Date of Completion

5-11-2013

Embargo Period

5-11-2013

Keywords

bacteriophage, virus assembly, protein folding, icosahedral

Major Advisor

Carolyn M. Teschke

Associate Advisor

Arlene Albert

Associate Advisor

Andrei Alexandrescu

Field of Study

Biochemistry

Degree

Doctor of Philosophy

Open Access

Campus Access

Abstract

Bacteriophage P22, which infects Salmonella enterica serovar Typhimurium, is a

paradigm for the assembly of tailed bacteriophage and Herpesviridae (Teschke

and Parent, 2010). For many dsDNA viruses, including bacteriophage P22,

chemically identical coat proteins occupy non-identical hexon and penton sites in

the icosahedron. This relies on coat protein plasticity, as the subunits must

undergo conformational switching during procapsid assembly and virion

maturation. Bacteriophage P22 coat protein shares a common HK97-like fold

with many dsDNA viruses, however it has an additional genetically inserted

domain. Capsids using the HK97-like fold range in size from ~24 nm to ~145 nm

in diameter (Bamford et al., 2005). The viruses that use this building block have

evolved specialized ways to manage folding, assembly, stabilization, and cell

infection. Biochemical, structural, and genetic studies on P22 coat protein

provide clues about the HK97-like fold, which likely represents the absolute most

abundant fold in the biosphere.

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