FhaA plays a key role in mycobacterial polar elongation and asymmetric growth
Mycobacteria, including pathogens like Mycobacterium tuberculosis, exhibit unique growth patterns and cell envelope structures that challenge our understanding of bacterial physiology. This study sheds light on FhaA, a conserved protein in Mycobacteriales, revealing its pivotal role in coordinating...
| Autores principales: | , , , , , , , , , , , , , , |
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| Formato: | Artículo |
| Lenguaje: | Inglés |
| Publicado: |
American Society for Microbiology
2025
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| Acceso en línea: | http://hdl.handle.net/20.500.12123/21814 https://journals.asm.org/doi/10.1128/mbio.02526-24 https://doi.org/10.1128/mbio.02526-24 |
| _version_ | 1855486822556106752 |
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| author | Rossello, Jessica Rivera, Bernardina Anzibar Fialho, Maximiliano Augusto, Ingrid Gil, Magdalena Forrellad, Marina Andrea Bigi, Fabiana Rodríguez Taño, Azalia Urdániz, Estefanía Piuri, Mariana Miranda, Kildare Wehenkel, Anne Marie Alzari, Pedro M. Malacrida, Leonel Durán, Rosario |
| author_browse | Alzari, Pedro M. Anzibar Fialho, Maximiliano Augusto, Ingrid Bigi, Fabiana Durán, Rosario Forrellad, Marina Andrea Gil, Magdalena Malacrida, Leonel Miranda, Kildare Piuri, Mariana Rivera, Bernardina Rodríguez Taño, Azalia Rossello, Jessica Urdániz, Estefanía Wehenkel, Anne Marie |
| author_facet | Rossello, Jessica Rivera, Bernardina Anzibar Fialho, Maximiliano Augusto, Ingrid Gil, Magdalena Forrellad, Marina Andrea Bigi, Fabiana Rodríguez Taño, Azalia Urdániz, Estefanía Piuri, Mariana Miranda, Kildare Wehenkel, Anne Marie Alzari, Pedro M. Malacrida, Leonel Durán, Rosario |
| author_sort | Rossello, Jessica |
| collection | INTA Digital |
| description | Mycobacteria, including pathogens like Mycobacterium tuberculosis, exhibit unique growth patterns and cell envelope structures that challenge our understanding of bacterial physiology. This study sheds light on FhaA, a conserved protein in Mycobacteriales, revealing its pivotal role in coordinating cell envelope biogenesis and asymmetric growth. The elucidation of the FhaA interactome in living mycobacterial cells reveals its participation in the protein network orchestrating cell envelope biogenesis and cell elongation/division. By manipulating FhaA levels, we uncovered its influence on cell morphology, cell envelope organization, and the localization of peptidoglycan biosynthesis machinery. Notably, fhaA deletion disrupted the characteristic asymmetric growth of mycobacteria, highlighting its importance in maintaining this distinctive feature. Our findings position FhaA as a key regulator in a complex protein network, orchestrating the asymmetric distribution and activity of cell envelope biosynthetic machinery. This work not only advances our understanding of mycobacterial growth mechanisms but also identifies FhaA as a potential target for future studies on cell envelope biogenesis and bacterial growth regulation. These insights into the fundamental biology of mycobacteria may pave the way for novel approaches to combat mycobacterial infections addressing the ongoing challenge of diseases like tuberculosis in global health. |
| format | Artículo |
| id | INTA21814 |
| institution | Instituto Nacional de Tecnología Agropecuaria (INTA -Argentina) |
| language | Inglés |
| publishDate | 2025 |
| publishDateRange | 2025 |
| publishDateSort | 2025 |
| publisher | American Society for Microbiology |
| publisherStr | American Society for Microbiology |
| record_format | dspace |
| spelling | INTA218142025-03-26T10:34:03Z FhaA plays a key role in mycobacterial polar elongation and asymmetric growth Rossello, Jessica Rivera, Bernardina Anzibar Fialho, Maximiliano Augusto, Ingrid Gil, Magdalena Forrellad, Marina Andrea Bigi, Fabiana Rodríguez Taño, Azalia Urdániz, Estefanía Piuri, Mariana Miranda, Kildare Wehenkel, Anne Marie Alzari, Pedro M. Malacrida, Leonel Durán, Rosario Mycobacterium Cell Division Proteomics Electron Microscopy Mycobacterium tuberculosis División Celular Proteómica Microscopía Electrónica Mycobacteria, including pathogens like Mycobacterium tuberculosis, exhibit unique growth patterns and cell envelope structures that challenge our understanding of bacterial physiology. This study sheds light on FhaA, a conserved protein in Mycobacteriales, revealing its pivotal role in coordinating cell envelope biogenesis and asymmetric growth. The elucidation of the FhaA interactome in living mycobacterial cells reveals its participation in the protein network orchestrating cell envelope biogenesis and cell elongation/division. By manipulating FhaA levels, we uncovered its influence on cell morphology, cell envelope organization, and the localization of peptidoglycan biosynthesis machinery. Notably, fhaA deletion disrupted the characteristic asymmetric growth of mycobacteria, highlighting its importance in maintaining this distinctive feature. Our findings position FhaA as a key regulator in a complex protein network, orchestrating the asymmetric distribution and activity of cell envelope biosynthetic machinery. This work not only advances our understanding of mycobacterial growth mechanisms but also identifies FhaA as a potential target for future studies on cell envelope biogenesis and bacterial growth regulation. These insights into the fundamental biology of mycobacteria may pave the way for novel approaches to combat mycobacterial infections addressing the ongoing challenge of diseases like tuberculosis in global health. Instituto de Biotecnología Fil: Rossello, Jessica. Instituto de Investigaciones Biológicas Clemente Estable and Institut Pasteur de Montevideo. Analytical Biochemistry and Proteomics Unit; Uruguay Fil: Rossello, Jessica. Universidad de la República and Institut Pasteur de Montevideo. Advanced Bioimaging Unit; Uruguay Fil: Rivera, Bernardina. Instituto de Investigaciones Biológicas Clemente Estable and Institut Pasteur de Montevideo. Analytical Biochemistry and Proteomics Unit; Uruguay Fil: Anzibar Fialho, Maximiliano. Universidad de la República and Institut Pasteur de Montevideo. Advanced Bioimaging Unit; Uruguay Fil: Augusto, Ingrid. Federal University of Rio de Janeiro. Carlos Chagas Filho Institute of Biophysics and National Center for Structural Biology and Bioimaging. Precision Medicine Research Centre; Brasil Fil: Gil, Magdalena. Instituto de Investigaciones Biológicas Clemente Estable and Institut Pasteur de Montevideo. Analytical Biochemistry and Proteomics Unit; Uruguay Fil: Forrellad, Marina Andrea. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular (IABIMO); Argentina Fil: Forrellad, Marina Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Bigi, Fabiana. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular (IABIMO); Argentina Fil: Bigi, Fabiana. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Rodríguez Taño, Azalia. Instituto de Investigaciones Biológicas Clemente Estable and Institut Pasteur de Montevideo. Analytical Biochemistry and Proteomics Unit; Uruguay Fil: Rodríguez Taño, Azalia. Universidad de la República. Facultad de Química. Programa de Posgrado; Uruguay Fil: Urdániz, Estefanía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina Fil: Piuri, Mariana. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina Fil: Miranda, Kildare. Federal University of Rio de Janeiro. Carlos Chagas Filho Institute of Biophysics and National Center for Structural Biology and Bioimaging. Precision Medicine Research Centre; Brasil Fil: Wehenkel, Anne Marie. Université Paris Cité. Institut Pasteur. Bacterial Cell Cycle Mechanisms Unit; Francia Fil: Alzari, Pedro M. Université Paris Cité. Institut Pasteur. Structural Microbiology Unit; Francia Fil: Malacrida, Leonel. Universidad de la República and Institut Pasteur de Montevideo. Advanced Bioimaging Unit; Uruguay Fil: Malacrida, Leonel. Universidad de la República. Facultad de Medicina. Hospital de Clínicas. Departamento de Fisiopatología; Uruguay Fil: Durán, Rosario. Instituto de Investigaciones Biológicas Clemente Estable and Institut Pasteur de Montevideo. Analytical Biochemistry and Proteomics Unit; Uruguay 2025-03-26T10:16:32Z 2025-03-26T10:16:32Z 2025-03 info:ar-repo/semantics/artículo info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://hdl.handle.net/20.500.12123/21814 https://journals.asm.org/doi/10.1128/mbio.02526-24 2161-2129 https://doi.org/10.1128/mbio.02526-24 eng info:eu-repo/semantics/openAccess 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 American Society for Microbiology mBio 16 (3) : e02526-24 (March 2025) |
| spellingShingle | Mycobacterium Cell Division Proteomics Electron Microscopy Mycobacterium tuberculosis División Celular Proteómica Microscopía Electrónica Rossello, Jessica Rivera, Bernardina Anzibar Fialho, Maximiliano Augusto, Ingrid Gil, Magdalena Forrellad, Marina Andrea Bigi, Fabiana Rodríguez Taño, Azalia Urdániz, Estefanía Piuri, Mariana Miranda, Kildare Wehenkel, Anne Marie Alzari, Pedro M. Malacrida, Leonel Durán, Rosario FhaA plays a key role in mycobacterial polar elongation and asymmetric growth |
| title | FhaA plays a key role in mycobacterial polar elongation and asymmetric growth |
| title_full | FhaA plays a key role in mycobacterial polar elongation and asymmetric growth |
| title_fullStr | FhaA plays a key role in mycobacterial polar elongation and asymmetric growth |
| title_full_unstemmed | FhaA plays a key role in mycobacterial polar elongation and asymmetric growth |
| title_short | FhaA plays a key role in mycobacterial polar elongation and asymmetric growth |
| title_sort | fhaa plays a key role in mycobacterial polar elongation and asymmetric growth |
| topic | Mycobacterium Cell Division Proteomics Electron Microscopy Mycobacterium tuberculosis División Celular Proteómica Microscopía Electrónica |
| url | http://hdl.handle.net/20.500.12123/21814 https://journals.asm.org/doi/10.1128/mbio.02526-24 https://doi.org/10.1128/mbio.02526-24 |
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