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Structural mechanisms of Tad pilus assembly and its interaction with an RNA virus. | LitMetric

Structural mechanisms of Tad pilus assembly and its interaction with an RNA virus.

Sci Adv

Center for Phage Technology, Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA.

Published: May 2024

AI Article Synopsis

  • - Tad pili, known for their role in mechanosensing and adherence, are distinct from other type IV pili due to their lack of a globular β sheet domain, making their assembly and interaction with phages like ΦCb5 complex and poorly understood.
  • - Researchers used cryo-electron microscopy to reveal that the Tad pilus assembly relies on a unique network of hydrogen bonds and identified its interaction with the ΦCb5 maturation protein (Mat) via specific binding to the β region.
  • - The study demonstrates that engineered ΦCb5 virions can be efficiently assembled and purified while retaining their infectivity, highlighting potential uses in RNA delivery and phage display technology.

Article Abstract

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 , maintaining infectivity against , which presents promising applications, including RNA delivery and phage display.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11067988PMC
http://dx.doi.org/10.1126/sciadv.adl4450DOI Listing

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