The tail-associated depolymerase of Erwinia amylovoraphage L1 mediates host cell adsorption and enzymatic capsule removal, which can enhance infection by other phage

Born, Yannick; Fieseler, Lars; Klumpp, Jochen; Eugster, Marcel R.; Zurfluh, Katrin; Duffy, Brion; Loessner, Martin J.

doi:10.1111/1462-2920.12212

Publication type:	Article in scientific journal
Type of review:	Peer review (publication)
Title:	The tail-associated depolymerase of Erwinia amylovoraphage L1 mediates host cell adsorption and enzymatic capsule removal, which can enhance infection by other phage
Authors:	Born, Yannick Fieseler, Lars Klumpp, Jochen Eugster, Marcel R. Zurfluh, Katrin Duffy, Brion Loessner, Martin J.
DOI:	10.1111/1462-2920.12212
Published in:	Environmental Microbiology
Volume(Issue):	16
Issue:	7
Page(s):	2168
Pages to:	2180
Issue Date:	2014
Publisher / Ed. Institution:	Wiley
ISSN:	1462-2912 1462-2920
Language:	English
Subjects:	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
Subject (DDC):	570: Biology
Abstract:	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
Fulltext version:	Published version
License (according to publishing contract):	Licence according to publishing contract
Departement:	Life Sciences and Facility Management
Organisational Unit:	Institute of Food and Beverage Innovation (ILGI)
Appears in collections:	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.