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Quantitative proteomic analysis of host—pathogen interactions: a study of Acinetobacter baumannii responses to host airways
BACKGROUND: Acinetobacter baumannii is a major health problem. The most common infection caused by A. baumannii is hospital acquired pneumonia, and the associated mortality rate is approximately 50 %. Neither in vivo nor ex vivo expression profiling has been performed at the proteomic or transcripto...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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BioMed Central
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4449591/ https://www.ncbi.nlm.nih.gov/pubmed/26025090 http://dx.doi.org/10.1186/s12864-015-1608-z |
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author | Méndez, Jose Antonio Mateos, Jesús Beceiro, Alejandro Lopez, María Tomás, María Poza, Margarita Bou, Germán |
author_facet | Méndez, Jose Antonio Mateos, Jesús Beceiro, Alejandro Lopez, María Tomás, María Poza, Margarita Bou, Germán |
author_sort | Méndez, Jose Antonio |
collection | PubMed |
description | BACKGROUND: Acinetobacter baumannii is a major health problem. The most common infection caused by A. baumannii is hospital acquired pneumonia, and the associated mortality rate is approximately 50 %. Neither in vivo nor ex vivo expression profiling has been performed at the proteomic or transcriptomic level for pneumonia caused by A. baumannii. In this study, we characterized the proteome of A. baumannii under conditions that simulate those found in the airways, to gain some insight into how A. baumannii adapts to the host and to improve knowledge about the pathogenesis and virulence of this bacterium. A clinical strain of A. baumannii was grown under different conditions: in the presence of bronchoalveolar lavage fluid from infected rats, of RAW 264.7 cells to simulate conditions in the respiratory tract and in control conditions. We used iTRAQ labelling and LC-MALDI-TOF/TOF to investigate how A. baumannii responds on exposure to macrophages/BALF. RESULTS: 179 proteins showed differential expression. In both models, proteins involved in the following processes were over-expressed: (i) pathogenesis and virulence (OmpA, YjjK); (ii) cell wall/membrane/envelope biogenesis (MurC); (iii) energy production and conversion (acetyl-CoA hydrolase); and (iv) translation (50S ribosomal protein L9). Proteins involved in the following were under-expressed: (i) lipid metabolism (short-chain dehydrogenase); (ii) amino acid metabolism and transport (aspartate aminotransferase); (iii) unknown function (DNA-binding protein); and (iv) inorganic ion transport and metabolism (hydroperoxidase). CONCLUSIONS: We observed alterations in cell wall synthesis and identified 2 upregulated virulence-associated proteins with >15 peptides/protein in both ex vivo models (OmpA and YjjK), suggesting that these proteins are fundamental for pathogenesis and virulence in the airways. This study is the first comprehensive overview of the ex vivo proteome of A. baumannii and is an important step towards identification of diagnostic biomarkers, novel drug targets and potential vaccine candidates in the fight against pneumonia caused by A. baumannii. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12864-015-1608-z) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-4449591 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-44495912015-05-31 Quantitative proteomic analysis of host—pathogen interactions: a study of Acinetobacter baumannii responses to host airways Méndez, Jose Antonio Mateos, Jesús Beceiro, Alejandro Lopez, María Tomás, María Poza, Margarita Bou, Germán BMC Genomics Research Article BACKGROUND: Acinetobacter baumannii is a major health problem. The most common infection caused by A. baumannii is hospital acquired pneumonia, and the associated mortality rate is approximately 50 %. Neither in vivo nor ex vivo expression profiling has been performed at the proteomic or transcriptomic level for pneumonia caused by A. baumannii. In this study, we characterized the proteome of A. baumannii under conditions that simulate those found in the airways, to gain some insight into how A. baumannii adapts to the host and to improve knowledge about the pathogenesis and virulence of this bacterium. A clinical strain of A. baumannii was grown under different conditions: in the presence of bronchoalveolar lavage fluid from infected rats, of RAW 264.7 cells to simulate conditions in the respiratory tract and in control conditions. We used iTRAQ labelling and LC-MALDI-TOF/TOF to investigate how A. baumannii responds on exposure to macrophages/BALF. RESULTS: 179 proteins showed differential expression. In both models, proteins involved in the following processes were over-expressed: (i) pathogenesis and virulence (OmpA, YjjK); (ii) cell wall/membrane/envelope biogenesis (MurC); (iii) energy production and conversion (acetyl-CoA hydrolase); and (iv) translation (50S ribosomal protein L9). Proteins involved in the following were under-expressed: (i) lipid metabolism (short-chain dehydrogenase); (ii) amino acid metabolism and transport (aspartate aminotransferase); (iii) unknown function (DNA-binding protein); and (iv) inorganic ion transport and metabolism (hydroperoxidase). CONCLUSIONS: We observed alterations in cell wall synthesis and identified 2 upregulated virulence-associated proteins with >15 peptides/protein in both ex vivo models (OmpA and YjjK), suggesting that these proteins are fundamental for pathogenesis and virulence in the airways. This study is the first comprehensive overview of the ex vivo proteome of A. baumannii and is an important step towards identification of diagnostic biomarkers, novel drug targets and potential vaccine candidates in the fight against pneumonia caused by A. baumannii. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12864-015-1608-z) contains supplementary material, which is available to authorized users. BioMed Central 2015-05-30 /pmc/articles/PMC4449591/ /pubmed/26025090 http://dx.doi.org/10.1186/s12864-015-1608-z Text en © Méndez et al.; licensee BioMed Central. 2015 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Article Méndez, Jose Antonio Mateos, Jesús Beceiro, Alejandro Lopez, María Tomás, María Poza, Margarita Bou, Germán Quantitative proteomic analysis of host—pathogen interactions: a study of Acinetobacter baumannii responses to host airways |
title | Quantitative proteomic analysis of host—pathogen interactions: a study of Acinetobacter baumannii responses to host airways |
title_full | Quantitative proteomic analysis of host—pathogen interactions: a study of Acinetobacter baumannii responses to host airways |
title_fullStr | Quantitative proteomic analysis of host—pathogen interactions: a study of Acinetobacter baumannii responses to host airways |
title_full_unstemmed | Quantitative proteomic analysis of host—pathogen interactions: a study of Acinetobacter baumannii responses to host airways |
title_short | Quantitative proteomic analysis of host—pathogen interactions: a study of Acinetobacter baumannii responses to host airways |
title_sort | quantitative proteomic analysis of host—pathogen interactions: a study of acinetobacter baumannii responses to host airways |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4449591/ https://www.ncbi.nlm.nih.gov/pubmed/26025090 http://dx.doi.org/10.1186/s12864-015-1608-z |
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