Next Article in Journal
Increased Plasma Cell-Free DNA Level during HTNV Infection: Correlation with Disease Severity and Virus Load
Next Article in Special Issue
Bluetongue Virus Capsid Assembly and Maturation
Previous Article in Journal
Rabbit Hemorrhagic Disease Virus Detected in Pico, Azores, Portugal, Revealed a Unique Endemic Strain with More Than 17 Years of Independent Evolution
Article Menu

Export Article

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

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

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)
View Full-Text   |   Download PDF [2689 KB, uploaded 12 May 2015]   |  


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. View Full-Text
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).

Supplementary materials

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

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

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Viruses EISSN 1999-4915 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top