Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2009-5-6
pubmed:databankReference
pubmed:abstractText
Hfq is a highly conserved pleiotropically acting prokaryotic RNA-binding protein involved in the post-transcriptional regulation of many stress-responsive genes by small RNAs. In this study, we show that Hfq of the strictly human pathogen Neisseria meningitidis is involved in the regulation of expression of components involved in general metabolic pathways, iron metabolism and virulence. A meningococcal hfq deletion strain (H44/76Deltahfq) is impaired in growth in nutrient-rich media and does not grow at all in nutrient-limiting medium. The growth defect was complemented by expression of hfq in trans. Using proteomics, the expression of 28 proteins was found to be significantly affected upon deletion of hfq. Of these, 20 proteins are involved in general metabolism, among them seven iron-responsive genes. Two proteins (PilE, TspA) are involved in adherence to human cells, a step crucial for the onset of disease. One of the differentially expressed proteins, GdhA, was identified as an essential virulence factor for establishment of sepsis in an animal model, studied earlier. These results show that in N. meningitidis Hfq is involved in the regulation of a variety of components contributing to the survival and establishment of meningococcal disease.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-10338501, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-10710307, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-10761919, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-11062540, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-12093755, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-14521880, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-14739933, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-15009882, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-15009900, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-15130126, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-15150220, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-15629922, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-15784566, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-16113288, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-16965515, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-17007876, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-17133369, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-17163975, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-17305430, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-17351036, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-17395525, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-18031983, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-18362134, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-18458066, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-18586945, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-18832319, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-18927406, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-19060140, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-2822666, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-7619468, http://linkedlifedata.com/resource/pubmed/commentcorrection/19374669-8675023
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1574-6968
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
294
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
216-24
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Molecular characterization and identification of proteins regulated by Hfq in Neisseria meningitidis.
pubmed:publicationType
Letter, Research Support, Non-U.S. Gov't