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Updated: Apr 27, 2026

An Assay for Quantifying Protein-RNA Binding in Bacteria
Published on: June 12, 2019
The role of the coat protein A-domain in p22 bacteriophage maturation
David S Morris1, Peter E Prevelige2
1Department of Microbiology, University of Alabama at Birmingham, 845 19th Street S, BBRB 414, Birmingham, AL 35294, USA. davidsm@uab.edu.
Abstract:
Bacteriophage P22 has long been considered a hallmark model for virus assembly and maturation. Repurposing of P22 and other similar virus structures for nanotechnology and nanomedicine has reinvigorated the need to further understand the protein-protein interactions that allow for the assembly, as well as the conformational shifts required for maturation. In this work, gp5, the major coat structural protein of P22, has been manipulated in order to examine the mutational effects on procapsid stability and maturation. Insertions to the P22 coat protein A-domain, while widely permissive of procapsid assembly, destabilize the interactions necessary for virus maturation and potentially allow for the tunable adjustment of procapsid stability. Future manipulation of this region of the coat protein subunit can potentially be used to alter the stability of the capsid for controllable disassembly.
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