Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/74064
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Type: Journal article
Title: Polyhistidine triad proteins of pathogenic streptococci
Author: Plumptre, C.
Ogunniyi, A.
Paton, J.
Citation: Trends in Microbiology, 2012; 20(10):485-493
Publisher: Elsevier Science London
Issue Date: 2012
ISSN: 0966-842X
1878-4380
Statement of
Responsibility: 
Charles D. Plumptre, Abiodun D. Ogunniyi and James C. Paton
Abstract: The polyhistidine triad (Pht) proteins are an intriguing family of proteins found on the surface of members of the genus Streptococcus. Their defining feature is the presence of multiple copies of the eponymous His triad motif HxxHxH. This review focuses on the Pht proteins of Streptococcus pneumoniae, which contribute to virulence and are leading candidates for inclusion in protein-based pneumococcal vaccines. They appear to have multiple functions, including metal ion homeostasis, evasion of complement deposition and adherence of bacteria to host cells. Across the streptococci, there are many Pht homologs, which can be grouped according to structural features. Critically, there is considerable potential to use members of the Pht protein family as components of vaccines targeted at other streptococci.
Keywords: Animals; Humans; Streptococcus pneumoniae; Histidine; Adhesins, Bacterial; Membrane Transport Proteins; Membrane Proteins; Virulence Factors; Bacterial Vaccines; Phylogeny; Sequence Homology; Models, Molecular
Rights: © 2012 Elsevier Ltd. All rights reserved.
RMID: 0020122163
DOI: 10.1016/j.tim.2012.06.004
Appears in Collections:Molecular and Biomedical Science publications

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