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Putative Iron Acquisition Systems in Stenotrophomonas maltophilia
Iron has been shown to regulate biofilm formation, oxidative stress response and several pathogenic mechanisms in Stenotrophomonas maltophilia. Thus, the present study is aimed at identifying various iron acquisition systems and iron sources utilized during iron starvation in S. maltophilia. The ann...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6222749/ https://www.ncbi.nlm.nih.gov/pubmed/30115820 http://dx.doi.org/10.3390/molecules23082048 |
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author | Kalidasan, V. Azman, Adleen Joseph, Narcisse Kumar, Suresh Awang Hamat, Rukman Neela, Vasantha Kumari |
author_facet | Kalidasan, V. Azman, Adleen Joseph, Narcisse Kumar, Suresh Awang Hamat, Rukman Neela, Vasantha Kumari |
author_sort | Kalidasan, V. |
collection | PubMed |
description | Iron has been shown to regulate biofilm formation, oxidative stress response and several pathogenic mechanisms in Stenotrophomonas maltophilia. Thus, the present study is aimed at identifying various iron acquisition systems and iron sources utilized during iron starvation in S. maltophilia. The annotations of the complete genome of strains K279a, R551-3, D457 and JV3 through Rapid Annotations using Subsystems Technology (RAST) revealed two putative subsystems to be involved in iron acquisition: the iron siderophore sensor and receptor system and the heme, hemin uptake and utilization systems/hemin transport system. Screening for these acquisition systems in S. maltophilia showed the presence of all tested functional genes in clinical isolates, but only a few in environmental isolates. NanoString nCounter Elements technology, applied to determine the expression pattern of the genes under iron-depleted condition, showed significant expression for FeSR (6.15-fold), HmuT (12.21-fold), Hup (5.46-fold), ETFb (2.28-fold), TonB (2.03-fold) and Fur (3.30-fold). The isolates, when further screened for the production and chemical nature of siderophores using CAS agar diffusion (CASAD) and Arnows’s colorimetric assay, revealed S. maltophilia to produce catechol-type siderophore. Siderophore production was also tested through liquid CAS assay and was found to be greater in the clinical isolate (30.8%) compared to environmental isolates (4%). Both clinical and environmental isolates utilized hemoglobin, hemin, transferrin and lactoferrin as iron sources. All data put together indicates that S. maltophilia utilizes siderophore-mediated and heme-mediated systems for iron acquisition during iron starvation. These data need to be further confirmed through several knockout studies. |
format | Online Article Text |
id | pubmed-6222749 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-62227492018-11-13 Putative Iron Acquisition Systems in Stenotrophomonas maltophilia Kalidasan, V. Azman, Adleen Joseph, Narcisse Kumar, Suresh Awang Hamat, Rukman Neela, Vasantha Kumari Molecules Article Iron has been shown to regulate biofilm formation, oxidative stress response and several pathogenic mechanisms in Stenotrophomonas maltophilia. Thus, the present study is aimed at identifying various iron acquisition systems and iron sources utilized during iron starvation in S. maltophilia. The annotations of the complete genome of strains K279a, R551-3, D457 and JV3 through Rapid Annotations using Subsystems Technology (RAST) revealed two putative subsystems to be involved in iron acquisition: the iron siderophore sensor and receptor system and the heme, hemin uptake and utilization systems/hemin transport system. Screening for these acquisition systems in S. maltophilia showed the presence of all tested functional genes in clinical isolates, but only a few in environmental isolates. NanoString nCounter Elements technology, applied to determine the expression pattern of the genes under iron-depleted condition, showed significant expression for FeSR (6.15-fold), HmuT (12.21-fold), Hup (5.46-fold), ETFb (2.28-fold), TonB (2.03-fold) and Fur (3.30-fold). The isolates, when further screened for the production and chemical nature of siderophores using CAS agar diffusion (CASAD) and Arnows’s colorimetric assay, revealed S. maltophilia to produce catechol-type siderophore. Siderophore production was also tested through liquid CAS assay and was found to be greater in the clinical isolate (30.8%) compared to environmental isolates (4%). Both clinical and environmental isolates utilized hemoglobin, hemin, transferrin and lactoferrin as iron sources. All data put together indicates that S. maltophilia utilizes siderophore-mediated and heme-mediated systems for iron acquisition during iron starvation. These data need to be further confirmed through several knockout studies. MDPI 2018-08-16 /pmc/articles/PMC6222749/ /pubmed/30115820 http://dx.doi.org/10.3390/molecules23082048 Text en © 2018 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 Kalidasan, V. Azman, Adleen Joseph, Narcisse Kumar, Suresh Awang Hamat, Rukman Neela, Vasantha Kumari Putative Iron Acquisition Systems in Stenotrophomonas maltophilia |
title | Putative Iron Acquisition Systems in Stenotrophomonas maltophilia |
title_full | Putative Iron Acquisition Systems in Stenotrophomonas maltophilia |
title_fullStr | Putative Iron Acquisition Systems in Stenotrophomonas maltophilia |
title_full_unstemmed | Putative Iron Acquisition Systems in Stenotrophomonas maltophilia |
title_short | Putative Iron Acquisition Systems in Stenotrophomonas maltophilia |
title_sort | putative iron acquisition systems in stenotrophomonas maltophilia |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6222749/ https://www.ncbi.nlm.nih.gov/pubmed/30115820 http://dx.doi.org/10.3390/molecules23082048 |
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