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Viruses 2014, 6(7), 2708-2722; doi:10.3390/v6072708

The Role of the Coat Protein A-Domain in P22 Bacteriophage Maturation

Jr. *
Department of Microbiology, University of Alabama at Birmingham, 845 19th Street S, BBRB 414, Birmingham, AL 35294, USA
* Author to whom correspondence should be addressed.
Received: 29 May 2014 / Revised: 26 June 2014 / Accepted: 1 July 2014 / Published: 14 July 2014
(This article belongs to the Special Issue Virus Maturation)
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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.
Keywords: procapsid; bacteriophage; maturation; recombineering procapsid; bacteriophage; maturation; recombineering
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Morris, D.S.; Prevelige, P.E., Jr. The Role of the Coat Protein A-Domain in P22 Bacteriophage Maturation. Viruses 2014, 6, 2708-2722.

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