Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/81859
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Type: Journal article
Title: Vaccination against Streptococcus pneumoniae using truncated derivatives of polyhistidine triad protein D
Author: Plumptre, C.
Ogunniyi, A.
Paton, J.
Citation: PLoS One, 2013; 8(10):1-11
Publisher: Public Library of Science
Issue Date: 2013
ISSN: 1932-6203
1932-6203
Editor: Miyaji, E.N.
Statement of
Responsibility: 
Charles D. Plumptre, Abiodun D. Ogunniyi, James C. Paton
Abstract: Polyhistidine triad protein D (PhtD) has been described as a promising vaccine candidate for use against Streptococcus pneumoniae, but there has been a lack of examination of its structure and of which region(s) of the protein are targeted by protective immune responses. In this study, we purified recombinant truncated derivatives of PhtD and examined their secondary structural composition, as well as their capacity to bind antibodies from polyclonal murine serum generated against the full length protein. This allowed the identification of a particularly immunogenic fragment of PhtD, which was also purified and characterised. The truncated derivatives were tested as vaccine antigens in mouse models of pneumococcal sepsis and colonisation, using alum and E. coli heat labile toxin B subunit respectively as adjuvants. These experiments revealed that whilst the immunogenic region identified may be a promising candidate to protect against sepsis, the full length PhtD was ineffective at conferring significant protective immunity. These results are significant for the potential for PhtD to be used in novel vaccines, which are currently being tested in clinical trials.
Keywords: Animals
Mice
Streptococcus pneumoniae
Pneumonia, Pneumococcal
Sepsis
Histidine
Bacterial Proteins
Pneumococcal Vaccines
Antigens, Bacterial
Vaccination
Circular Dichroism
Binding Sites
Rights: © 2013 Plumptre et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
DOI: 10.1371/journal.pone.0078916
Grant ID: http://purl.org/au-research/grants/arc/DP120101432
Published version: http://dx.doi.org/10.1371/journal.pone.0078916
Appears in Collections:Aurora harvest
Molecular and Biomedical Science publications

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