Partial complementation of Sinorhizobium meliloti bacA mutant phenotypes by the Mycobacterium tuberculosis BacA protein
| Autor: | Bernhard Kerscher, Timothy J. Mitchell, Clifton E. Barry, I Mair, Andrea M. Mitchell, Gail P. Ferguson, Matteo Zanda, R McDonald, Marco Scocchi, Markus F. F. Arnold, Andreas F. Haag, Dominic J. Campopiano, Helena I. Boshoff, S Capewell, Peter Mergaert, Euan K. James |
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| Přispěvatelé: | Division of Infection and Immunity [University of Glasgow], School of Life Sciences [University of Glasgow], University of Glasgow-University of Glasgow, Institut des sciences du végétal (ISV), Centre National de la Recherche Scientifique (CNRS), M. F. F., Arnold, A. F., Haag, S., Capewell, H. I., Boshoff, E. K., Jame, R., Mcdonald, I., Mair, A. M., Mitchell, B., Kerscher, T. J., Mitchell, P., Mergaert, C. E., Barry, Scocchi, Marco, M., Zanda, D. J., Campopiano, G. P., Ferguson |
| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
BacA protein
beta-Defensins MESH: Mycobacterium tuberculosis Antimicrobial peptides Mutant MESH: Anti-Infective Agents ATP-binding cassette transporter Biology Microbiology law.invention MESH: Membrane Transport Proteins Mycobacterium tuberculosis 03 medical and health sciences Anti-Infective Agents Bacterial Proteins law [SDV.BV]Life Sciences [q-bio]/Vegetal Biology Symbiosis legume peptide NCR Molecular Biology MESH: Bacterial Proteins 030304 developmental biology MESH: Medicago sativa 0303 health sciences Sinorhizobium meliloti MESH: Genetic Complementation Test MESH: Symbiosis 030306 microbiology Genetic Complementation Test Membrane Transport Proteins food and beverages Articles biology.organism_classification 3. Good health MESH: beta-Defensins Complementation Recombinant DNA nodulating symbiosi nodulating symbiosis MESH: Sinorhizobium meliloti Bacteria Medicago sativa |
| Zdroj: | Journal of Bacteriology Journal of Bacteriology, American Society for Microbiology, 2013, 195 (2), pp.389-98. ⟨10.1128/JB.01445-12⟩ Journal of bacteriology 195 (2013): 389–398. doi:10.1128/JB.01445-12 info:cnr-pdr/source/autori:Arnold, M. F. F.; Haag, A. F.; Capewell, S.; Boshoff, H. I.; James, E. K.; McDonald, R.; Mair, I.; Mitchell, A. M.; Kerscher, B.; Mitchell, T. J.; Mergaert, P.; Barry, C. E., III; Scocchi, M.; Zanda, M.; Campopiano, D. J.; Ferguson, G. P./titolo:Partial Complementation of Sinorhizobium meliloti bacA Mutant Phenotypes by the Mycobacterium tuberculosis BacA Protein/doi:10.1128%2FJB.01445-12/rivista:Journal of bacteriology (Print)/anno:2013/pagina_da:389/pagina_a:398/intervallo_pagine:389–398/volume:195 Arnold, M F F, Haag, A F, Capewell, S, Boshoff, H I, James, E K, McDonald, R, Mair, I, Mitchell, A M, Kerscher, B, Mitchell, T J, Mergaert, P, Barry, C E, Scocchi, M, Zanda, M, Campopiano, D J & Ferguson, G P 2013, ' Partial complementation of Sinorhizobium meliloti bacA mutant phenotypes by the Mycobacterium tuberculosis BacA protein ', Journal of Bacteriology, vol. 195, no. 2, pp. 389-98 . https://doi.org/10.1128/JB.01445-12 |
| ISSN: | 0021-9193 1098-5530 |
| DOI: | 10.1128/JB.01445-12⟩ |
| Popis: | The Sinorhizobium meliloti BacA ABC transporter protein plays an important role in its nodulating symbiosis with the legume alfalfa ( Medicago sativa ). The Mycobacterium tuberculosis BacA homolog was found to be important for the maintenance of chronic murine infections, yet its in vivo function is unknown. In the legume plant as well as in the mammalian host, bacteria encounter host antimicrobial peptides (AMPs). We found that the M. tuberculosis BacA protein was able to partially complement the symbiotic defect of an S. meliloti BacA-deficient mutant on alfalfa plants and to protect this mutant in vitro from the antimicrobial activity of a synthetic legume peptide, NCR247, and a recombinant human β-defensin 2 (HBD2). This finding was also confirmed using an M. tuberculosis insertion mutant. Furthermore, M. tuberculosis BacA-mediated protection of the legume symbiont S. meliloti against legume defensins as well as HBD2 is dependent on its attached ATPase domain. In addition, we show that M. tuberculosis BacA mediates peptide uptake of the truncated bovine AMP, Bac7 1-16 . This process required a functional ATPase domain. We therefore suggest that M. tuberculosis BacA is important for the transport of peptides across the cytoplasmic membrane and is part of a complete ABC transporter. Hence, BacA-mediated protection against host AMPs might be important for the maintenance of latent infections. |
| Databáze: | OpenAIRE |
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