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Microbiology 153 (2007), 3757-3765; DOI  10.1099/mic.0.2007/010116-0
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Microbiology 153 (2007), 3757-3765; DOI  10.1099/mic.0.2007/010116-0
© 2007 Society for General Microbiology

Legionella pneumophila exhibits plasminogen activator activity

Leen Vranckx, Emmy De Buck, Jozef Anné and Elke Lammertyn

Laboratory for Bacteriology, Rega Institute for Medical Research, Katholieke Universiteit Leuven, Minderbroedersstraat 10, B-3000 Leuven, Belgium

Correspondence
Jozef Anné
Jozef.Anne{at}rega.kuleuven.be

Based on their localization at the boundary of the bacterial cell and its environment, outer-membrane proteins (Omps) are important determinants for interaction of bacteria with their host cell. Therefore, they can be considered as important determinants for virulence. Looking for Legionella pneumophila Omps potentially involved in virulence, we identified a gene encoding a homologue of the plasminogen activator (Pla) of Yersinia pestis. Pla belongs to the class of omptins, a family of surface proteases/adhesins that exhibit different virulence-associated functions. In this report we describe the cloning and identification of the plasminogen activator homologue Lpa of L. pneumophila and demonstrate its outer-membrane localization. Transcriptional analysis of the Lpa region revealed expression of the gene in both exponential and stationary growth phase and showed that transcription of the lpa gene is directed by its own promoter. We also show, to our knowledge for the first time, that L. pneumophila has the capacity to convert plasminogen into plasmin by the action of the outer-membrane Lpa protein.

Abbreviations: {alpha}2AP, {alpha}2-antiplasmin; Lpa, Legionella plasminogen activator; MOMP, major outer-membrane protein; Omps, outer-membrane proteins; Pla, plasminogen activator; Plg, plasminogen






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Copyright © 2007 Society for General Microbiology.