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AuthorNasrallah, Gheyath K.
AuthorAbdelhady, Hany
AuthorTompkins, Nicholas P.
AuthorCarson, Kaitlyn R.
AuthorGarduno, Rafael A.
Available date2016-09-21T08:12:10Z
Publication Date2014-07
Publication NameInternational Journal of Medical Microbiology
ResourceScopus
Identifierhttp://dx.doi.org/10.1016/j.ijmm.2014.05.004
CitationNasrallah, G.K., Abdelhady, H., Tompkins, N.P., Carson, K.R., Garduno, R.A. "Deletion of potD, encoding a putative spermidine-binding protein, results in a complex phenotype in Legionella pneumophila" (2014) International Journal of Medical Microbiology, 304 (5-6), pp. 703-716.
ISSN1438-4221
URIhttp://hdl.handle.net/10576/4726
AbstractL. pneumophila is an intracellular pathogen that replicates in a membrane-bound compartment known as the Legionella-containing vacuole (LCV). We previously observed that the polyamine spermidine, produced by host cells or added exogenously, enhances the intracellular growth of L. pneumophila. To study this enhancing effect and determine whether polyamines are used as nutrients, we deleted potD from L. pneumophila strain JR32. The gene potD encodes a spermidine-binding protein that in other bacteria is essential for the function of the PotABCD polyamine transporter. Deletion of potD did not affect L. pneumophila growth in vitro in the presence or absence of spermidine and putrescine, suggesting that PotD plays a redundant or no role in polyamine uptake. However, deletion of potD resulted in a puzzlingly complex phenotype that included defects in L. pneumophila's ability to form filaments, tolerate Na+, associate with macrophages and amoeba, recruit host vesicles to the LCV, and initiate intracellular growth. Moreover, the ?potD mutant was completely unable to grow in L929 cells treated with a pharmacological inhibitor of spermidine synthesis. These complex and disparate effects suggest that the L. pneumophila potD encodes either: (i) a multifunctional protein, (ii) a protein that interacts with, or regulates a, multifunctional protein, or (iii) a protein that contributes (directly or indirectly) to a regulatory network. Protein function studies with the L. pneumophila PotD protein are thus warranted.
SponsorDiscovery Grant to RAG from the Natural Sciences and Engineering Research Council (NSERC) of Canada and a start-up Grant to GKN from Qatar University.
Languageen
PublisherElsevier GmbH
SubjectLegionella
Pathogenesis
Polyamines
PotD
Spermidine-binding protein
TitleDeletion of potD, encoding a putative spermidine-binding protein, results in a complex phenotype in Legionella pneumophila
TypeArticle
Pagination703-716
Issue Number5--6
Volume Number304
dc.accessType Abstract Only


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