Klebsiella pneumoniae ST258 impairs intracellular elastase mobilization and persists within human neutrophils
Klebsiella pneumoniae (Kp) strains of sequence type (ST) 258 producing K. pneumoniae-carbapenemase (KPC) are a major cause of hospital-associated outbreaks and the main contributors of carbapenemase spreading. Here, we deepen into the mechanisms behind the inhibition of neutrophil bactericidal funct...
| Autores principales: | , , , , , , , , , |
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| Formato: | info:ar-repo/semantics/artículo |
| Lenguaje: | Inglés |
| Publicado: |
Elsevier
2025
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| Materias: | |
| Acceso en línea: | http://hdl.handle.net/20.500.12123/21502 https://www.sciencedirect.com/science/article/abs/pii/S0944501324004361 https://doi.org/10.1016/j.micres.2024.128035 |
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| author | Birnberg-Weiss, Federico Castro, Joselyn E. Pittaluga, Jose R. Castillo, Luis A. Martire-Greco, Daiana Fuentes, Federico Bigi, Fabiana Gomez, Sonia A. Landoni, Veronica I. Fernandez, Gabriela C. |
| author_browse | Bigi, Fabiana Birnberg-Weiss, Federico Castillo, Luis A. Castro, Joselyn E. Fernandez, Gabriela C. Fuentes, Federico Gomez, Sonia A. Landoni, Veronica I. Martire-Greco, Daiana Pittaluga, Jose R. |
| author_facet | Birnberg-Weiss, Federico Castro, Joselyn E. Pittaluga, Jose R. Castillo, Luis A. Martire-Greco, Daiana Fuentes, Federico Bigi, Fabiana Gomez, Sonia A. Landoni, Veronica I. Fernandez, Gabriela C. |
| author_sort | Birnberg-Weiss, Federico |
| collection | INTA Digital |
| description | Klebsiella pneumoniae (Kp) strains of sequence type (ST) 258 producing K. pneumoniae-carbapenemase (KPC) are a major cause of hospital-associated outbreaks and the main contributors of carbapenemase spreading. Here, we deepen into the mechanisms behind the inhibition of neutrophil bactericidal functions mediated by a clinical isolate of Kp ST258 KPC, Kp from now on. We found that NETs formation induced by different stimuli (PMA, ionomycin, Staphylococcus aureus) was significantly reduced in the presence of Kp. We revealed that Kp affects actin polymerization which correlates with impaired mobilization of elastase from azurophilic granules to the nucleus and reduced elastase mobilization towards phagosomes that contain bacteria. In line with these results, Kp survived within neutrophils for 3 h post-challenge without compromising neutrophil viability. We also found that different Kp clinical isolates inhibited NETs formation and actin polymerization. These results describe a strategy of evasion used by Kp to subvert PMN-mediating both intra and extracellular mechanisms of killing, representing a clear advantage for the survival and spreading of this multidrug-resistant bacteria. |
| format | info:ar-repo/semantics/artículo |
| id | INTA21502 |
| institution | Instituto Nacional de Tecnología Agropecuaria (INTA -Argentina) |
| language | Inglés |
| publishDate | 2025 |
| publishDateRange | 2025 |
| publishDateSort | 2025 |
| publisher | Elsevier |
| publisherStr | Elsevier |
| record_format | dspace |
| spelling | INTA215022025-02-28T10:56:50Z Klebsiella pneumoniae ST258 impairs intracellular elastase mobilization and persists within human neutrophils Birnberg-Weiss, Federico Castro, Joselyn E. Pittaluga, Jose R. Castillo, Luis A. Martire-Greco, Daiana Fuentes, Federico Bigi, Fabiana Gomez, Sonia A. Landoni, Veronica I. Fernandez, Gabriela C. Klebsiella pneumoniae Neutrófilos Neutrophils Klebsiella pneumoniae (Kp) strains of sequence type (ST) 258 producing K. pneumoniae-carbapenemase (KPC) are a major cause of hospital-associated outbreaks and the main contributors of carbapenemase spreading. Here, we deepen into the mechanisms behind the inhibition of neutrophil bactericidal functions mediated by a clinical isolate of Kp ST258 KPC, Kp from now on. We found that NETs formation induced by different stimuli (PMA, ionomycin, Staphylococcus aureus) was significantly reduced in the presence of Kp. We revealed that Kp affects actin polymerization which correlates with impaired mobilization of elastase from azurophilic granules to the nucleus and reduced elastase mobilization towards phagosomes that contain bacteria. In line with these results, Kp survived within neutrophils for 3 h post-challenge without compromising neutrophil viability. We also found that different Kp clinical isolates inhibited NETs formation and actin polymerization. These results describe a strategy of evasion used by Kp to subvert PMN-mediating both intra and extracellular mechanisms of killing, representing a clear advantage for the survival and spreading of this multidrug-resistant bacteria. Instituto de Biotecnología Fil: Birnberg-Weiss, Federico. Academia Nacional de Medicina de Buenos Aires. Instituto de Medicina Experimental. Laboratorio de Fisiología de los Procesos Inflamatorios; Argentina Fil: Birnberg-Weiss, Federico. Consejo Nacional de investigaciones Científicas y Técnicas; Argentina Fil: Castro, Joselyn E. Academia Nacional de Medicina de Buenos Aires. Instituto de Medicina Experimental. Laboratorio de Fisiología de los Procesos Inflamatorios; Argentina Fil: Castro, Joselyn E. Consejo Nacional de investigaciones Científicas y Técnicas; Argentina Fil: Pittaluga, Jose R. Academia Nacional de Medicina de Buenos Aires. Instituto de Medicina Experimental. Laboratorio de Fisiología de los Procesos Inflamatorios; Argentina Fil: Pittaluga, Jose R. Consejo Nacional de investigaciones Científicas y Técnicas; Argentina Fil: Castillo, Luis A. Academia Nacional de Medicina de Buenos Aires. Instituto de Medicina Experimental. Laboratorio de Fisiología de los Procesos Inflamatorios; Argentina Fil: Castillo, Luis A. Consejo Nacional de investigaciones Científicas y Técnicas; Argentina Fil: Martire-Greco, Daiana. Academia Nacional de Medicina de Buenos Aires. Instituto de Medicina Experimental. Laboratorio de Fisiología de los Procesos Inflamatorios; Argentina Fil: Martire-Greco, Daiana. Consejo Nacional de investigaciones Científicas y Técnicas; Argentina Fil: Fuentes, Federico. Academia Nacional de Medicina de Buenos Aires. Instituto de Medicina Experimental. Laboratorio de Fisiología de los Procesos Inflamatorios; Argentina Fil: Fuentes, Federico. Consejo Nacional de investigaciones Científicas y Técnicas; Argentina Fil: Bigi, Fabiana. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular; Argentina Fil: Bigi, Fabiana. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Gomez, Sonia A. Administración Nacional de Laboratorios e Institutos de Salud. Instituto Nacional de Enfermedades Infecciosas Dr. Carlos G. Malbrán. Servicio de Antimicrobianos; Argentina Fil: Gomez, Sonia A. Consejo Nacional de investigaciones Científicas y Técnicas; Argentina Fil: Landoni, Veronica I. Academia Nacional de Medicina de Buenos Aires. Instituto de Medicina Experimental. Laboratorio de Fisiología de los Procesos Inflamatorios; Argentina Fil: Landoni, Veronica I. Consejo Nacional de investigaciones Científicas y Técnicas; Argentina Fil: Fernandez, Gabriela C. Academia Nacional de Medicina de Buenos Aires. Instituto de Medicina Experimental. Laboratorio de Fisiología de los Procesos Inflamatorios; Argentina Fil: Fernandez, Gabriela C. Consejo Nacional de investigaciones Científicas y Técnicas; Argentina 2025-02-28T10:49:59Z 2025-02-28T10:49:59Z 2025-03 info:ar-repo/semantics/artículo info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://hdl.handle.net/20.500.12123/21502 https://www.sciencedirect.com/science/article/abs/pii/S0944501324004361 1618-0623 0944-5013 https://doi.org/10.1016/j.micres.2024.128035 eng info:eu-repo/semantics/restrictedAccess http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) application/pdf Elsevier Microbiological Research 292 : 128035 (March 2025) |
| spellingShingle | Klebsiella pneumoniae Neutrófilos Neutrophils Birnberg-Weiss, Federico Castro, Joselyn E. Pittaluga, Jose R. Castillo, Luis A. Martire-Greco, Daiana Fuentes, Federico Bigi, Fabiana Gomez, Sonia A. Landoni, Veronica I. Fernandez, Gabriela C. Klebsiella pneumoniae ST258 impairs intracellular elastase mobilization and persists within human neutrophils |
| title | Klebsiella pneumoniae ST258 impairs intracellular elastase mobilization and persists within human neutrophils |
| title_full | Klebsiella pneumoniae ST258 impairs intracellular elastase mobilization and persists within human neutrophils |
| title_fullStr | Klebsiella pneumoniae ST258 impairs intracellular elastase mobilization and persists within human neutrophils |
| title_full_unstemmed | Klebsiella pneumoniae ST258 impairs intracellular elastase mobilization and persists within human neutrophils |
| title_short | Klebsiella pneumoniae ST258 impairs intracellular elastase mobilization and persists within human neutrophils |
| title_sort | klebsiella pneumoniae st258 impairs intracellular elastase mobilization and persists within human neutrophils |
| topic | Klebsiella pneumoniae Neutrófilos Neutrophils |
| url | http://hdl.handle.net/20.500.12123/21502 https://www.sciencedirect.com/science/article/abs/pii/S0944501324004361 https://doi.org/10.1016/j.micres.2024.128035 |
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