dc.contributor.author | Norville, IH | |
dc.contributor.author | Harmer, Nicholas | |
dc.contributor.author | Harding, SV | |
dc.contributor.author | Fischer, Gunter | |
dc.contributor.author | Keith, KE | |
dc.contributor.author | Brown, Katherine A. | |
dc.contributor.author | Sarkar-Tyson, M | |
dc.contributor.author | Titball, Richard W. | |
dc.date.accessioned | 2013-05-30T13:05:11Z | |
dc.date.issued | 2011-11 | |
dc.description.abstract | Macrophage infectivity potentiators (Mips) are a group of virulence factors encoded by pathogenic bacteria such as Legionella, Chlamydia, and Neisseria species. Mips are part of the FK506-binding protein (FKBP) family, whose members typically exhibit peptidylprolyl cis-trans isomerase (PPIase) activity which is inhibitable by the immunosuppressants FK506 and rapamycin. Here we describe the identification and characterization of BPSS1823, a Mip-like protein in the intracellular pathogen Burkholderia pseudomallei. Recombinant BPSS1823 protein has rapamycin-inhibitable PPIase activity, indicating that it is a functional FKBP. A mutant strain generated by deletion of BPSS1823 in B. pseudomallei exhibited a reduced ability to survive within cells and significant attenuation in vivo, suggesting that BPSS1823 is important for B. pseudomallei virulence. In addition, pleiotropic effects were observed with a reduction in virulence mechanisms, including resistance to host killing mechanisms, swarming motility, and protease production. | en_GB |
dc.identifier.citation | Infection and Immunity , 2011, Vol. 79, Issue 11, pp. 4299 - 4307 | en_GB |
dc.identifier.doi | 10.1128/IAI.00134-11 | |
dc.identifier.other | IAI.00134-11 | |
dc.identifier.uri | http://hdl.handle.net/10871/9714 | |
dc.language.iso | en | en_GB |
dc.publisher | American Society for Microbiology | en_GB |
dc.relation.url | http://www.ncbi.nlm.nih.gov/pubmed/21859853 | en_GB |
dc.relation.url | http://iai.asm.org/content/79/11/4299.long | en_GB |
dc.subject | Amino Acid Sequence | en_GB |
dc.subject | Animals | en_GB |
dc.subject | Anti-Bacterial Agents | en_GB |
dc.subject | Bacterial Proteins | en_GB |
dc.subject | Burkholderia pseudomallei | en_GB |
dc.subject | Gene Expression Regulation, Bacterial | en_GB |
dc.subject | Mice | en_GB |
dc.subject | Mice, Inbred BALB C | en_GB |
dc.subject | Models, Molecular | en_GB |
dc.subject | Molecular Sequence Data | en_GB |
dc.subject | Peptidylprolyl Isomerase | en_GB |
dc.subject | Protein Conformation | en_GB |
dc.subject | Recombinant Proteins | en_GB |
dc.subject | Sirolimus | en_GB |
dc.subject | Tacrolimus Binding Proteins | en_GB |
dc.subject | Virulence | en_GB |
dc.title | A Burkholderia pseudomallei macrophage infectivity potentiator-like protein has rapamycin-inhibitable peptidylprolyl isomerase activity and pleiotropic effects on virulence | en_GB |
dc.type | Article | en_GB |
dc.date.available | 2013-05-30T13:05:11Z | |
exeter.place-of-publication | United States | |
dc.description | addresses: Defence Science and Technology Laboratory, Porton Down SP4 0JQ, UK. ihnorville@dstl.gov.uk | en_GB |
dc.description | notes: PMCID: PMC3257933 | en_GB |
dc.description | types: Journal Article; Research Support, Non-U.S. Gov't | en_GB |
dc.description | This is the author's post-print version of an article published in Infection and Immunity , 2011, Vol. 79, Issue 11, pp. 4299 – 4307. Copyright © 2011, American Society for Microbiology | en_GB |
dc.identifier.journal | Infection and Immunity | en_GB |