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The Landscape of Pseudomonas aeruginosa Membrane-Associated Proteins
Background: Pseudomonas aeruginosa cell envelope-associated proteins play a relevant role in infection mechanisms. They can contribute to the antibiotic resistance of the bacterial cells and be involved in the interaction with host cells. Thus, studies contributing to elucidating these key molecular...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7694347/ https://www.ncbi.nlm.nih.gov/pubmed/33167383 http://dx.doi.org/10.3390/cells9112421 |
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author | Motta, Sara Vecchietti, Davide Martorana, Alessandra M. Brunetti, Pietro Bertoni, Giovanni Polissi, Alessandra Mauri, Pierluigi Di Silvestre, Dario |
author_facet | Motta, Sara Vecchietti, Davide Martorana, Alessandra M. Brunetti, Pietro Bertoni, Giovanni Polissi, Alessandra Mauri, Pierluigi Di Silvestre, Dario |
author_sort | Motta, Sara |
collection | PubMed |
description | Background: Pseudomonas aeruginosa cell envelope-associated proteins play a relevant role in infection mechanisms. They can contribute to the antibiotic resistance of the bacterial cells and be involved in the interaction with host cells. Thus, studies contributing to elucidating these key molecular elements are of great importance to find alternative therapeutics. Methods: Proteins and peptides were extracted by different methods and analyzed by Multidimensional Protein Identification Technology (MudPIT) approach. Proteomic data were processed by Discoverer2.1 software and multivariate statistics, i.e., Linear Discriminant Analysis (LDA), while the Immune Epitope Database (IEDB) resources were used to predict antigenicity and immunogenicity of experimental identified peptides and proteins. Results: The combination of 29 MudPIT runs allowed the identification of 10,611 peptides and 2539 distinct proteins. Following application of extraction methods enriching specific protein domains, about 15% of total identified peptides were classified in trans inner-membrane, inner-membrane exposed, trans outer-membrane and outer-membrane exposed. In this scenario, nine outer membrane proteins (OprE, OprI, OprF, OprD, PagL, OprG, PA1053, PAL and PA0833) were predicted to be highly antigenic. Thus, they were further processed and epitopes target of T cells (MHC Class I and Class II) and B cells were predicted. Conclusion: The present study represents one of the widest characterizations of the P. aeruginosa membrane-associated proteome. The feasibility of our method may facilitates the investigation of other bacterial species whose envelope exposed protein domains are still unknown. Besides, the stepwise prioritization of proteome, by combining experimental proteomic data and reverse vaccinology, may be useful for reducing the number of proteins to be tested in vaccine development. |
format | Online Article Text |
id | pubmed-7694347 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-76943472020-11-28 The Landscape of Pseudomonas aeruginosa Membrane-Associated Proteins Motta, Sara Vecchietti, Davide Martorana, Alessandra M. Brunetti, Pietro Bertoni, Giovanni Polissi, Alessandra Mauri, Pierluigi Di Silvestre, Dario Cells Article Background: Pseudomonas aeruginosa cell envelope-associated proteins play a relevant role in infection mechanisms. They can contribute to the antibiotic resistance of the bacterial cells and be involved in the interaction with host cells. Thus, studies contributing to elucidating these key molecular elements are of great importance to find alternative therapeutics. Methods: Proteins and peptides were extracted by different methods and analyzed by Multidimensional Protein Identification Technology (MudPIT) approach. Proteomic data were processed by Discoverer2.1 software and multivariate statistics, i.e., Linear Discriminant Analysis (LDA), while the Immune Epitope Database (IEDB) resources were used to predict antigenicity and immunogenicity of experimental identified peptides and proteins. Results: The combination of 29 MudPIT runs allowed the identification of 10,611 peptides and 2539 distinct proteins. Following application of extraction methods enriching specific protein domains, about 15% of total identified peptides were classified in trans inner-membrane, inner-membrane exposed, trans outer-membrane and outer-membrane exposed. In this scenario, nine outer membrane proteins (OprE, OprI, OprF, OprD, PagL, OprG, PA1053, PAL and PA0833) were predicted to be highly antigenic. Thus, they were further processed and epitopes target of T cells (MHC Class I and Class II) and B cells were predicted. Conclusion: The present study represents one of the widest characterizations of the P. aeruginosa membrane-associated proteome. The feasibility of our method may facilitates the investigation of other bacterial species whose envelope exposed protein domains are still unknown. Besides, the stepwise prioritization of proteome, by combining experimental proteomic data and reverse vaccinology, may be useful for reducing the number of proteins to be tested in vaccine development. MDPI 2020-11-05 /pmc/articles/PMC7694347/ /pubmed/33167383 http://dx.doi.org/10.3390/cells9112421 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Motta, Sara Vecchietti, Davide Martorana, Alessandra M. Brunetti, Pietro Bertoni, Giovanni Polissi, Alessandra Mauri, Pierluigi Di Silvestre, Dario The Landscape of Pseudomonas aeruginosa Membrane-Associated Proteins |
title | The Landscape of Pseudomonas aeruginosa Membrane-Associated Proteins |
title_full | The Landscape of Pseudomonas aeruginosa Membrane-Associated Proteins |
title_fullStr | The Landscape of Pseudomonas aeruginosa Membrane-Associated Proteins |
title_full_unstemmed | The Landscape of Pseudomonas aeruginosa Membrane-Associated Proteins |
title_short | The Landscape of Pseudomonas aeruginosa Membrane-Associated Proteins |
title_sort | landscape of pseudomonas aeruginosa membrane-associated proteins |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7694347/ https://www.ncbi.nlm.nih.gov/pubmed/33167383 http://dx.doi.org/10.3390/cells9112421 |
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