Proteomic Adaptation of <i>Streptococcus pneumoniae</i> to the Antimicrobial Peptide Human Beta Defensin 3 (hBD3) in Comparison to Other Cell Surface Stresses
The antimicrobial peptide human Beta defensin 3 (hBD3) is an essential part of the innate immune system and is involved in protection against respiratory pathogens by specifically permeabilizing bacterial membranes. The Gram-positive bacterium <i>Streptococcus pneumoniae</i> causes serio...
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| Format: | Article |
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MDPI AG
2020-10-01
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| Series: | Microorganisms |
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| Online Access: | https://www.mdpi.com/2076-2607/8/11/1697 |
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| author | Pierre-Alexander Mücke Anne Ostrzinski Sven Hammerschmidt Sandra Maaß Dörte Becher |
| author_facet | Pierre-Alexander Mücke Anne Ostrzinski Sven Hammerschmidt Sandra Maaß Dörte Becher |
| author_sort | Pierre-Alexander Mücke |
| collection | DOAJ |
| description | The antimicrobial peptide human Beta defensin 3 (hBD3) is an essential part of the innate immune system and is involved in protection against respiratory pathogens by specifically permeabilizing bacterial membranes. The Gram-positive bacterium <i>Streptococcus pneumoniae</i> causes serious diseases including pneumonia, meningitis, and septicemia, despite being frequently exposed to human defense molecules, including hBD3 during colonization and infection. Thus, the question arises how pneumococci adapt to stress caused by antimicrobial peptides. We addressed this subject by analyzing the proteome of <i>S. pneumoniae</i> after treatment with hBD3 and compared our data with the proteomic changes induced by LL-37, another crucial antimicrobial peptide present in the human respiratory tract. As antimicrobial peptides usually cause membrane perturbations, the response to the membrane active cationic detergent cetyltrimethylammonium bromide (CTAB) was examined to assess the specificity of the pneumococcal response to antimicrobial peptides. In brief, hBD3 and LL-37 induce a similar response in pneumococci and especially, changes in proteins with annotated transporter and virulence function have been identified. However, LL-37 causes changes in the abundance of cell surface modification proteins that cannot be observed after treatment with hBD3. Interestingly, CTAB induces unique proteomic changes in <i>S. pneumoniae</i>. Though, the detergent seems to activate a two-component system that is also activated in response to antimicrobial peptide stress (TCS 05). Overall, our data represent a novel resource on pneumococcal adaptation to specific cell surface stresses on a functional level. This knowledge can potentially be used to develop strategies to circumvent pneumococcal resistance to antimicrobial peptides. |
| first_indexed | 2024-03-10T15:11:47Z |
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| id | doaj.art-41d2641f18bc4ee89a3233eb202ea136 |
| institution | Directory Open Access Journal |
| issn | 2076-2607 |
| language | English |
| last_indexed | 2024-03-10T15:11:47Z |
| publishDate | 2020-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Microorganisms |
| spelling | doaj.art-41d2641f18bc4ee89a3233eb202ea1362023-11-20T19:15:01ZengMDPI AGMicroorganisms2076-26072020-10-01811169710.3390/microorganisms8111697Proteomic Adaptation of <i>Streptococcus pneumoniae</i> to the Antimicrobial Peptide Human Beta Defensin 3 (hBD3) in Comparison to Other Cell Surface StressesPierre-Alexander Mücke0Anne Ostrzinski1Sven Hammerschmidt2Sandra Maaß3Dörte Becher4Department of Microbial Proteomics, Institute of Microbiology, Center for Functional Genomics of Microbes, University of Greifswald, Felix-Hausdorff-Str. 8, 17489 Greifswald, GermanyDepartment of Microbial Proteomics, Institute of Microbiology, Center for Functional Genomics of Microbes, University of Greifswald, Felix-Hausdorff-Str. 8, 17489 Greifswald, GermanyDepartment of Molecular Genetics and Infection Biology, Interfaculty Institute for Genetics and Functional Genomics, Center for Functional Genomics of Microbes, University of Greifswald, Felix-Hausdorff-Str. 8, 17489 Greifswald, GermanyDepartment of Microbial Proteomics, Institute of Microbiology, Center for Functional Genomics of Microbes, University of Greifswald, Felix-Hausdorff-Str. 8, 17489 Greifswald, GermanyDepartment of Microbial Proteomics, Institute of Microbiology, Center for Functional Genomics of Microbes, University of Greifswald, Felix-Hausdorff-Str. 8, 17489 Greifswald, GermanyThe antimicrobial peptide human Beta defensin 3 (hBD3) is an essential part of the innate immune system and is involved in protection against respiratory pathogens by specifically permeabilizing bacterial membranes. The Gram-positive bacterium <i>Streptococcus pneumoniae</i> causes serious diseases including pneumonia, meningitis, and septicemia, despite being frequently exposed to human defense molecules, including hBD3 during colonization and infection. Thus, the question arises how pneumococci adapt to stress caused by antimicrobial peptides. We addressed this subject by analyzing the proteome of <i>S. pneumoniae</i> after treatment with hBD3 and compared our data with the proteomic changes induced by LL-37, another crucial antimicrobial peptide present in the human respiratory tract. As antimicrobial peptides usually cause membrane perturbations, the response to the membrane active cationic detergent cetyltrimethylammonium bromide (CTAB) was examined to assess the specificity of the pneumococcal response to antimicrobial peptides. In brief, hBD3 and LL-37 induce a similar response in pneumococci and especially, changes in proteins with annotated transporter and virulence function have been identified. However, LL-37 causes changes in the abundance of cell surface modification proteins that cannot be observed after treatment with hBD3. Interestingly, CTAB induces unique proteomic changes in <i>S. pneumoniae</i>. Though, the detergent seems to activate a two-component system that is also activated in response to antimicrobial peptide stress (TCS 05). Overall, our data represent a novel resource on pneumococcal adaptation to specific cell surface stresses on a functional level. This knowledge can potentially be used to develop strategies to circumvent pneumococcal resistance to antimicrobial peptides.https://www.mdpi.com/2076-2607/8/11/1697<i>Streptococcus pneumoniae</i>antimicrobial peptideshBD3LL-37adaptationproteomics |
| spellingShingle | Pierre-Alexander Mücke Anne Ostrzinski Sven Hammerschmidt Sandra Maaß Dörte Becher Proteomic Adaptation of <i>Streptococcus pneumoniae</i> to the Antimicrobial Peptide Human Beta Defensin 3 (hBD3) in Comparison to Other Cell Surface Stresses Microorganisms <i>Streptococcus pneumoniae</i> antimicrobial peptides hBD3 LL-37 adaptation proteomics |
| title | Proteomic Adaptation of <i>Streptococcus pneumoniae</i> to the Antimicrobial Peptide Human Beta Defensin 3 (hBD3) in Comparison to Other Cell Surface Stresses |
| title_full | Proteomic Adaptation of <i>Streptococcus pneumoniae</i> to the Antimicrobial Peptide Human Beta Defensin 3 (hBD3) in Comparison to Other Cell Surface Stresses |
| title_fullStr | Proteomic Adaptation of <i>Streptococcus pneumoniae</i> to the Antimicrobial Peptide Human Beta Defensin 3 (hBD3) in Comparison to Other Cell Surface Stresses |
| title_full_unstemmed | Proteomic Adaptation of <i>Streptococcus pneumoniae</i> to the Antimicrobial Peptide Human Beta Defensin 3 (hBD3) in Comparison to Other Cell Surface Stresses |
| title_short | Proteomic Adaptation of <i>Streptococcus pneumoniae</i> to the Antimicrobial Peptide Human Beta Defensin 3 (hBD3) in Comparison to Other Cell Surface Stresses |
| title_sort | proteomic adaptation of i streptococcus pneumoniae i to the antimicrobial peptide human beta defensin 3 hbd3 in comparison to other cell surface stresses |
| topic | <i>Streptococcus pneumoniae</i> antimicrobial peptides hBD3 LL-37 adaptation proteomics |
| url | https://www.mdpi.com/2076-2607/8/11/1697 |
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