| Publikationstyp: | Beitrag in wissenschaftlicher Zeitschrift |
| Art der Begutachtung: | Peer review (Publikation) |
| Titel: | The tail-associated depolymerase of Erwinia amylovoraphage L1 mediates host cell adsorption and enzymatic capsule removal, which can enhance infection by other phage |
| Autor/-in: | Born, Yannick Fieseler, Lars Klumpp, Jochen Eugster, Marcel R. Zurfluh, Katrin Duffy, Brion Loessner, Martin J. |
| DOI: | 10.1111/1462-2920.12212 |
| Erschienen in: | Environmental Microbiology |
| Band(Heft): | 16 |
| Heft: | 7 |
| Seite(n): | 2168 |
| Seiten bis: | 2180 |
| Erscheinungsdatum: | 2014 |
| Verlag / Hrsg. Institution: | Wiley |
| ISSN: | 1462-2912 1462-2920 |
| Sprache: | Englisch |
| Schlagwörter: | Bacterial adhesion; Erwinia amylovora; Escherichia coli; Host Specificity; Hydrogen-Ion concentration; Hydrolysis; Kinetics; Podoviridae; Bacterial polysaccharides; Tertiary protein structure; Recombinant proteins; Rosaceae; Viral proteins; Virion; Biological control agents |
| Fachgebiet (DDC): | 570: Biologie |
| Zusammenfassung: | The depolymerase enzyme (DpoL1) encoded by the T7-like phage L1 efficiently degrades amylovoran, an important virulence factor and major component of the extracellular polysaccharide (EPS) of its host, the plant pathogen Erwinia amylovora. Mass spectrometry analysis of hydrolysed EPS revealed that DpoL1 cleaves the galactose-containing backbone of amylovoran. The enzyme is most active at pH 6 and 50°C, and features a modular architecture. Removal of 180 N-terminal amino acids was shown not to affect enzyme activity. The C-terminus harbours the hydrolase activity, while the N-terminal domain links the enzyme to the phage particle. Electron microscopy demonstrated that DpoL1-specific antibodies cross-link phage particles at their tails, either lateral or frontal, and immunogold staining confirmed that DpoL1 is located at the tail spikes. Exposure of high-level EPS-producing Er. amylovora strain CFBP1430 to recombinant DpoL1 dramatically increased sensitivity to the Dpo-negative phage Y2, which was not the case for EPS-negative mutants or low-level EPS-producing Er. amylovora. Our findings indicate that enhanced phage susceptibility is based on enzymatic removal of the EPS capsule, normally a physical barrier to Y2 infection, and that use of DpoL1 together with the broad host range, virulent phage Y2 represents an attractive combination for biocontrol of fire blight. |
| URI: | https://digitalcollection.zhaw.ch/handle/11475/12267 |
| Volltext Version: | Publizierte Version |
| Lizenz (gemäss Verlagsvertrag): | Lizenz gemäss Verlagsvertrag |
| Departement: | Life Sciences und Facility Management |
| Organisationseinheit: | Institut für Lebensmittel- und Getränkeinnovation (ILGI) |
| Enthalten in den Sammlungen: | Publikationen Life Sciences und Facility Management |
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Born, Y., Fieseler, L., Klumpp, J., Eugster, M. R., Zurfluh, K., Duffy, B., & Loessner, M. J. (2014). The tail-associated depolymerase of Erwinia amylovoraphage L1 mediates host cell adsorption and enzymatic capsule removal, which can enhance infection by other phage. Environmental Microbiology, 16(7), 2168–2180. https://doi.org/10.1111/1462-2920.12212
Born, Y. et al. (2014) ‘The tail-associated depolymerase of Erwinia amylovoraphage L1 mediates host cell adsorption and enzymatic capsule removal, which can enhance infection by other phage’, Environmental Microbiology, 16(7), pp. 2168–2180. Available at: https://doi.org/10.1111/1462-2920.12212.
Y. Born et al., “The tail-associated depolymerase of Erwinia amylovoraphage L1 mediates host cell adsorption and enzymatic capsule removal, which can enhance infection by other phage,” Environmental Microbiology, vol. 16, no. 7, pp. 2168–2180, 2014, doi: 10.1111/1462-2920.12212.
BORN, Yannick, Lars FIESELER, Jochen KLUMPP, Marcel R. EUGSTER, Katrin ZURFLUH, Brion DUFFY und Martin J. LOESSNER, 2014. The tail-associated depolymerase of Erwinia amylovoraphage L1 mediates host cell adsorption and enzymatic capsule removal, which can enhance infection by other phage. Environmental Microbiology. 2014. Bd. 16, Nr. 7, S. 2168–2180. DOI 10.1111/1462-2920.12212
Born, Yannick, Lars Fieseler, Jochen Klumpp, Marcel R. Eugster, Katrin Zurfluh, Brion Duffy, and Martin J. Loessner. 2014. “The Tail-Associated Depolymerase of Erwinia Amylovoraphage L1 Mediates Host Cell Adsorption and Enzymatic Capsule Removal, Which Can Enhance Infection by Other Phage.” Environmental Microbiology 16 (7): 2168–80. https://doi.org/10.1111/1462-2920.12212.
Born, Yannick, et al. “The Tail-Associated Depolymerase of Erwinia Amylovoraphage L1 Mediates Host Cell Adsorption and Enzymatic Capsule Removal, Which Can Enhance Infection by Other Phage.” Environmental Microbiology, vol. 16, no. 7, 2014, pp. 2168–80, https://doi.org/10.1111/1462-2920.12212.
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