Presentation Title

Investigation into the effect of pVIII and pIII protein modifications during M13 bacteriophage transformation

Faculty Mentor

Elaine D. Haberer

Start Date

18-11-2017 10:00 AM

End Date

18-11-2017 11:00 AM

Location

BSC-Ursa Minor 89

Session

Poster 1

Type of Presentation

Poster

Subject Area

engineering_computer_science

Abstract

Since the discovery of phage display in the 1980s, the M13 bacteriophage has been used as a powerful tool for templating nano- to macro- scale hierarchical structures. The filamentous phage consists of a protein coat and a single stranded DNA loop. The viral capsid is composed of 2700 copies of the pVIII protein and is capped on one end by 5 copies of the pIII protein. Unlike most viruses, it is able to transform into several different shapes, giving a wide set of potential nanostructures. When M13 is exposed to chloroform, the nearly 1 µm filament contracts into a 50 nm spheroid. The addition of material-binding peptides to the viral protein coat may have an impact on the structure of the transformed phage. In this work, we observed the effects on the phage transformation due to modified pIII and/or pVIII for ZnS and Au mineralization, respectively. The transformation progress in the protein helicity and arrangement were monitored using transmission electron microscopy, fluorescence, and circular dichroism spectroscopy. It was shown that the pIII and pVIII modifications had a major impact on the rate of transformation and protein arrangement of the spheroids. Additionally, while the spheroidal shape was maintained across all samples, the insertion of binding peptides within multiple viral capsid proteins, caused the spheroidal size to increase. This study demonstrated that when modifying pIII and pVIII proteins, arrangement and structure should be taken into consideration for future templating work with different materials.

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Nov 18th, 10:00 AM Nov 18th, 11:00 AM

Investigation into the effect of pVIII and pIII protein modifications during M13 bacteriophage transformation

BSC-Ursa Minor 89

Since the discovery of phage display in the 1980s, the M13 bacteriophage has been used as a powerful tool for templating nano- to macro- scale hierarchical structures. The filamentous phage consists of a protein coat and a single stranded DNA loop. The viral capsid is composed of 2700 copies of the pVIII protein and is capped on one end by 5 copies of the pIII protein. Unlike most viruses, it is able to transform into several different shapes, giving a wide set of potential nanostructures. When M13 is exposed to chloroform, the nearly 1 µm filament contracts into a 50 nm spheroid. The addition of material-binding peptides to the viral protein coat may have an impact on the structure of the transformed phage. In this work, we observed the effects on the phage transformation due to modified pIII and/or pVIII for ZnS and Au mineralization, respectively. The transformation progress in the protein helicity and arrangement were monitored using transmission electron microscopy, fluorescence, and circular dichroism spectroscopy. It was shown that the pIII and pVIII modifications had a major impact on the rate of transformation and protein arrangement of the spheroids. Additionally, while the spheroidal shape was maintained across all samples, the insertion of binding peptides within multiple viral capsid proteins, caused the spheroidal size to increase. This study demonstrated that when modifying pIII and pVIII proteins, arrangement and structure should be taken into consideration for future templating work with different materials.