Exploring metal availability in the natural niche of Streptococcus pneumoniae to discover potential vaccine antigens
Nasopharyngeal colonization by Streptococcus pneumoniae is a prerequisite for pneumococcal transmission and disease. Current vaccines protect only against disease and colonization caused by a limited number of serotypes, consequently allowing serotype replacement and transmission. Therefore, the dev...
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Taylor & Francis Group
2020
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oai:doaj.org-article:3e016418b8e44a38bee691ecfa6505c32021-11-17T14:21:59ZExploring metal availability in the natural niche of Streptococcus pneumoniae to discover potential vaccine antigens2150-55942150-560810.1080/21505594.2020.1825908https://doaj.org/article/3e016418b8e44a38bee691ecfa6505c32020-12-01T00:00:00Zhttp://dx.doi.org/10.1080/21505594.2020.1825908https://doaj.org/toc/2150-5594https://doaj.org/toc/2150-5608Nasopharyngeal colonization by Streptococcus pneumoniae is a prerequisite for pneumococcal transmission and disease. Current vaccines protect only against disease and colonization caused by a limited number of serotypes, consequently allowing serotype replacement and transmission. Therefore, the development of a broadly protective vaccine against colonization, transmission and disease is desired but requires a better understanding of pneumococcal adaptation to its natural niche. Hence, we measured the levels of free and protein-bound transition metals in human nasal fluid, to determine the effect of metal concentrations on the growth and proteome of S. pneumoniae. Pneumococci cultured in medium containing metal levels comparable to nasal fluid showed a highly distinct proteomic profile compared to standard culture conditions, including the increased abundance of nine conserved, putative surface-exposed proteins. AliA, an oligopeptide binding protein, was identified as the strongest protective antigen, demonstrated by the significantly reduced bacterial load in a murine colonization and a lethal mouse pneumonia model, highlighting its potential as vaccine antigen.Lucille F. van BeekKristin SurmannH. Bart van den Berg van SaparoeaDiane HoubenWouter S. P. JongChristian HentschkerThomas H. A. EderveenElena MitsiDaniela M. FerreiraFred van OpzeelandChrista E. van der Gaast – de JonghIrma JoostenUwe VölkerFrank SchmidtJoen LuirinkDimitri A. DiavatopoulosMarien I. de JongeTaylor & Francis Grouparticlestreptococcus pneumoniaetransition metalsnasal fluidprotein antigenscolonizationin vivo-mimickingInfectious and parasitic diseasesRC109-216ENVirulence, Vol 11, Iss 1, Pp 1310-1328 (2020) |
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streptococcus pneumoniae transition metals nasal fluid protein antigens colonization in vivo-mimicking Infectious and parasitic diseases RC109-216 |
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streptococcus pneumoniae transition metals nasal fluid protein antigens colonization in vivo-mimicking Infectious and parasitic diseases RC109-216 Lucille F. van Beek Kristin Surmann H. Bart van den Berg van Saparoea Diane Houben Wouter S. P. Jong Christian Hentschker Thomas H. A. Ederveen Elena Mitsi Daniela M. Ferreira Fred van Opzeeland Christa E. van der Gaast – de Jongh Irma Joosten Uwe Völker Frank Schmidt Joen Luirink Dimitri A. Diavatopoulos Marien I. de Jonge Exploring metal availability in the natural niche of Streptococcus pneumoniae to discover potential vaccine antigens |
description |
Nasopharyngeal colonization by Streptococcus pneumoniae is a prerequisite for pneumococcal transmission and disease. Current vaccines protect only against disease and colonization caused by a limited number of serotypes, consequently allowing serotype replacement and transmission. Therefore, the development of a broadly protective vaccine against colonization, transmission and disease is desired but requires a better understanding of pneumococcal adaptation to its natural niche. Hence, we measured the levels of free and protein-bound transition metals in human nasal fluid, to determine the effect of metal concentrations on the growth and proteome of S. pneumoniae. Pneumococci cultured in medium containing metal levels comparable to nasal fluid showed a highly distinct proteomic profile compared to standard culture conditions, including the increased abundance of nine conserved, putative surface-exposed proteins. AliA, an oligopeptide binding protein, was identified as the strongest protective antigen, demonstrated by the significantly reduced bacterial load in a murine colonization and a lethal mouse pneumonia model, highlighting its potential as vaccine antigen. |
format |
article |
author |
Lucille F. van Beek Kristin Surmann H. Bart van den Berg van Saparoea Diane Houben Wouter S. P. Jong Christian Hentschker Thomas H. A. Ederveen Elena Mitsi Daniela M. Ferreira Fred van Opzeeland Christa E. van der Gaast – de Jongh Irma Joosten Uwe Völker Frank Schmidt Joen Luirink Dimitri A. Diavatopoulos Marien I. de Jonge |
author_facet |
Lucille F. van Beek Kristin Surmann H. Bart van den Berg van Saparoea Diane Houben Wouter S. P. Jong Christian Hentschker Thomas H. A. Ederveen Elena Mitsi Daniela M. Ferreira Fred van Opzeeland Christa E. van der Gaast – de Jongh Irma Joosten Uwe Völker Frank Schmidt Joen Luirink Dimitri A. Diavatopoulos Marien I. de Jonge |
author_sort |
Lucille F. van Beek |
title |
Exploring metal availability in the natural niche of Streptococcus pneumoniae to discover potential vaccine antigens |
title_short |
Exploring metal availability in the natural niche of Streptococcus pneumoniae to discover potential vaccine antigens |
title_full |
Exploring metal availability in the natural niche of Streptococcus pneumoniae to discover potential vaccine antigens |
title_fullStr |
Exploring metal availability in the natural niche of Streptococcus pneumoniae to discover potential vaccine antigens |
title_full_unstemmed |
Exploring metal availability in the natural niche of Streptococcus pneumoniae to discover potential vaccine antigens |
title_sort |
exploring metal availability in the natural niche of streptococcus pneumoniae to discover potential vaccine antigens |
publisher |
Taylor & Francis Group |
publishDate |
2020 |
url |
https://doaj.org/article/3e016418b8e44a38bee691ecfa6505c3 |
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