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Analysis of a cloned sequence of Legionella pneumophila encoding a 38 kD metalloprotease possessing haemolytic and cytotoxic activities
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| Zeitschriftentitel: | Molecular Microbiology |
|---|---|
| Personen und Körperschaften: | , |
| In: | Molecular Microbiology, 3, 1989, 6, S. 797-805 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
Quinn, F. D. Tompkins, L. S. Quinn, F. D. Tompkins, L. S. |
|---|---|
| author |
Quinn, F. D. Tompkins, L. S. |
| spellingShingle |
Quinn, F. D. Tompkins, L. S. Molecular Microbiology Analysis of a cloned sequence of Legionella pneumophila encoding a 38 kD metalloprotease possessing haemolytic and cytotoxic activities Molecular Biology Microbiology |
| author_sort |
quinn, f. d. |
| spelling |
Quinn, F. D. Tompkins, L. S. 0950-382X 1365-2958 Wiley Molecular Biology Microbiology http://dx.doi.org/10.1111/j.1365-2958.1989.tb00228.x <jats:title>Summary</jats:title><jats:p>The DNA encoding the zinc metalloprotease of <jats:italic>Legionella pneumophila</jats:italic> Philadelphia 1 has been isolated and expressed in <jats:italic>Escherichia coli.</jats:italic> This protein, which is 38000 Daltons in size, possesses immunological and biochemical properties identical to those previously described for the purified <jats:italic>L. pneumophila</jats:italic> protease. Periplasmic extracts of E. <jats:italic>coli</jats:italic> clones expressing the recombinant protease are also capable of causing the haemolysis of canine erythrocytes and the cytotoxic destruction of CHO cells. Using trans‐poson mutagenesis, it was determined that a maximum of 1.2 kb of DNA encoded all three biological activities. Inactrvation of proteolytic activity by trans‐poson insertion occurred concomitantly with losses of the haemolytic and cytotoxic phenotypes. A putative regulatory sequence approximately 200‐500bp upstream of the gene's coding region was identified. A 4.0 kb fragment encoding these activities hybridized to the chromosomal DNA of the parent strain of <jats:italic>L. pneumophila</jats:italic> Philadelphia 1 as well as clinical isolates of <jats:italic>L. pneumophila.</jats:italic></jats:p> Analysis of a cloned sequence of <i>Legionella pneumophila</i> encoding a 38 kD metalloprotease possessing haemolytic and cytotoxic activities Molecular Microbiology |
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Molecular Microbiology |
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| title |
Analysis of a cloned sequence of Legionella pneumophila encoding a 38 kD metalloprotease possessing haemolytic and cytotoxic activities |
| title_unstemmed |
Analysis of a cloned sequence of Legionella pneumophila encoding a 38 kD metalloprotease possessing haemolytic and cytotoxic activities |
| title_full |
Analysis of a cloned sequence of Legionella pneumophila encoding a 38 kD metalloprotease possessing haemolytic and cytotoxic activities |
| title_fullStr |
Analysis of a cloned sequence of Legionella pneumophila encoding a 38 kD metalloprotease possessing haemolytic and cytotoxic activities |
| title_full_unstemmed |
Analysis of a cloned sequence of Legionella pneumophila encoding a 38 kD metalloprotease possessing haemolytic and cytotoxic activities |
| title_short |
Analysis of a cloned sequence of Legionella pneumophila encoding a 38 kD metalloprotease possessing haemolytic and cytotoxic activities |
| title_sort |
analysis of a cloned sequence of <i>legionella pneumophila</i> encoding a 38 kd metalloprotease possessing haemolytic and cytotoxic activities |
| topic |
Molecular Biology Microbiology |
| url |
http://dx.doi.org/10.1111/j.1365-2958.1989.tb00228.x |
| publishDate |
1989 |
| physical |
797-805 |
| description |
<jats:title>Summary</jats:title><jats:p>The DNA encoding the zinc metalloprotease of <jats:italic>Legionella pneumophila</jats:italic> Philadelphia 1 has been isolated and expressed in <jats:italic>Escherichia coli.</jats:italic> This protein, which is 38000 Daltons in size, possesses immunological and biochemical properties identical to those previously described for the purified <jats:italic>L. pneumophila</jats:italic> protease. Periplasmic extracts of E. <jats:italic>coli</jats:italic> clones expressing the recombinant protease are also capable of causing the haemolysis of canine erythrocytes and the cytotoxic destruction of CHO cells. Using trans‐poson mutagenesis, it was determined that a maximum of 1.2 kb of DNA encoded all three biological activities. Inactrvation of proteolytic activity by trans‐poson insertion occurred concomitantly with losses of the haemolytic and cytotoxic phenotypes. A putative regulatory sequence approximately 200‐500bp upstream of the gene's coding region was identified. A 4.0 kb fragment encoding these activities hybridized to the chromosomal DNA of the parent strain of <jats:italic>L. pneumophila</jats:italic> Philadelphia 1 as well as clinical isolates of <jats:italic>L. pneumophila.</jats:italic></jats:p> |
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| description | <jats:title>Summary</jats:title><jats:p>The DNA encoding the zinc metalloprotease of <jats:italic>Legionella pneumophila</jats:italic> Philadelphia 1 has been isolated and expressed in <jats:italic>Escherichia coli.</jats:italic> This protein, which is 38000 Daltons in size, possesses immunological and biochemical properties identical to those previously described for the purified <jats:italic>L. pneumophila</jats:italic> protease. Periplasmic extracts of E. <jats:italic>coli</jats:italic> clones expressing the recombinant protease are also capable of causing the haemolysis of canine erythrocytes and the cytotoxic destruction of CHO cells. Using trans‐poson mutagenesis, it was determined that a maximum of 1.2 kb of DNA encoded all three biological activities. Inactrvation of proteolytic activity by trans‐poson insertion occurred concomitantly with losses of the haemolytic and cytotoxic phenotypes. A putative regulatory sequence approximately 200‐500bp upstream of the gene's coding region was identified. A 4.0 kb fragment encoding these activities hybridized to the chromosomal DNA of the parent strain of <jats:italic>L. pneumophila</jats:italic> Philadelphia 1 as well as clinical isolates of <jats:italic>L. pneumophila.</jats:italic></jats:p> |
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| imprint | Wiley, 1989 |
| imprint_str_mv | Wiley, 1989 |
| institution | DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-D161 |
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| physical | 797-805 |
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| series | Molecular Microbiology |
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| spelling | Quinn, F. D. Tompkins, L. S. 0950-382X 1365-2958 Wiley Molecular Biology Microbiology http://dx.doi.org/10.1111/j.1365-2958.1989.tb00228.x <jats:title>Summary</jats:title><jats:p>The DNA encoding the zinc metalloprotease of <jats:italic>Legionella pneumophila</jats:italic> Philadelphia 1 has been isolated and expressed in <jats:italic>Escherichia coli.</jats:italic> This protein, which is 38000 Daltons in size, possesses immunological and biochemical properties identical to those previously described for the purified <jats:italic>L. pneumophila</jats:italic> protease. Periplasmic extracts of E. <jats:italic>coli</jats:italic> clones expressing the recombinant protease are also capable of causing the haemolysis of canine erythrocytes and the cytotoxic destruction of CHO cells. Using trans‐poson mutagenesis, it was determined that a maximum of 1.2 kb of DNA encoded all three biological activities. Inactrvation of proteolytic activity by trans‐poson insertion occurred concomitantly with losses of the haemolytic and cytotoxic phenotypes. A putative regulatory sequence approximately 200‐500bp upstream of the gene's coding region was identified. A 4.0 kb fragment encoding these activities hybridized to the chromosomal DNA of the parent strain of <jats:italic>L. pneumophila</jats:italic> Philadelphia 1 as well as clinical isolates of <jats:italic>L. pneumophila.</jats:italic></jats:p> Analysis of a cloned sequence of <i>Legionella pneumophila</i> encoding a 38 kD metalloprotease possessing haemolytic and cytotoxic activities Molecular Microbiology |
| spellingShingle | Quinn, F. D., Tompkins, L. S., Molecular Microbiology, Analysis of a cloned sequence of Legionella pneumophila encoding a 38 kD metalloprotease possessing haemolytic and cytotoxic activities, Molecular Biology, Microbiology |
| title | Analysis of a cloned sequence of Legionella pneumophila encoding a 38 kD metalloprotease possessing haemolytic and cytotoxic activities |
| title_full | Analysis of a cloned sequence of Legionella pneumophila encoding a 38 kD metalloprotease possessing haemolytic and cytotoxic activities |
| title_fullStr | Analysis of a cloned sequence of Legionella pneumophila encoding a 38 kD metalloprotease possessing haemolytic and cytotoxic activities |
| title_full_unstemmed | Analysis of a cloned sequence of Legionella pneumophila encoding a 38 kD metalloprotease possessing haemolytic and cytotoxic activities |
| title_short | Analysis of a cloned sequence of Legionella pneumophila encoding a 38 kD metalloprotease possessing haemolytic and cytotoxic activities |
| title_sort | analysis of a cloned sequence of <i>legionella pneumophila</i> encoding a 38 kd metalloprotease possessing haemolytic and cytotoxic activities |
| title_unstemmed | Analysis of a cloned sequence of Legionella pneumophila encoding a 38 kD metalloprotease possessing haemolytic and cytotoxic activities |
| topic | Molecular Biology, Microbiology |
| url | http://dx.doi.org/10.1111/j.1365-2958.1989.tb00228.x |