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Projekt Druckansicht

Identification and evaluation of peptides for active and passive immunization against Pseudomonas aeruginosa

Fachliche Zuordnung Parasitologie und Biologie der Erreger tropischer Infektionskrankheiten
Förderung Förderung von 2012 bis 2017
Projektkennung Deutsche Forschungsgemeinschaft (DFG) - Projektnummer 217957200
 
Erstellungsjahr 2017

Zusammenfassung der Projektergebnisse

Pseudomonas aeruginosa is a major nosocomial pathogen which can cause severe infections in immunocompromised patients including blood stream infections that are associated with a high mortality. Cystic fibrosis patients chronically colonized by P. aeruginosa suffer from a significant decline in pulmonary function. In light of the intrinsic and acquired antibiotic resistance of P. aeruginosa and its ubiquitous presence efforts directed at preventing an infection have been made. However, to date, no vaccine is available. In this study we sought to identify and characterize appropriate vaccine proteins utilizing reverse vaccinology and to construct composite recombinant antigens to enhance immunogenicity. Several candidate constructs with multiple epitopes displayed in surface-exposed loops of the beta-barrel protein OmpX were generated for production of antisera in rabbits and opsonization assays.

Projektbezogene Publikationen (Auswahl)

  • 2015. Strategies for the analysis of short protein motifs on the example of the Bam recognition motif in outer membrane proteins. In: S. Buchanan, N. Noinaj, editors, The BAM Complex - Methods and Protocols. Methods in Molecular Biology 1329: 271-277
    Paramasivam, N, Linke D
    (Siehe online unter https://doi.org/10.1007/978-1-4939-2871-2_21)
  • 2016. “Reverse vaccinology”: the pathway from genomes and epitope predictions to tailored, recombinant vaccines. Methods in Molecular Biology 1403: 87-106
    Michalik, M, Djahanshiri B, Leo J, Linke D
    (Siehe online unter https://doi.org/10.1007/978-1-4939-3387-7_4)
  • An evolutionarily conserved glycine-tyrosine motif forms a folding core in outer membrane proteins. eLIFE, submitted
    Michalik M, Orwick-Rydmark M, Arnold T, Linke D
    (Siehe online unter https://doi.org/10.1371/journal.pone.0182016)
 
 

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