Näytä suppeat kuvailutiedot

dc.contributor.authorKan, Sherry
dc.contributor.authorFornelos Martins, Nadine
dc.contributor.authorSchuch, Raymond
dc.contributor.authorFischetti, Vincent
dc.date.accessioned2016-02-09T07:05:58Z
dc.date.available2016-02-09T07:05:58Z
dc.date.issued2013
dc.identifier.citationKan, S., Fornelos Martins, N., Schuch, R., & Fischetti, V. (2013). Identification of a ligand on the Wip1 bacteriophage highly specific for a receptor on B. anthracis.. <i>Journal of Bacteriology</i>, <i>195</i>(19), 4355-64. <a href="https://doi.org/10.1128/JB.00655-13" target="_blank">https://doi.org/10.1128/JB.00655-13</a>
dc.identifier.otherCONVID_22539755
dc.identifier.otherTUTKAID_57460
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/48686
dc.description.abstractTectiviridae is a family of tailless bacteriophages with Gram-negative and Gram-positive hosts. The family model PRD1 and its close relatives all infect a broad range of enterobacteria by recognizing a plasmid-encoded conjugal transfer complex as a receptor. In contrast, tectiviruses with Gram-positive hosts are highly specific to only a few hosts within the same bacterial species. The cellular determinants that account for the observed specificity remain unknown. Here we present the genome sequence of Wip1, a tectivirus that infects the pathogen Bacillus anthracis. The Wip1 genome is related to other tectiviruses with Gram-positive hosts, notably, AP50, but displays some interesting differences in its genome organization. We identified Wip1 candidate genes for the viral spike complex, the structure located at the capsid vertices and involved in host receptor binding. Phage adsorption and inhibition tests were combined with immunofluorescence microscopy to show that the Wip1 gene product p23 is a receptor binding protein. His-p23 also formed a stable complex with p24, a Wip1 protein of unknown function, suggesting that the latter is involved with p23 in host cell recognition. The narrow host range of phage Wip1 and the identification of p23 as a receptor binding protein offer a new range of suitable tools for the rapid identification of B. anthracis.
dc.language.isoeng
dc.publisherAmerican Society for Microbiology
dc.relation.ispartofseriesJournal of Bacteriology
dc.relation.urihttp://jb.asm.org/content/early/2013/07/22/JB.00655-13.long
dc.subject.otherbacteriophage
dc.subject.othertectivirus
dc.subject.otherlysin
dc.titleIdentification of a ligand on the Wip1 bacteriophage highly specific for a receptor on B. anthracis.
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-201602051475
dc.contributor.laitosBio- ja ympäristötieteiden laitosfi
dc.contributor.laitosDepartment of Biological and Environmental Scienceen
dc.contributor.oppiaineSolu- ja molekyylibiologiafi
dc.contributor.oppiaineBiologisten vuorovaikutusten huippututkimusyksikköfi
dc.contributor.oppiaineCell and Molecular Biologyen
dc.contributor.oppiaineCentre of Excellence in Biological Interactions Researchen
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.date.updated2016-02-05T13:15:03Z
dc.type.coarhttp://purl.org/coar/resource_type/c_2df8fbb1
dc.description.reviewstatuspeerReviewed
dc.format.pagerange4355-64
dc.relation.issn0021-9193
dc.relation.numberinseries19
dc.relation.volume195
dc.type.versionpublishedVersion
dc.rights.copyright© 2013, American Society for Microbiology. Published in this repository with the kind permission of the publisher.
dc.rights.accesslevelopenAccessfi
dc.relation.doi10.1128/JB.00655-13
dc.type.okmA1


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