ArticleJournal of bacteriology2002
Characterization of PauB, a novel broad-spectrum plasminogen activator from Streptococcus uberis.
Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 28 citations in OpenAlex.
- Hydrophobic residues in the D-domain of a plasminogen-binding M-protein modulate α-helicity, oligomerization, and surface anchoring in Streptococcus pyogenes.Protein science : a publication of the Protein Society · 2025Article
- Sequence characterisation and novel insights into bovine mastitis-associated Streptococcus uberis in dairy herds.Scientific reports · 2021Article
- Variations in the secondary structures of PAM proteins influence their binding affinities to human plasminogen.Journal of structural biology · 2019Article
- Contributions of different modules of the plasminogen-binding Streptococcus pyogenes M-protein that mediate its functional dimerization.Journal of structural biology · 2018Article
- Fibrin-targeted plasminogen activation by plasminogen activator, PadA, from Streptococcus dysgalactiae.Protein science : a publication of the Protein Society · 2014Article
- Characterization of streptokinases from group A Streptococci reveals a strong functional relationship that supports the coinheritance of plasminogen-binding M protein and cluster 2b streptokinase.The Journal of biological chemistry · 2012Article
- Vru (Sub0144) controls expression of proven and putative virulence determinants and alters the ability of Streptococcus uberis to cause disease in dairy cattle.Microbiology (Reading, England) · 2012Article
- Skizzle is a novel plasminogen- and plasmin-binding protein from Streptococcus agalactiae that targets proteins of human fibrinolysis to promote plasmin generation.The Journal of biological chemistry · 2010Article
- Evidence for niche adaptation in the genome of the bovine pathogen Streptococcus uberis.BMC genomics · 2009Article
- Global transcriptional profiling reveals Streptococcus agalactiae genes controlled by the MtaR transcription factor.BMC genomics · 2008Article
- First insights into the evolution of Streptococcus uberis: a multilocus sequence typing scheme that enables investigation of its population biology.Applied and environmental microbiology · 2006Article
- The activation of bovine plasminogen by PauA is not required for virulence of Streptococcus uberis.Infection and immunity · 2003Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A bovine plasminogen activator of atypical molecular mass ( approximately 45 kDa) from Streptococcus uberis strain SK880 had been identified previously (L. B. Johnsen, K. Poulsen, M. Kilian, and T. E. Petersen. Infect. Immun. 67:1072-1078, 1999). The strain was isolated from a clinical case of bovine mastitis. The isolate was found not to secrete PauA, a bovine plasminogen activator expressed by the majority of S. uberis strains. Analysis of the locus normally occupied by pauA revealed an absence of the pauA open reading frame. However, an alternative open reading frame was identified within the same locus. Sequence analysis of the putative gene suggested limited but significant homology to other plasminogen activators. A candidate signal peptide sequence and cleavage site were also identified. Expression cloning of DNA encoding the predicted mature protein (lacking signal peptide) confirmed that the open reading frame encoded a plasminogen activator of the expected size, which we have named PauB. Both native and recombinant forms of PauB displayed an unexpectedly broad specificity profile for bovine, ovine, equine, caprine, porcine, rabbit, and human plasminogen. Clinical and nonclinical field isolates from nine United Kingdom sites were screened for the pauB gene and none were identified as carrying it. Similarly, clinical isolates from 20 Danish herds were all found to encode PauA and not PauB. Therefore, PauB represents a novel but rare bacterial plasminogen activator which displays very broad specificity.
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