Exploring metal availability in the natural niche of Streptococcus pneumoniae to discover potential vaccine antigens
العنوان: | Exploring metal availability in the natural niche of Streptococcus pneumoniae to discover potential vaccine antigens |
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المؤلفون: | H. Bart van den Berg van Saparoea, Daniela M. Ferreira, Thomas H. A. Ederveen, Irma Joosten, Joen Luirink, Lucille F. van Beek, Diane Houben, Kristin Surmann, Elena Mitsi, Uwe Völker, Frank Schmidt, Christian Hentschker, Dimitri A. Diavatopoulos, Fred van Opzeeland, Christa E. van der Gaast-de Jongh, Wouter S. P. Jong, Marien I. de Jonge |
المساهمون: | Molecular Microbiology, AIMMS, LaserLaB - Molecular Biophysics |
المصدر: | Virulence, 11, 1310-1328 Virulence article-version (VoR) Version of Record Virulence, 11(1), 1310-1328. Landes Bioscience Virulence, Vol 11, Iss 1, Pp 1310-1328 (2020) van Beek, L F, Surmann, K, van den Berg van Saparoea, H B, Houben, D, Jong, W S P, Hentschker, C, Ederveen, T H A, Mitsi, E, Ferreira, D M, van Opzeeland, F, van der Gaast–de Jongh, C E, Joosten, I, Völker, U, Schmidt, F, Luirink, J, Diavatopoulos, D A & de Jonge, M I 2020, ' Exploring metal availability in the natural niche of Streptococcus pneumoniae to discover potential vaccine antigens ', Virulence, vol. 11, no. 1, pp. 1310-1328 . https://doi.org/10.1080/21505594.2020.1825908 Virulence, 11, 1, pp. 1310-1328 |
سنة النشر: | 2020 |
مصطلحات موضوعية: | Serotype, Male, wc_100, protein antigens, lnfectious Diseases and Global Health Radboud Institute for Molecular Life Sciences [Radboudumc 4], Infectious and parasitic diseases, RC109-216, medicine.disease_cause, Pneumococcal Vaccines, Mice, Nasopharynx, Colonization, 0303 health sciences, Transmission (medicine), nasal fluid, wc_217, Middle Aged, Antibodies, Bacterial, Infectious Diseases, Streptococcus pneumoniae, Metals, Proteome, Female, Pneumonia (non-human), Inflammatory diseases Radboud Institute for Molecular Life Sciences [Radboudumc 5], Research Article, Research Paper, Microbiology (medical), Adult, Immunology, Biology, Microbiology, transition metals, Pneumococcal Infections, qw_805, 03 medical and health sciences, Young Adult, All institutes and research themes of the Radboud University Medical Center, SDG 3 - Good Health and Well-being, medicine, Animals, Humans, Molecular Biology, 030304 developmental biology, Antigens, Bacterial, Proteomic Profile, 030306 microbiology, in vivo-mimicking, Membrane Proteins, medicine.disease, colonization, Nasal Lavage Fluid, Culture Media, Mice, Inbred C57BL, Disease Models, Animal, Parasitology, qw_142, Oligopeptide binding |
الوصف: | 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. |
وصف الملف: | application/pdf; application/vnd.openxmlformats-officedocument.wordprocessingml.document |
تدمد: | 2150-5594 |
URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88f314fe87e70e5de7bf5653f443dda7 http://hdl.handle.net/2066/226220 |
حقوق: | OPEN |
رقم الأكسشن: | edsair.doi.dedup.....88f314fe87e70e5de7bf5653f443dda7 |
قاعدة البيانات: | OpenAIRE |
تدمد: | 21505594 |
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