| pubmed-article:17060465 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17060465 | lifeskim:mentions | umls-concept:C0016676 | lld:lifeskim |
| pubmed-article:17060465 | lifeskim:mentions | umls-concept:C0042765 | lld:lifeskim |
| pubmed-article:17060465 | lifeskim:mentions | umls-concept:C0001109 | lld:lifeskim |
| pubmed-article:17060465 | lifeskim:mentions | umls-concept:C0001721 | lld:lifeskim |
| pubmed-article:17060465 | lifeskim:mentions | umls-concept:C0038952 | lld:lifeskim |
| pubmed-article:17060465 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:17060465 | pubmed:dateCreated | 2006-12-21 | lld:pubmed |
| pubmed-article:17060465 | pubmed:abstractText | AcpA of Francisella spp. is a respiratory-burst-inhibiting acid phosphatase that also exhibits phospholipase C activity. To better understand the molecular basis of AcpA in virulence, a deletion of acpA was constructed in Francisella novicida. The phosphatase and lipase activities were reduced 10-fold and 8-fold, respectively, in the acpA mutant compared to the wild type and were found mostly associated with the outer membrane. The acpA mutant was more susceptible to intracellular killing than the wild-type strain in the THP-1 human macrophage-like cell line. In addition, mice infected with the acpA mutant survived longer than the wild-type strain and were less fit than the wild-type strain in competition infection assays. Transmission electron microscopy showed that the acpA mutant was delayed in escape from macrophage phagosomes, as more than 75% of acpA mutant bacteria could still be found inside phagosomes after 12 h of infection in THP-1 cells and human monocyte-derived macrophages, whereas most of the wild-type bacteria had escaped from the phagosome by 6 h postinfection. Thus, AcpA affects intracellular trafficking and the fate of Francisella within host macrophages. | lld:pubmed |
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| pubmed-article:17060465 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17060465 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17060465 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17060465 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17060465 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:17060465 | pubmed:issn | 0019-9567 | lld:pubmed |
| pubmed-article:17060465 | pubmed:author | pubmed-author:SchlesingerLa... | lld:pubmed |
| pubmed-article:17060465 | pubmed:author | pubmed-author:GunnJohn SJS | lld:pubmed |
| pubmed-article:17060465 | pubmed:author | pubmed-author:BalagopalAshw... | lld:pubmed |
| pubmed-article:17060465 | pubmed:author | pubmed-author:MohapatraNrus... | lld:pubmed |
| pubmed-article:17060465 | pubmed:author | pubmed-author:SoniShilpaS | lld:pubmed |
| pubmed-article:17060465 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17060465 | pubmed:volume | 75 | lld:pubmed |
| pubmed-article:17060465 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17060465 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17060465 | pubmed:pagination | 390-6 | lld:pubmed |
| pubmed-article:17060465 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:17060465 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17060465 | pubmed:articleTitle | AcpA is a Francisella acid phosphatase that affects intramacrophage survival and virulence. | lld:pubmed |
| pubmed-article:17060465 | pubmed:affiliation | Center for Microbial Interface Biology, Department of Molecular Virology, Immunology, and Medical Genetics, and Department of Internal Medicine, Division of Infectious Diseases, The Ohio State University, Columbus, Ohio 43210, USA. | lld:pubmed |
| pubmed-article:17060465 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17060465 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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