1. ZHAW digitalcollection
  2. Life Sciences und Facility Management
  3. Publikationen
  4. Publikationen Life Sciences und Facility Management
Full metadata record
DC FieldValueLanguage
dc.contributor.authorBorn, Yannick-
dc.contributor.authorFieseler, Lars-
dc.contributor.authorKlumpp, Jochen-
dc.contributor.authorEugster, Marcel R.-
dc.contributor.authorZurfluh, Katrin-
dc.contributor.authorDuffy, Brion-
dc.contributor.authorLoessner, Martin J.-
dc.date.accessioned2018-10-29T14:38:26Z-
dc.date.available2018-10-29T14:38:26Z-
dc.date.issued2014-
dc.identifier.issn1462-2912de_CH
dc.identifier.issn1462-2920de_CH
dc.identifier.urihttps://digitalcollection.zhaw.ch/handle/11475/12267-
dc.description.abstractThe 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.de_CH
dc.language.isoende_CH
dc.publisherWileyde_CH
dc.relation.ispartofEnvironmental Microbiologyde_CH
dc.rightsLicence according to publishing contractde_CH
dc.subjectBacterial adhesionde_CH
dc.subjectErwinia amylovorade_CH
dc.subjectEscherichia colide_CH
dc.subjectHost Specificityde_CH
dc.subjectHydrogen-Ion concentrationde_CH
dc.subjectHydrolysisde_CH
dc.subjectKineticsde_CH
dc.subjectPodoviridaede_CH
dc.subjectBacterial polysaccharidesde_CH
dc.subjectTertiary protein structurede_CH
dc.subjectRecombinant proteinsde_CH
dc.subjectRosaceaede_CH
dc.subjectViral proteinsde_CH
dc.subjectVirionde_CH
dc.subjectBiological control agentsde_CH
dc.subject.ddc570: Biologiede_CH
dc.titleThe tail-associated depolymerase of Erwinia amylovoraphage L1 mediates host cell adsorption and enzymatic capsule removal, which can enhance infection by other phagede_CH
dc.typeBeitrag in wissenschaftlicher Zeitschriftde_CH
dcterms.typeTextde_CH
zhaw.departementLife Sciences und Facility Managementde_CH
zhaw.organisationalunitInstitut für Lebensmittel- und Getränkeinnovation (ILGI)de_CH
dc.identifier.doi10.1111/1462-2920.12212de_CH
dc.identifier.pmid23944160de_CH
zhaw.funding.euNode_CH
zhaw.issue7de_CH
zhaw.originated.zhawYesde_CH
zhaw.pages.end2180de_CH
zhaw.pages.start2168de_CH
zhaw.publication.statuspublishedVersionde_CH
zhaw.volume16de_CH
zhaw.publication.reviewPeer review (Publikation)de_CH
zhaw.webfeedMikrobiologiede_CH
Appears in collections:Publikationen Life Sciences und Facility Management

Files in This Item:
There are no files associated with this item.
Show simple item record
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.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.