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Structural mechanisms of Tad pilus assembly and its interaction with an RNA virus.
- Source :
-
Science advances [Sci Adv] 2024 May 03; Vol. 10 (18), pp. eadl4450. Date of Electronic Publication: 2024 May 03. - Publication Year :
- 2024
-
Abstract
- Caulobacter crescentus Tad (tight adherence) pili, part of the type IV pili family, are crucial for mechanosensing, surface adherence, bacteriophage (phage) adsorption, and cell-cycle regulation. Unlike other type IV pilins, Tad pilins lack the typical globular β sheet domain responsible for pilus assembly and phage binding. The mechanisms of Tad pilus assembly and its interaction with phage ΦCb5 have been elusive. Using cryo-electron microscopy, we unveiled the Tad pilus assembly mechanism, featuring a unique network of hydrogen bonds at its core. We then identified the Tad pilus binding to the ΦCb5 maturation protein (Mat) through its β region. Notably, the amino terminus of ΦCb5 Mat is exposed outside the capsid and phage/pilus interface, enabling the attachment of fluorescent and affinity tags. These engineered ΦCb5 virions can be efficiently assembled and purified in Escherichia coli , maintaining infectivity against C. crescentus , which presents promising applications, including RNA delivery and phage display.
- Subjects :
- Cryoelectron Microscopy
Fimbriae Proteins
Escherichia coli
Viral Proteins chemistry
Viral Proteins metabolism
Caulobacter crescentus cytology
Caulobacter crescentus metabolism
Caulobacter crescentus virology
Fimbriae, Bacterial metabolism
Fimbriae, Bacterial ultrastructure
Bacteriophages chemistry
Bacteriophages metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 2375-2548
- Volume :
- 10
- Issue :
- 18
- Database :
- MEDLINE
- Journal :
- Science advances
- Publication Type :
- Academic Journal
- Accession number :
- 38701202
- Full Text :
- https://doi.org/10.1126/sciadv.adl4450