mass spectroscopy Bacteria protein analysis Antimicrobial Nisin |
| url | http://www.sciencedirect.com/science/article/pii/S2352340922005455 |
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