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Review
. 2018 May 17;14(5):e1006971.
doi: 10.1371/journal.ppat.1006971. eCollection 2018 May.

Lessons from bacteriophages part 1: Deriving utility from protein structure, function, and evolution

Affiliations
Review

Lessons from bacteriophages part 1: Deriving utility from protein structure, function, and evolution

Kunica Asija et al. PLoS Pathog. .
No abstract available

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Conflict of interest statement

The authors have declared that no competing interests exist.

Figures

Fig 1
Fig 1
(A) Capsid structure of bacteriophage P22. The left side of panel A shows the mature P22 capsid. The pentons are highlighted in blue, and hexons are shown in gray. The asymmetric unit (seven subunits) of the capsid is represented in ribbon format in the center of the capsid. The asymmetric unit is magnified and shown on the right of the panel. (B) Ribbon diagrams of coat monomers of P22 (left) and HK97 (right). The A-domains, P-domains, E-loops, and N-arms have been highlighted in cyan, green, yellow, and red, respectively. The I-domain of P22 coat protein has been highlighted in coral. The arrows indicate the D-loop (purple) of the monomer of P22 (left) and the G-loop (purple) on the monomer of HK97 (right).
Fig 2
Fig 2. Phage use in vaccine design and delivery.
The left panel shows the use of a VLP to express an antigenic gene product on its capsid. The right panel shows an antigenic gene being cloned into the phage genome and its subsequent use as a DNA vaccine carrier. VLP, virus-like particle.

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