Transcriptional organization of pneumococcal psrP-secY2A2 and impact of GtfA and GtfB deletion on PsrP-associated virulence properties
Pneumococcal serine-rich repeat protein (PsrP) is a glycoprotein that mediates Streptococcus pneumoniae attachment to lung cells and promotes biofilm formation. Herein, we investigated the transcriptional organization of psrP-secY2A2, the 37-kbp pathogenicity island encoding PsrP and its accessory g...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Lizcano, Anel [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2017transfer abstract |
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| Umfang: |
11 |
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| Übergeordnetes Werk: |
Enthalten in: A multifaceted educational intervention to prevent delirium in older inpatients: A before and after study - Wand, Anne P.F. ELSEVIER, 2014, a journal on infectious agents and host defenses, Paris [u.a.] |
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| Übergeordnetes Werk: |
volume:19 ; year:2017 ; number:6 ; pages:323-333 ; extent:11 |
| Links: |
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| DOI / URN: |
10.1016/j.micinf.2017.04.001 |
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ELV036064858 |
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| 245 | 1 | 0 | |a Transcriptional organization of pneumococcal psrP-secY2A2 and impact of GtfA and GtfB deletion on PsrP-associated virulence properties |
| 264 | 1 | |c 2017transfer abstract | |
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| 520 | |a Pneumococcal serine-rich repeat protein (PsrP) is a glycoprotein that mediates Streptococcus pneumoniae attachment to lung cells and promotes biofilm formation. Herein, we investigated the transcriptional organization of psrP-secY2A2, the 37-kbp pathogenicity island encoding PsrP and its accessory genes. PCR amplification of cDNA and RNA-seq analysis found psrP-secY2A2 to be minimally composed of three operons: psrP-glyA, glyB, and glyC-asp5. Transcription of all three operons was greatest during biofilm growth and immunoblot analyses confirmed increased PsrP production by biofilm pneumococci. Using gas chromatography–mass spectrometry we identified monomeric N-acetylglucosamine as the primary glycoconjugate present on a recombinant intracellular version of PsrP, i.e. PsrP1–734. This finding was validated by immunoblot using lectins with known carbohydrate specificities. We subsequently deleted gtfA and gtfB, the GTFs thought to be responsible for addition of O-linked N-acetylglucosamine, and tested for PsrP and its associated virulence properties. These deletions negatively affected our ability to detect PsrP1–734 in bacterial whole cell lysates. Moreover, S. pneumoniae mutants lacking these genes pheno-copied the psrP mutant and were attenuated for: biofilm formation, adhesion to lung epithelial cells, and pneumonia in mice. Our studies identify the transcriptional organization of psrP-secY2A2 and show the indispensable role of GtfA and GtfB on PsrP-mediated pneumococcal virulence. | ||
| 520 | |a Pneumococcal serine-rich repeat protein (PsrP) is a glycoprotein that mediates Streptococcus pneumoniae attachment to lung cells and promotes biofilm formation. Herein, we investigated the transcriptional organization of psrP-secY2A2, the 37-kbp pathogenicity island encoding PsrP and its accessory genes. PCR amplification of cDNA and RNA-seq analysis found psrP-secY2A2 to be minimally composed of three operons: psrP-glyA, glyB, and glyC-asp5. Transcription of all three operons was greatest during biofilm growth and immunoblot analyses confirmed increased PsrP production by biofilm pneumococci. Using gas chromatography–mass spectrometry we identified monomeric N-acetylglucosamine as the primary glycoconjugate present on a recombinant intracellular version of PsrP, i.e. PsrP1–734. This finding was validated by immunoblot using lectins with known carbohydrate specificities. We subsequently deleted gtfA and gtfB, the GTFs thought to be responsible for addition of O-linked N-acetylglucosamine, and tested for PsrP and its associated virulence properties. These deletions negatively affected our ability to detect PsrP1–734 in bacterial whole cell lysates. Moreover, S. pneumoniae mutants lacking these genes pheno-copied the psrP mutant and were attenuated for: biofilm formation, adhesion to lung epithelial cells, and pneumonia in mice. Our studies identify the transcriptional organization of psrP-secY2A2 and show the indispensable role of GtfA and GtfB on PsrP-mediated pneumococcal virulence. | ||
| 650 | 7 | |a Serine-rich repeat proteins |2 Elsevier | |
| 650 | 7 | |a Biofilms |2 Elsevier | |
| 650 | 7 | |a Transcription |2 Elsevier | |
| 650 | 7 | |a PsrP |2 Elsevier | |
| 650 | 7 | |a Streptococcus pneumoniae |2 Elsevier | |
| 650 | 7 | |a Glycosylation |2 Elsevier | |
| 700 | 1 | |a Akula Suresh Babu, Ramya |4 oth | |
| 700 | 1 | |a Shenoy, Anukul T. |4 oth | |
| 700 | 1 | |a Saville, Alison Maren |4 oth | |
| 700 | 1 | |a Kumar, Nikhil |4 oth | |
| 700 | 1 | |a D'Mello, Adonis |4 oth | |
| 700 | 1 | |a Hinojosa, Cecilia A. |4 oth | |
| 700 | 1 | |a Gilley, Ryan P. |4 oth | |
| 700 | 1 | |a Segovia, Jesus |4 oth | |
| 700 | 1 | |a Mitchell, Timothy J. |4 oth | |
| 700 | 1 | |a Tettelin, Hervé |4 oth | |
| 700 | 1 | |a Orihuela, Carlos J. |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |n Elsevier |a Wand, Anne P.F. ELSEVIER |t A multifaceted educational intervention to prevent delirium in older inpatients: A before and after study |d 2014 |d a journal on infectious agents and host defenses |g Paris [u.a.] |w (DE-627)ELV023093161 |
| 773 | 1 | 8 | |g volume:19 |g year:2017 |g number:6 |g pages:323-333 |g extent:11 |
| 856 | 4 | 0 | |u https://doi.org/10.1016/j.micinf.2017.04.001 |3 Volltext |
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2017transfer abstract |
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2017 |
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10.1016/j.micinf.2017.04.001 doi GBVA2017018000010.pica (DE-627)ELV036064858 (ELSEVIER)S1286-4579(17)30043-6 DE-627 ger DE-627 rakwb eng 570 570 DE-600 610 VZ 690 VZ 74.12 bkl 74.72 bkl Lizcano, Anel verfasserin aut Transcriptional organization of pneumococcal psrP-secY2A2 and impact of GtfA and GtfB deletion on PsrP-associated virulence properties 2017transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Pneumococcal serine-rich repeat protein (PsrP) is a glycoprotein that mediates Streptococcus pneumoniae attachment to lung cells and promotes biofilm formation. Herein, we investigated the transcriptional organization of psrP-secY2A2, the 37-kbp pathogenicity island encoding PsrP and its accessory genes. PCR amplification of cDNA and RNA-seq analysis found psrP-secY2A2 to be minimally composed of three operons: psrP-glyA, glyB, and glyC-asp5. Transcription of all three operons was greatest during biofilm growth and immunoblot analyses confirmed increased PsrP production by biofilm pneumococci. Using gas chromatography–mass spectrometry we identified monomeric N-acetylglucosamine as the primary glycoconjugate present on a recombinant intracellular version of PsrP, i.e. PsrP1–734. This finding was validated by immunoblot using lectins with known carbohydrate specificities. We subsequently deleted gtfA and gtfB, the GTFs thought to be responsible for addition of O-linked N-acetylglucosamine, and tested for PsrP and its associated virulence properties. These deletions negatively affected our ability to detect PsrP1–734 in bacterial whole cell lysates. Moreover, S. pneumoniae mutants lacking these genes pheno-copied the psrP mutant and were attenuated for: biofilm formation, adhesion to lung epithelial cells, and pneumonia in mice. Our studies identify the transcriptional organization of psrP-secY2A2 and show the indispensable role of GtfA and GtfB on PsrP-mediated pneumococcal virulence. Pneumococcal serine-rich repeat protein (PsrP) is a glycoprotein that mediates Streptococcus pneumoniae attachment to lung cells and promotes biofilm formation. Herein, we investigated the transcriptional organization of psrP-secY2A2, the 37-kbp pathogenicity island encoding PsrP and its accessory genes. PCR amplification of cDNA and RNA-seq analysis found psrP-secY2A2 to be minimally composed of three operons: psrP-glyA, glyB, and glyC-asp5. Transcription of all three operons was greatest during biofilm growth and immunoblot analyses confirmed increased PsrP production by biofilm pneumococci. Using gas chromatography–mass spectrometry we identified monomeric N-acetylglucosamine as the primary glycoconjugate present on a recombinant intracellular version of PsrP, i.e. PsrP1–734. This finding was validated by immunoblot using lectins with known carbohydrate specificities. We subsequently deleted gtfA and gtfB, the GTFs thought to be responsible for addition of O-linked N-acetylglucosamine, and tested for PsrP and its associated virulence properties. These deletions negatively affected our ability to detect PsrP1–734 in bacterial whole cell lysates. Moreover, S. pneumoniae mutants lacking these genes pheno-copied the psrP mutant and were attenuated for: biofilm formation, adhesion to lung epithelial cells, and pneumonia in mice. Our studies identify the transcriptional organization of psrP-secY2A2 and show the indispensable role of GtfA and GtfB on PsrP-mediated pneumococcal virulence. Serine-rich repeat proteins Elsevier Biofilms Elsevier Transcription Elsevier PsrP Elsevier Streptococcus pneumoniae Elsevier Glycosylation Elsevier Akula Suresh Babu, Ramya oth Shenoy, Anukul T. oth Saville, Alison Maren oth Kumar, Nikhil oth D'Mello, Adonis oth Hinojosa, Cecilia A. oth Gilley, Ryan P. oth Segovia, Jesus oth Mitchell, Timothy J. oth Tettelin, Hervé oth Orihuela, Carlos J. oth Enthalten in Elsevier Wand, Anne P.F. ELSEVIER A multifaceted educational intervention to prevent delirium in older inpatients: A before and after study 2014 a journal on infectious agents and host defenses Paris [u.a.] (DE-627)ELV023093161 volume:19 year:2017 number:6 pages:323-333 extent:11 https://doi.org/10.1016/j.micinf.2017.04.001 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO GBV_ILN_22 GBV_ILN_40 GBV_ILN_73 GBV_ILN_252 74.12 Stadtgeographie Siedlungsgeographie VZ 74.72 Stadtplanung kommunale Planung VZ AR 19 2017 6 323-333 11 045F 570 |
| spelling |
10.1016/j.micinf.2017.04.001 doi GBVA2017018000010.pica (DE-627)ELV036064858 (ELSEVIER)S1286-4579(17)30043-6 DE-627 ger DE-627 rakwb eng 570 570 DE-600 610 VZ 690 VZ 74.12 bkl 74.72 bkl Lizcano, Anel verfasserin aut Transcriptional organization of pneumococcal psrP-secY2A2 and impact of GtfA and GtfB deletion on PsrP-associated virulence properties 2017transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Pneumococcal serine-rich repeat protein (PsrP) is a glycoprotein that mediates Streptococcus pneumoniae attachment to lung cells and promotes biofilm formation. Herein, we investigated the transcriptional organization of psrP-secY2A2, the 37-kbp pathogenicity island encoding PsrP and its accessory genes. PCR amplification of cDNA and RNA-seq analysis found psrP-secY2A2 to be minimally composed of three operons: psrP-glyA, glyB, and glyC-asp5. Transcription of all three operons was greatest during biofilm growth and immunoblot analyses confirmed increased PsrP production by biofilm pneumococci. Using gas chromatography–mass spectrometry we identified monomeric N-acetylglucosamine as the primary glycoconjugate present on a recombinant intracellular version of PsrP, i.e. PsrP1–734. This finding was validated by immunoblot using lectins with known carbohydrate specificities. We subsequently deleted gtfA and gtfB, the GTFs thought to be responsible for addition of O-linked N-acetylglucosamine, and tested for PsrP and its associated virulence properties. These deletions negatively affected our ability to detect PsrP1–734 in bacterial whole cell lysates. Moreover, S. pneumoniae mutants lacking these genes pheno-copied the psrP mutant and were attenuated for: biofilm formation, adhesion to lung epithelial cells, and pneumonia in mice. Our studies identify the transcriptional organization of psrP-secY2A2 and show the indispensable role of GtfA and GtfB on PsrP-mediated pneumococcal virulence. Pneumococcal serine-rich repeat protein (PsrP) is a glycoprotein that mediates Streptococcus pneumoniae attachment to lung cells and promotes biofilm formation. Herein, we investigated the transcriptional organization of psrP-secY2A2, the 37-kbp pathogenicity island encoding PsrP and its accessory genes. PCR amplification of cDNA and RNA-seq analysis found psrP-secY2A2 to be minimally composed of three operons: psrP-glyA, glyB, and glyC-asp5. Transcription of all three operons was greatest during biofilm growth and immunoblot analyses confirmed increased PsrP production by biofilm pneumococci. Using gas chromatography–mass spectrometry we identified monomeric N-acetylglucosamine as the primary glycoconjugate present on a recombinant intracellular version of PsrP, i.e. PsrP1–734. This finding was validated by immunoblot using lectins with known carbohydrate specificities. We subsequently deleted gtfA and gtfB, the GTFs thought to be responsible for addition of O-linked N-acetylglucosamine, and tested for PsrP and its associated virulence properties. These deletions negatively affected our ability to detect PsrP1–734 in bacterial whole cell lysates. Moreover, S. pneumoniae mutants lacking these genes pheno-copied the psrP mutant and were attenuated for: biofilm formation, adhesion to lung epithelial cells, and pneumonia in mice. Our studies identify the transcriptional organization of psrP-secY2A2 and show the indispensable role of GtfA and GtfB on PsrP-mediated pneumococcal virulence. Serine-rich repeat proteins Elsevier Biofilms Elsevier Transcription Elsevier PsrP Elsevier Streptococcus pneumoniae Elsevier Glycosylation Elsevier Akula Suresh Babu, Ramya oth Shenoy, Anukul T. oth Saville, Alison Maren oth Kumar, Nikhil oth D'Mello, Adonis oth Hinojosa, Cecilia A. oth Gilley, Ryan P. oth Segovia, Jesus oth Mitchell, Timothy J. oth Tettelin, Hervé oth Orihuela, Carlos J. oth Enthalten in Elsevier Wand, Anne P.F. ELSEVIER A multifaceted educational intervention to prevent delirium in older inpatients: A before and after study 2014 a journal on infectious agents and host defenses Paris [u.a.] (DE-627)ELV023093161 volume:19 year:2017 number:6 pages:323-333 extent:11 https://doi.org/10.1016/j.micinf.2017.04.001 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO GBV_ILN_22 GBV_ILN_40 GBV_ILN_73 GBV_ILN_252 74.12 Stadtgeographie Siedlungsgeographie VZ 74.72 Stadtplanung kommunale Planung VZ AR 19 2017 6 323-333 11 045F 570 |
| allfields_unstemmed |
10.1016/j.micinf.2017.04.001 doi GBVA2017018000010.pica (DE-627)ELV036064858 (ELSEVIER)S1286-4579(17)30043-6 DE-627 ger DE-627 rakwb eng 570 570 DE-600 610 VZ 690 VZ 74.12 bkl 74.72 bkl Lizcano, Anel verfasserin aut Transcriptional organization of pneumococcal psrP-secY2A2 and impact of GtfA and GtfB deletion on PsrP-associated virulence properties 2017transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Pneumococcal serine-rich repeat protein (PsrP) is a glycoprotein that mediates Streptococcus pneumoniae attachment to lung cells and promotes biofilm formation. Herein, we investigated the transcriptional organization of psrP-secY2A2, the 37-kbp pathogenicity island encoding PsrP and its accessory genes. PCR amplification of cDNA and RNA-seq analysis found psrP-secY2A2 to be minimally composed of three operons: psrP-glyA, glyB, and glyC-asp5. Transcription of all three operons was greatest during biofilm growth and immunoblot analyses confirmed increased PsrP production by biofilm pneumococci. Using gas chromatography–mass spectrometry we identified monomeric N-acetylglucosamine as the primary glycoconjugate present on a recombinant intracellular version of PsrP, i.e. PsrP1–734. This finding was validated by immunoblot using lectins with known carbohydrate specificities. We subsequently deleted gtfA and gtfB, the GTFs thought to be responsible for addition of O-linked N-acetylglucosamine, and tested for PsrP and its associated virulence properties. These deletions negatively affected our ability to detect PsrP1–734 in bacterial whole cell lysates. Moreover, S. pneumoniae mutants lacking these genes pheno-copied the psrP mutant and were attenuated for: biofilm formation, adhesion to lung epithelial cells, and pneumonia in mice. Our studies identify the transcriptional organization of psrP-secY2A2 and show the indispensable role of GtfA and GtfB on PsrP-mediated pneumococcal virulence. Pneumococcal serine-rich repeat protein (PsrP) is a glycoprotein that mediates Streptococcus pneumoniae attachment to lung cells and promotes biofilm formation. Herein, we investigated the transcriptional organization of psrP-secY2A2, the 37-kbp pathogenicity island encoding PsrP and its accessory genes. PCR amplification of cDNA and RNA-seq analysis found psrP-secY2A2 to be minimally composed of three operons: psrP-glyA, glyB, and glyC-asp5. Transcription of all three operons was greatest during biofilm growth and immunoblot analyses confirmed increased PsrP production by biofilm pneumococci. Using gas chromatography–mass spectrometry we identified monomeric N-acetylglucosamine as the primary glycoconjugate present on a recombinant intracellular version of PsrP, i.e. PsrP1–734. This finding was validated by immunoblot using lectins with known carbohydrate specificities. We subsequently deleted gtfA and gtfB, the GTFs thought to be responsible for addition of O-linked N-acetylglucosamine, and tested for PsrP and its associated virulence properties. These deletions negatively affected our ability to detect PsrP1–734 in bacterial whole cell lysates. Moreover, S. pneumoniae mutants lacking these genes pheno-copied the psrP mutant and were attenuated for: biofilm formation, adhesion to lung epithelial cells, and pneumonia in mice. Our studies identify the transcriptional organization of psrP-secY2A2 and show the indispensable role of GtfA and GtfB on PsrP-mediated pneumococcal virulence. Serine-rich repeat proteins Elsevier Biofilms Elsevier Transcription Elsevier PsrP Elsevier Streptococcus pneumoniae Elsevier Glycosylation Elsevier Akula Suresh Babu, Ramya oth Shenoy, Anukul T. oth Saville, Alison Maren oth Kumar, Nikhil oth D'Mello, Adonis oth Hinojosa, Cecilia A. oth Gilley, Ryan P. oth Segovia, Jesus oth Mitchell, Timothy J. oth Tettelin, Hervé oth Orihuela, Carlos J. oth Enthalten in Elsevier Wand, Anne P.F. ELSEVIER A multifaceted educational intervention to prevent delirium in older inpatients: A before and after study 2014 a journal on infectious agents and host defenses Paris [u.a.] (DE-627)ELV023093161 volume:19 year:2017 number:6 pages:323-333 extent:11 https://doi.org/10.1016/j.micinf.2017.04.001 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO GBV_ILN_22 GBV_ILN_40 GBV_ILN_73 GBV_ILN_252 74.12 Stadtgeographie Siedlungsgeographie VZ 74.72 Stadtplanung kommunale Planung VZ AR 19 2017 6 323-333 11 045F 570 |
| allfieldsGer |
10.1016/j.micinf.2017.04.001 doi GBVA2017018000010.pica (DE-627)ELV036064858 (ELSEVIER)S1286-4579(17)30043-6 DE-627 ger DE-627 rakwb eng 570 570 DE-600 610 VZ 690 VZ 74.12 bkl 74.72 bkl Lizcano, Anel verfasserin aut Transcriptional organization of pneumococcal psrP-secY2A2 and impact of GtfA and GtfB deletion on PsrP-associated virulence properties 2017transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Pneumococcal serine-rich repeat protein (PsrP) is a glycoprotein that mediates Streptococcus pneumoniae attachment to lung cells and promotes biofilm formation. Herein, we investigated the transcriptional organization of psrP-secY2A2, the 37-kbp pathogenicity island encoding PsrP and its accessory genes. PCR amplification of cDNA and RNA-seq analysis found psrP-secY2A2 to be minimally composed of three operons: psrP-glyA, glyB, and glyC-asp5. Transcription of all three operons was greatest during biofilm growth and immunoblot analyses confirmed increased PsrP production by biofilm pneumococci. Using gas chromatography–mass spectrometry we identified monomeric N-acetylglucosamine as the primary glycoconjugate present on a recombinant intracellular version of PsrP, i.e. PsrP1–734. This finding was validated by immunoblot using lectins with known carbohydrate specificities. We subsequently deleted gtfA and gtfB, the GTFs thought to be responsible for addition of O-linked N-acetylglucosamine, and tested for PsrP and its associated virulence properties. These deletions negatively affected our ability to detect PsrP1–734 in bacterial whole cell lysates. Moreover, S. pneumoniae mutants lacking these genes pheno-copied the psrP mutant and were attenuated for: biofilm formation, adhesion to lung epithelial cells, and pneumonia in mice. Our studies identify the transcriptional organization of psrP-secY2A2 and show the indispensable role of GtfA and GtfB on PsrP-mediated pneumococcal virulence. Pneumococcal serine-rich repeat protein (PsrP) is a glycoprotein that mediates Streptococcus pneumoniae attachment to lung cells and promotes biofilm formation. Herein, we investigated the transcriptional organization of psrP-secY2A2, the 37-kbp pathogenicity island encoding PsrP and its accessory genes. PCR amplification of cDNA and RNA-seq analysis found psrP-secY2A2 to be minimally composed of three operons: psrP-glyA, glyB, and glyC-asp5. Transcription of all three operons was greatest during biofilm growth and immunoblot analyses confirmed increased PsrP production by biofilm pneumococci. Using gas chromatography–mass spectrometry we identified monomeric N-acetylglucosamine as the primary glycoconjugate present on a recombinant intracellular version of PsrP, i.e. PsrP1–734. This finding was validated by immunoblot using lectins with known carbohydrate specificities. We subsequently deleted gtfA and gtfB, the GTFs thought to be responsible for addition of O-linked N-acetylglucosamine, and tested for PsrP and its associated virulence properties. These deletions negatively affected our ability to detect PsrP1–734 in bacterial whole cell lysates. Moreover, S. pneumoniae mutants lacking these genes pheno-copied the psrP mutant and were attenuated for: biofilm formation, adhesion to lung epithelial cells, and pneumonia in mice. Our studies identify the transcriptional organization of psrP-secY2A2 and show the indispensable role of GtfA and GtfB on PsrP-mediated pneumococcal virulence. Serine-rich repeat proteins Elsevier Biofilms Elsevier Transcription Elsevier PsrP Elsevier Streptococcus pneumoniae Elsevier Glycosylation Elsevier Akula Suresh Babu, Ramya oth Shenoy, Anukul T. oth Saville, Alison Maren oth Kumar, Nikhil oth D'Mello, Adonis oth Hinojosa, Cecilia A. oth Gilley, Ryan P. oth Segovia, Jesus oth Mitchell, Timothy J. oth Tettelin, Hervé oth Orihuela, Carlos J. oth Enthalten in Elsevier Wand, Anne P.F. ELSEVIER A multifaceted educational intervention to prevent delirium in older inpatients: A before and after study 2014 a journal on infectious agents and host defenses Paris [u.a.] (DE-627)ELV023093161 volume:19 year:2017 number:6 pages:323-333 extent:11 https://doi.org/10.1016/j.micinf.2017.04.001 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO GBV_ILN_22 GBV_ILN_40 GBV_ILN_73 GBV_ILN_252 74.12 Stadtgeographie Siedlungsgeographie VZ 74.72 Stadtplanung kommunale Planung VZ AR 19 2017 6 323-333 11 045F 570 |
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10.1016/j.micinf.2017.04.001 doi GBVA2017018000010.pica (DE-627)ELV036064858 (ELSEVIER)S1286-4579(17)30043-6 DE-627 ger DE-627 rakwb eng 570 570 DE-600 610 VZ 690 VZ 74.12 bkl 74.72 bkl Lizcano, Anel verfasserin aut Transcriptional organization of pneumococcal psrP-secY2A2 and impact of GtfA and GtfB deletion on PsrP-associated virulence properties 2017transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Pneumococcal serine-rich repeat protein (PsrP) is a glycoprotein that mediates Streptococcus pneumoniae attachment to lung cells and promotes biofilm formation. Herein, we investigated the transcriptional organization of psrP-secY2A2, the 37-kbp pathogenicity island encoding PsrP and its accessory genes. PCR amplification of cDNA and RNA-seq analysis found psrP-secY2A2 to be minimally composed of three operons: psrP-glyA, glyB, and glyC-asp5. Transcription of all three operons was greatest during biofilm growth and immunoblot analyses confirmed increased PsrP production by biofilm pneumococci. Using gas chromatography–mass spectrometry we identified monomeric N-acetylglucosamine as the primary glycoconjugate present on a recombinant intracellular version of PsrP, i.e. PsrP1–734. This finding was validated by immunoblot using lectins with known carbohydrate specificities. We subsequently deleted gtfA and gtfB, the GTFs thought to be responsible for addition of O-linked N-acetylglucosamine, and tested for PsrP and its associated virulence properties. These deletions negatively affected our ability to detect PsrP1–734 in bacterial whole cell lysates. Moreover, S. pneumoniae mutants lacking these genes pheno-copied the psrP mutant and were attenuated for: biofilm formation, adhesion to lung epithelial cells, and pneumonia in mice. Our studies identify the transcriptional organization of psrP-secY2A2 and show the indispensable role of GtfA and GtfB on PsrP-mediated pneumococcal virulence. Pneumococcal serine-rich repeat protein (PsrP) is a glycoprotein that mediates Streptococcus pneumoniae attachment to lung cells and promotes biofilm formation. Herein, we investigated the transcriptional organization of psrP-secY2A2, the 37-kbp pathogenicity island encoding PsrP and its accessory genes. PCR amplification of cDNA and RNA-seq analysis found psrP-secY2A2 to be minimally composed of three operons: psrP-glyA, glyB, and glyC-asp5. Transcription of all three operons was greatest during biofilm growth and immunoblot analyses confirmed increased PsrP production by biofilm pneumococci. Using gas chromatography–mass spectrometry we identified monomeric N-acetylglucosamine as the primary glycoconjugate present on a recombinant intracellular version of PsrP, i.e. PsrP1–734. This finding was validated by immunoblot using lectins with known carbohydrate specificities. We subsequently deleted gtfA and gtfB, the GTFs thought to be responsible for addition of O-linked N-acetylglucosamine, and tested for PsrP and its associated virulence properties. These deletions negatively affected our ability to detect PsrP1–734 in bacterial whole cell lysates. Moreover, S. pneumoniae mutants lacking these genes pheno-copied the psrP mutant and were attenuated for: biofilm formation, adhesion to lung epithelial cells, and pneumonia in mice. Our studies identify the transcriptional organization of psrP-secY2A2 and show the indispensable role of GtfA and GtfB on PsrP-mediated pneumococcal virulence. Serine-rich repeat proteins Elsevier Biofilms Elsevier Transcription Elsevier PsrP Elsevier Streptococcus pneumoniae Elsevier Glycosylation Elsevier Akula Suresh Babu, Ramya oth Shenoy, Anukul T. oth Saville, Alison Maren oth Kumar, Nikhil oth D'Mello, Adonis oth Hinojosa, Cecilia A. oth Gilley, Ryan P. oth Segovia, Jesus oth Mitchell, Timothy J. oth Tettelin, Hervé oth Orihuela, Carlos J. oth Enthalten in Elsevier Wand, Anne P.F. ELSEVIER A multifaceted educational intervention to prevent delirium in older inpatients: A before and after study 2014 a journal on infectious agents and host defenses Paris [u.a.] (DE-627)ELV023093161 volume:19 year:2017 number:6 pages:323-333 extent:11 https://doi.org/10.1016/j.micinf.2017.04.001 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO GBV_ILN_22 GBV_ILN_40 GBV_ILN_73 GBV_ILN_252 74.12 Stadtgeographie Siedlungsgeographie VZ 74.72 Stadtplanung kommunale Planung VZ AR 19 2017 6 323-333 11 045F 570 |
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Transcriptional organization of pneumococcal psrP-secY2A2 and impact of GtfA and GtfB deletion on PsrP-associated virulence properties |
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Pneumococcal serine-rich repeat protein (PsrP) is a glycoprotein that mediates Streptococcus pneumoniae attachment to lung cells and promotes biofilm formation. Herein, we investigated the transcriptional organization of psrP-secY2A2, the 37-kbp pathogenicity island encoding PsrP and its accessory genes. PCR amplification of cDNA and RNA-seq analysis found psrP-secY2A2 to be minimally composed of three operons: psrP-glyA, glyB, and glyC-asp5. Transcription of all three operons was greatest during biofilm growth and immunoblot analyses confirmed increased PsrP production by biofilm pneumococci. Using gas chromatography–mass spectrometry we identified monomeric N-acetylglucosamine as the primary glycoconjugate present on a recombinant intracellular version of PsrP, i.e. PsrP1–734. This finding was validated by immunoblot using lectins with known carbohydrate specificities. We subsequently deleted gtfA and gtfB, the GTFs thought to be responsible for addition of O-linked N-acetylglucosamine, and tested for PsrP and its associated virulence properties. These deletions negatively affected our ability to detect PsrP1–734 in bacterial whole cell lysates. Moreover, S. pneumoniae mutants lacking these genes pheno-copied the psrP mutant and were attenuated for: biofilm formation, adhesion to lung epithelial cells, and pneumonia in mice. Our studies identify the transcriptional organization of psrP-secY2A2 and show the indispensable role of GtfA and GtfB on PsrP-mediated pneumococcal virulence. |
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Pneumococcal serine-rich repeat protein (PsrP) is a glycoprotein that mediates Streptococcus pneumoniae attachment to lung cells and promotes biofilm formation. Herein, we investigated the transcriptional organization of psrP-secY2A2, the 37-kbp pathogenicity island encoding PsrP and its accessory genes. PCR amplification of cDNA and RNA-seq analysis found psrP-secY2A2 to be minimally composed of three operons: psrP-glyA, glyB, and glyC-asp5. Transcription of all three operons was greatest during biofilm growth and immunoblot analyses confirmed increased PsrP production by biofilm pneumococci. Using gas chromatography–mass spectrometry we identified monomeric N-acetylglucosamine as the primary glycoconjugate present on a recombinant intracellular version of PsrP, i.e. PsrP1–734. This finding was validated by immunoblot using lectins with known carbohydrate specificities. We subsequently deleted gtfA and gtfB, the GTFs thought to be responsible for addition of O-linked N-acetylglucosamine, and tested for PsrP and its associated virulence properties. These deletions negatively affected our ability to detect PsrP1–734 in bacterial whole cell lysates. Moreover, S. pneumoniae mutants lacking these genes pheno-copied the psrP mutant and were attenuated for: biofilm formation, adhesion to lung epithelial cells, and pneumonia in mice. Our studies identify the transcriptional organization of psrP-secY2A2 and show the indispensable role of GtfA and GtfB on PsrP-mediated pneumococcal virulence. |
| abstract_unstemmed |
Pneumococcal serine-rich repeat protein (PsrP) is a glycoprotein that mediates Streptococcus pneumoniae attachment to lung cells and promotes biofilm formation. Herein, we investigated the transcriptional organization of psrP-secY2A2, the 37-kbp pathogenicity island encoding PsrP and its accessory genes. PCR amplification of cDNA and RNA-seq analysis found psrP-secY2A2 to be minimally composed of three operons: psrP-glyA, glyB, and glyC-asp5. Transcription of all three operons was greatest during biofilm growth and immunoblot analyses confirmed increased PsrP production by biofilm pneumococci. Using gas chromatography–mass spectrometry we identified monomeric N-acetylglucosamine as the primary glycoconjugate present on a recombinant intracellular version of PsrP, i.e. PsrP1–734. This finding was validated by immunoblot using lectins with known carbohydrate specificities. We subsequently deleted gtfA and gtfB, the GTFs thought to be responsible for addition of O-linked N-acetylglucosamine, and tested for PsrP and its associated virulence properties. These deletions negatively affected our ability to detect PsrP1–734 in bacterial whole cell lysates. Moreover, S. pneumoniae mutants lacking these genes pheno-copied the psrP mutant and were attenuated for: biofilm formation, adhesion to lung epithelial cells, and pneumonia in mice. Our studies identify the transcriptional organization of psrP-secY2A2 and show the indispensable role of GtfA and GtfB on PsrP-mediated pneumococcal virulence. |
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| title_short |
Transcriptional organization of pneumococcal psrP-secY2A2 and impact of GtfA and GtfB deletion on PsrP-associated virulence properties |
| url |
https://doi.org/10.1016/j.micinf.2017.04.001 |
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Akula Suresh Babu, Ramya Shenoy, Anukul T. Saville, Alison Maren Kumar, Nikhil D'Mello, Adonis Hinojosa, Cecilia A. Gilley, Ryan P. Segovia, Jesus Mitchell, Timothy J. Tettelin, Hervé Orihuela, Carlos J. |
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Akula Suresh Babu, Ramya Shenoy, Anukul T. Saville, Alison Maren Kumar, Nikhil D'Mello, Adonis Hinojosa, Cecilia A. Gilley, Ryan P. Segovia, Jesus Mitchell, Timothy J. Tettelin, Hervé Orihuela, Carlos J. |
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10.1016/j.micinf.2017.04.001 |
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2024-07-06T19:12:27.765Z |
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