ArticleInfection and immunity2010
Temperature-induced changes in the lipopolysaccharide of Yersinia pestis affect plasminogen activation by the pla surface protease.
Article in Infection and immunity, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 40 citations in OpenAlex.
- Progress on the research and development of plague vaccines with a call to action.NPJ vaccines · 2024Review
- A protein O-GlcNAc glycosyltransferase regulates the antioxidative response in Yersinia pestis.Nature communications · 2024Article
- Unveiling the dance of evolution: Pla-mediated cleavage of Ymt modulates the virulence dynamics ofmBio · 2024Article
- Plague Outbreak of aVector borne and zoonotic diseases (Larchmont, N.Y.) · 2022Article
- Different expression patterns of inflammatory cytokines induced by lipopolysaccharides from Escherichia coli or Porphyromonas gingivalis in human dental pulp stem cells.BMC oral health · 2022Article
- Lipopolysaccharide of theBiomolecules · 2021Review
- Review
- A Dual Role for the Plasminogen Activator Protease During the Preinflammatory Phase of Primary Pneumonic Plague.The Journal of infectious diseases · 2020Article
- Lipopolysaccharides fromToxins · 2019Article
- New Promising Targets for Synthetic Omptin-Based Peptide Vaccine against Gram-Negative Pathogens.Vaccines · 2019Article
- Adhesive properties of YapV and paralogous autotransporter proteins of Yersinia pestis.Infection and immunity · 2015Article
- Combinational deletion of three membrane protein-encoding genes highly attenuates yersinia pestis while retaining immunogenicity in a mouse model of pneumonic plague.Infection and immunity · 2015Article
- The outer membrane protease PgtE of Salmonella enterica interferes with the alternative complement pathway by cleaving factors B and H.Frontiers in microbiology · 2015Article
- Temperature-dependence of yadBC phenotypes in Yersinia pestis.Microbiology (Reading, England) · 2014Article
- Fortifying the barrier: the impact of lipid A remodelling on bacterial pathogenesis.Nature reviews. Microbiology · 2013Review
- Pathogenicity of Yersinia pestis synthesis of 1-dephosphorylated lipid A.Infection and immunity · 2013Article
- Fibrinolytic and coagulative activities of Yersinia pestis.Frontiers in cellular and infection microbiology · 2013Review
- Lipopolysaccharide of Yersinia pestis, the Cause of Plague: Structure, Genetics, Biological Properties.Acta naturae · 2012Article
- 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
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Pla surface protease of Yersinia pestis activates human plasminogen and is a central virulence factor in bubonic and pneumonic plague. Pla is a transmembrane beta-barrel protein and member of the omptin family of outer membrane proteases which require bound lipopolysaccharide (LPS) to be proteolytically active. Plasminogen activation and autoprocessing of Pla were dramatically higher in Y. pestis cells grown at 37 degrees C than in cells grown at 20 degrees C; the difference in enzymatic activity by far exceeded the increase in the cellular content of the Pla protein. Y. pestis modifies its LPS structure in response to growth temperature. We purified His(6)-Pla under denaturing conditions and compared various LPS types for their capacity to enhance plasmin formation by His(6)-Pla solubilized in detergent. Reactivation of His(6)-Pla was higher with Y. pestis LPSs isolated from bacteria grown at 37 degrees C than with LPSs from cells grown at 25 degrees C. Lack of O antigens and the presence of the outer core region as well as a lowered level of acylation in LPS were found to enhance the Pla-LPS interaction. Genetic substitution of arginine 138, which is part of a three-dimensional protein motif for binding to lipid A phosphates, decreased both the enzymatic activity of His(6)-Pla and the amount of Pla in Y. pestis cells, suggesting the importance of the Pla-lipid A phosphate interaction. The temperature-induced changes in LPS are known to help Y. pestis to avoid innate immune responses, and our results strongly suggest that they also potentiate Pla-mediated proteolysis.
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