Virulence factors contributing to invasive activities of Serratia grimesii and Serratia proteamaculans

© 2015, Springer-Verlag Berlin Heidelberg. Previously, we have shown that facultative pathogens Serratia grimesii and Serratia proteamaculans are capable to invade eukaryotic cells provided that they synthesize intracellular metalloprotease grimelysin or protealysin, respectively (Bozhokina et al. in Cell Biol Int 35(2):111–118, 2011). Noninvasive Escherichia coli transformed with grimelysin or protealysin gene became invasive, indicating that the protease is a virulence factor. Here we elucidated involvement of other virulence factors in the invasion of S. grimesii and S. proteamaculans. Under similar experimental conditions, the amount of S. proteamaculans internalized within human carcinoma HeLa cells was fivefold higher than that of S. grimesii. In accord with this, in S. proteamaculans, high activities of pore-forming hemolysin ShlA and extracellular metalloprotease serralysin were detected. In S. grimesii, activity of toxin ShlA was not detected, and the serralysin activity of the bacterial growth medium was very low. We also show that iron depletion strongly enhanced invasive activity of S. proteamaculans, increasing activities of hemolysin ShlA and serralysin, but did not affect S. grimesii properties. These results show that the invasive activity of S. proteamaculans is maintained, along with protealysin, by hemolysin and serralysin. On the other hand, grimelysin is so far the only known invasion factor of S.grimesii

Peculiarities of Proteus mirabilis extracellular metalloproteinase biosynthesis

© 2015, Pleiades Publishing, Inc. Biosynthesis of metalloproteinase by the Proteus mirabilis 5127-1 strain on different media and the influence of glucose and urea on biosynthesis were studied. It was found that the P. mirabilis 5127-1 bacteria secretes metalloproteinase in the medium in two isoforms (52 and 50 kDa). It was established that proteinase synthesis is completely suppressed during the growth of bacteria on synthetic media, as well as in the presence of glucose in the LB medium. It was demonstrated that addition of urea in the medium results in an increase of the culture productivity in the proteinase synthesis. Maximal culture productivity in the proteinase synthesis was found in the medium with natural urine. During the growth of bacteria on artificial urine, proteinase appeared in the medium only after 12 hours of growth as a single isoform

Virulence factors contributing to invasive activities of Serratia grimesii and Serratia proteamaculans

© 2015, Springer-Verlag Berlin Heidelberg. Previously, we have shown that facultative pathogens Serratia grimesii and Serratia proteamaculans are capable to invade eukaryotic cells provided that they synthesize intracellular metalloprotease grimelysin or protealysin, respectively (Bozhokina et al. in Cell Biol Int 35(2):111–118, 2011). Noninvasive Escherichia coli transformed with grimelysin or protealysin gene became invasive, indicating that the protease is a virulence factor. Here we elucidated involvement of other virulence factors in the invasion of S. grimesii and S. proteamaculans. Under similar experimental conditions, the amount of S. proteamaculans internalized within human carcinoma HeLa cells was fivefold higher than that of S. grimesii. In accord with this, in S. proteamaculans, high activities of pore-forming hemolysin ShlA and extracellular metalloprotease serralysin were detected. In S. grimesii, activity of toxin ShlA was not detected, and the serralysin activity of the bacterial growth medium was very low. We also show that iron depletion strongly enhanced invasive activity of S. proteamaculans, increasing activities of hemolysin ShlA and serralysin, but did not affect S. grimesii properties. These results show that the invasive activity of S. proteamaculans is maintained, along with protealysin, by hemolysin and serralysin. On the other hand, grimelysin is so far the only known invasion factor of S.grimesii

Tolerance to a contact allergen in the mouse does not require antibody. Abstr.

© 2015, Springer-Verlag Berlin Heidelberg. Previously, we have shown that facultative pathogens Serratia grimesii and Serratia proteamaculans are capable to invade eukaryotic cells provided that they synthesize intracellular metalloprotease grimelysin or protealysin, respectively (Bozhokina et al. in Cell Biol Int 35(2):111–118, 2011). Noninvasive Escherichia coli transformed with grimelysin or protealysin gene became invasive, indicating that the protease is a virulence factor. Here we elucidated involvement of other virulence factors in the invasion of S. grimesii and S. proteamaculans. Under similar experimental conditions, the amount of S. proteamaculans internalized within human carcinoma HeLa cells was fivefold higher than that of S. grimesii. In accord with this, in S. proteamaculans, high activities of pore-forming hemolysin ShlA and extracellular metalloprotease serralysin were detected. In S. grimesii, activity of toxin ShlA was not detected, and the serralysin activity of the bacterial growth medium was very low. We also show that iron depletion strongly enhanced invasive activity of S. proteamaculans, increasing activities of hemolysin ShlA and serralysin, but did not affect S. grimesii properties. These results show that the invasive activity of S. proteamaculans is maintained, along with protealysin, by hemolysin and serralysin. On the other hand, grimelysin is so far the only known invasion factor of S.grimesii

Peculiarities of Proteus mirabilis extracellular metalloproteinase biosynthesis

© 2015, Pleiades Publishing, Inc. Biosynthesis of metalloproteinase by the Proteus mirabilis 5127-1 strain on different media and the influence of glucose and urea on biosynthesis were studied. It was found that the P. mirabilis 5127-1 bacteria secretes metalloproteinase in the medium in two isoforms (52 and 50 kDa). It was established that proteinase synthesis is completely suppressed during the growth of bacteria on synthetic media, as well as in the presence of glucose in the LB medium. It was demonstrated that addition of urea in the medium results in an increase of the culture productivity in the proteinase synthesis. Maximal culture productivity in the proteinase synthesis was found in the medium with natural urine. During the growth of bacteria on artificial urine, proteinase appeared in the medium only after 12 hours of growth as a single isoform

Peculiarities of Proteus mirabilis extracellular metalloproteinase biosynthesis

© 2015, Pleiades Publishing, Inc. Biosynthesis of metalloproteinase by the Proteus mirabilis 5127-1 strain on different media and the influence of glucose and urea on biosynthesis were studied. It was found that the P. mirabilis 5127-1 bacteria secretes metalloproteinase in the medium in two isoforms (52 and 50 kDa). It was established that proteinase synthesis is completely suppressed during the growth of bacteria on synthetic media, as well as in the presence of glucose in the LB medium. It was demonstrated that addition of urea in the medium results in an increase of the culture productivity in the proteinase synthesis. Maximal culture productivity in the proteinase synthesis was found in the medium with natural urine. During the growth of bacteria on artificial urine, proteinase appeared in the medium only after 12 hours of growth as a single isoform

Peculiarities of Proteus mirabilis extracellular metalloproteinase biosynthesis

© 2015, Pleiades Publishing, Inc. Biosynthesis of metalloproteinase by the Proteus mirabilis 5127-1 strain on different media and the influence of glucose and urea on biosynthesis were studied. It was found that the P. mirabilis 5127-1 bacteria secretes metalloproteinase in the medium in two isoforms (52 and 50 kDa). It was established that proteinase synthesis is completely suppressed during the growth of bacteria on synthetic media, as well as in the presence of glucose in the LB medium. It was demonstrated that addition of urea in the medium results in an increase of the culture productivity in the proteinase synthesis. Maximal culture productivity in the proteinase synthesis was found in the medium with natural urine. During the growth of bacteria on artificial urine, proteinase appeared in the medium only after 12 hours of growth as a single isoform