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dc.contributor.authorItzek, Andreas
dc.contributor.authorGillen, Christine M
dc.contributor.authorFulde, Marcus
dc.contributor.authorFriedrichs, Claudia
dc.contributor.authorRodloff, Arne C
dc.contributor.authorChhatwal, Gursharan S
dc.contributor.authorNitsche-Schmitz, Daniel Patric
dc.date.accessioned2011-05-18T10:49:27Z
dc.date.available2011-05-18T10:49:27Z
dc.date.issued2010
dc.identifier.citationContribution of plasminogen activation towards the pathogenic potential of oral streptococci. 2010, 5 (11):e13826 PLoS ONEen
dc.identifier.issn1932-6203
dc.identifier.pmid21072208
dc.identifier.doi10.1371/journal.pone.0013826
dc.identifier.urihttp://hdl.handle.net/10033/129748
dc.description.abstractOral streptococci are a heterogeneous group of human commensals, with a potential to cause serious infections. Activation of plasminogen has been shown to increase the virulence of typical human pathogenic streptococci such as S. pneumoniae. One important factor for plasminogen activation is the streptococcal α-enolase. Here we report that plasminogen activation is also common in oral streptococci species involved in clinical infection and that it depends on the action of human plasminogen activators. The ability to activate plasminogen did not require full conservation of the internal plasminogen binding sequence motif FYDKERKVY of α-enolase that was previously described as crucial for increased plasminogen binding, activation and virulence. Instead, experiments with recombinant α-enolase variants indicate that the naturally occurring variations do not impair plasminogen binding. In spite of these variations in the internal plasminogen binding motif oral streptococci showed similar activation of plasminogen. We conclude that the pathomechanism of plasminogen activation is conserved in oral streptococci that cause infections in human. This may contribute to their opportunistic pathogenic character that is unfurled in certain niches.
dc.language.isoenen
dc.subject.meshAmino Acid Sequenceen
dc.subject.meshBacterial Proteinsen
dc.subject.meshBinding Sitesen
dc.subject.meshElectrophoresis, Polyacrylamide Gelen
dc.subject.meshFibrinolysinen
dc.subject.meshHumansen
dc.subject.meshImmunoblottingen
dc.subject.meshMolecular Sequence Dataen
dc.subject.meshMouthen
dc.subject.meshMutationen
dc.subject.meshPhosphopyruvate Hydrataseen
dc.subject.meshPlasminogenen
dc.subject.meshPlasminogen Activatorsen
dc.subject.meshProtein Bindingen
dc.subject.meshSequence Homology, Amino Aciden
dc.subject.meshSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionizationen
dc.subject.meshStreptococcal Infectionsen
dc.subject.meshStreptococcusen
dc.subject.meshStreptococcus oralisen
dc.subject.meshVirulenceen
dc.titleContribution of plasminogen activation towards the pathogenic potential of oral streptococci.en
dc.typeArticleen
dc.contributor.departmentDepartment of Medical Microbiology, Helmholtz Centre for Infection Research, Braunschweig, Germany.en
dc.identifier.journalPloS oneen
refterms.dateFOA2018-06-13T17:10:59Z
html.description.abstractOral streptococci are a heterogeneous group of human commensals, with a potential to cause serious infections. Activation of plasminogen has been shown to increase the virulence of typical human pathogenic streptococci such as S. pneumoniae. One important factor for plasminogen activation is the streptococcal α-enolase. Here we report that plasminogen activation is also common in oral streptococci species involved in clinical infection and that it depends on the action of human plasminogen activators. The ability to activate plasminogen did not require full conservation of the internal plasminogen binding sequence motif FYDKERKVY of α-enolase that was previously described as crucial for increased plasminogen binding, activation and virulence. Instead, experiments with recombinant α-enolase variants indicate that the naturally occurring variations do not impair plasminogen binding. In spite of these variations in the internal plasminogen binding motif oral streptococci showed similar activation of plasminogen. We conclude that the pathomechanism of plasminogen activation is conserved in oral streptococci that cause infections in human. This may contribute to their opportunistic pathogenic character that is unfurled in certain niches.


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