ArticleJournal of bacteriology2009
The single substitution I259T, conserved in the plasminogen activator Pla of pandemic Yersinia pestis branches, enhances fibrinolytic activity.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 30 citations in OpenAlex.
- Emergence, global dispersal, and local adaptations ofApplied and environmental microbiology · 2026Review
- Retracing the path of evolution: polymorphisms ofEmerging microbes & infections · 2025Article
- Unveiling the dance of evolution: Pla-mediated cleavage of Ymt modulates the virulence dynamics ofmBio · 2024Article
- Review
- Phylogenetically Defined Isoforms ofInternational journal of molecular sciences · 2019Article
- New Promising Targets for Synthetic Omptin-Based Peptide Vaccine against Gram-Negative Pathogens.Vaccines · 2019Article
- Humoral and cellular immune responses to Yersinia pestis Pla antigen in humans immunized with live plague vaccine.PLoS neglected tropical diseases · 2018Article
- Proteolysis of plasminogen activator inhibitor-1 by Yersinia pestis remodulates the host environment to promote virulence.Journal of thrombosis and haemostasis : JTH · 2016Article
- Ecological Opportunity, Evolution, and the Emergence of Flea-Borne Plague.Infection and immunity · 2016Review
- Yersinia virulence factors - a sophisticated arsenal for combating host defences.F1000Research · 2016Review
- Article
- Impact of the Pla protease substrate α2-antiplasmin on the progression of primary pneumonic plague.Infection and immunity · 2015Article
- Early emergence of Yersinia pestis as a severe respiratory pathogen.Nature communications · 2015Article
- Coregulation of host-adapted metabolism and virulence by pathogenic yersiniae.Frontiers in cellular and infection microbiology · 2014Review
- Inter- and intra-specific pan-genomes of Borrelia burgdorferi sensu lato: genome stability and adaptive radiation.BMC genomics · 2013Article
- Fibrinolytic and coagulative activities of Yersinia pestis.Frontiers in cellular and infection microbiology · 2013Review
- An additional step in the transmission of Yersinia pestis?The ISME journal · 2012Review
- Cpa, the outer membrane protease of Cronobacter sakazakii, activates plasminogen and mediates resistance to serum bactericidal activity.Infection and immunity · 2011Article
- Molecular adaptation of a plant-bacterium outer membrane protease towards plague virulence factor Pla.BMC evolutionary biology · 2011Article
- The omptins of Yersinia pestis and Salmonella enterica cleave the reactive center loop of plasminogen activator inhibitor 1.Journal of bacteriology · 2010Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The outer membrane plasminogen activator Pla of Yersinia pestis is a central virulence factor in plague. The primary structure of the Pla beta-barrel is conserved in Y. pestis biovars Antiqua, Medievalis, and Orientalis, which are associated with pandemics of plague. The Pla molecule of the ancestral Y. pestis lineages Microtus and Angola carries the single amino acid change T259I located in surface loop 5 of the beta-barrel. Recombinant Y. pestis KIM D34 or Escherichia coli XL1 expressing Pla T259I was impaired in fibrinolysis and in plasminogen activation. Lack of detectable generation of the catalytic light chain of plasmin and inactivation of plasmin enzymatic activity by the Pla T259I construct indicated that Microtus Pla cleaved the plasminogen molecule more unspecifically than did common Pla. The isoform pattern of the Pla T259I molecule was different from that of the common Pla molecule. Microtus Pla was more efficient than wild-type Pla in alpha(2)-antiplasmin inactivation. Pla of Y. pestis and PgtE of Salmonella enterica have evolved from the same omptin ancestor, and their comparison showed that PgtE was poor in plasminogen activation but exhibited efficient antiprotease inactivation. The substitution (259)IIDKT/TIDKN in PgtE, constructed to mimic the L5 region in Pla, altered proteolysis in favor of plasmin formation, whereas the reverse substitution (259)TIDKN/IIDKT in Pla altered proteolysis in favor of alpha(2)-antiplasmin inactivation. The results suggest that Microtus Pla represents an ancestral form of Pla that has evolved into a more efficient plasminogen activator in the pandemic Y. pestis lineages.
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