An extensive disulfide bond network prevents tail contraction in Agrobacterium tumefaciens phage Milano

dc.contributor.authorSonani, Ravi R.en
dc.contributor.authorPalmer, Lee K.en
dc.contributor.authorEsteves, Nathaniel C.en
dc.contributor.authorHorton, Abigail A.en
dc.contributor.authorSebastian, Amanda L.en
dc.contributor.authorKelly, Rebecca J.en
dc.contributor.authorWang, Fengbinen
dc.contributor.authorKreutzberger, Mark A. B.en
dc.contributor.authorRussell, William K.en
dc.contributor.authorLeiman, Petr G.en
dc.contributor.authorScharf, Birgit E.en
dc.contributor.authorEgelman, Edward H.en
dc.date.accessioned2024-02-01T14:11:08Zen
dc.date.available2024-02-01T14:11:08Zen
dc.date.issued2024-01-26en
dc.description.abstractA contractile sheath and rigid tube assembly is a widespread apparatus used by bacteriophages, tailocins, and the bacterial type VI secretion system to penetrate cell membranes. In this mechanism, contraction of an external sheath powers the motion of an inner tube through the membrane. The structure, energetics, and mechanism of the machinery imply rigidity and straightness. The contractile tail of Agrobacterium tumefaciens bacteriophage Milano is flexible and bent to varying degrees, which sets it apart from other contractile tail-like systems. Here, we report structures of the Milano tail including the sheath-tube complex, baseplate, and putative receptor-binding proteins. The flexible-to-rigid transformation of the Milano tail upon contraction can be explained by unique electrostatic properties of the tail tube and sheath. All components of the Milano tail, including sheath subunits, are crosslinked by disulfides, some of which must be reduced for contraction to occur. The putative receptor-binding complex of Milano contains a tailspike, a tail fiber, and at least two small proteins that form a garland around the distal ends of the tailspikes and tail fibers. Despite being flagellotropic, Milano lacks thread-like tail filaments that can wrap around the flagellum, and is thus likely to employ a different binding mechanism.en
dc.description.versionPublished versionen
dc.format.mimetypeapplication/pdfen
dc.identifier756 (Article number)en
dc.identifier.doihttps://doi.org/10.1038/s41467-024-44959-zen
dc.identifier.eissn2041-1723en
dc.identifier.issn2041-1723en
dc.identifier.issue1en
dc.identifier.orcidScharf, Birgit [0000-0001-6271-8972]en
dc.identifier.other10.1038/s41467-024-44959-z (PII)en
dc.identifier.pmid38272938en
dc.identifier.urihttps://hdl.handle.net/10919/117782en
dc.identifier.volume15en
dc.language.isoenen
dc.publisherSpringeren
dc.relation.urihttps://www.ncbi.nlm.nih.gov/pubmed/38272938en
dc.rightsCreative Commons Attribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.titleAn extensive disulfide bond network prevents tail contraction in Agrobacterium tumefaciens phage Milanoen
dc.title.serialNature Communicationsen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten
dc.type.otherJournal Articleen
dcterms.dateAccepted2024-01-10en
pubs.organisational-group/Virginia Techen
pubs.organisational-group/Virginia Tech/Scienceen
pubs.organisational-group/Virginia Tech/Science/Biological Sciencesen
pubs.organisational-group/Virginia Tech/Faculty of Health Sciencesen
pubs.organisational-group/Virginia Tech/All T&R Facultyen
pubs.organisational-group/Virginia Tech/Science/COS T&R Facultyen

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