Document Detail


In vitro secretion kinetics of proteins from Legionella pneumophila in comparison to proteins from non-pneumophila species.
MedLine Citation:
PMID:  11700363     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
It has been shown that the loss of PilD, a prepilin peptidase necessary for type IV pilus biogenesis and establishment of the type II secretion apparatus is associated with loss of virulence in Legionella pneumophila. L. pneumophila is the species most frequently associated with Legionnaires' disease, but virulence factors unique to this species are not known, so the secretion kinetics of several pilD-dependent enzyme activities, including protease, acid phosphatase, phospholipase A (PLA) and lysophospholipase A (LPLA), of L. pneumophila and non-pneumophila species were compared during growth in BYE broth. Enzyme activity appeared during mid-exponential growth phase and reached maximal levels on entry into stationary growth phase. None of the enzyme activities were unique to L. pneumophila and it did not exclusively secrete the highest amounts of the hydrolytic proteins. However, the timing of PLA and LPLA secretion in L. pneumophila differed compared to other species. PLA activity was secreted prior to LPLA activity in L. pneumophila, which may lead to an accumulation of the cytotoxic agent lysophosphatidylcholine (LPC). In addition to L. pneumophila, several other Legionella species, including Legionella steigerwaltii and Legionella gormanii, were able to enrich for LPC due to a very potent PLA activity accompanied by only moderate LPLA activity. These species, in contrast to L. pneumophila, have not been shown to multiply within monocytic host cells. Thus none of the secreted enzymic activities investigated were unique to L. pneumophila, nor were they secreted at high concentrations. However, the timing of PLA and LPLA secretion may contribute to pathogenicity.
Authors:
A Flieger; S Gong; M Faigle; H Northoff; B Neumeister
Related Documents :
12384513 - Maspin inhibits cell migration in the absence of protease inhibitory activity.
21327653 - Analysis of mitogen-activated protein kinase activation.
19480563 - Pras40: target or modulator of mtorc1 signalling and insulin action?
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Microbiology (Reading, England)     Volume:  147     ISSN:  1350-0872     ISO Abbreviation:  Microbiology (Reading, Engl.)     Publication Date:  2001 Nov 
Date Detail:
Created Date:  2001-11-08     Completed Date:  2002-01-10     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9430468     Medline TA:  Microbiology     Country:  England    
Other Details:
Languages:  eng     Pagination:  3127-34     Citation Subset:  IM    
Affiliation:
Abteilung für Transfusionsmedizin, Universitätsklinikum Tübingen, Otfried-Müller-Str. 4/1, D-72076 Tübingen, Germany.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Acid Phosphatase / secretion
Bacterial Proteins / metabolism,  secretion*
Endopeptidases / secretion
Enzymes / secretion*
Epithelial Cells / microbiology
Genes, Bacterial
Kinetics
Legionella pneumophila / enzymology,  metabolism*,  pathogenicity
Lysophospholipase / secretion
Phospholipases A / secretion
Species Specificity
Virulence
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Enzymes; EC 3.1.1.-/Phospholipases A; EC 3.1.1.5/Lysophospholipase; EC 3.1.3.2/Acid Phosphatase; EC 3.4.-/Endopeptidases; EC 3.4.-/prepilin peptidase protein, Bacteria

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Role of biofilms in the survival of Legionella pneumophila in a model potable-water system.
Next Document:  Substrate-specific diffusion of select dicarboxylates through Chlamydia trachomatis PorB.