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Viruses 2017, 9(12), 384; doi:10.3390/v9120384

Cleavage and Structural Transitions during Maturation of Staphylococcus aureus Bacteriophage 80α and SaPI1 Capsids

1
Department of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294, USA
2
Protein Expression Laboratory, National Institute of Arthritis and Musculoskeletal and Skin Diseases, The National Institutes of Health, Bethesda, MD 20892, USA
3
Department of Microbiology and Immunology, Virginia Commonwealth University, Richmond, VA 23298, USA
4
Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306, USA
Current address: Laboratory of Molecular Biology, National Cancer Institute, The National Institutes of Health, Bethesda, MD 20892, USA.
Current address: U.S. Food and Drug Administration, Silver Spring, MD 20993, USA.
§
Current address: Direct Electron, LP, San Diego, CA 92128, USA.
*
Author to whom correspondence should be addressed.
Received: 17 November 2017 / Revised: 8 December 2017 / Accepted: 15 December 2017 / Published: 16 December 2017
(This article belongs to the Special Issue Advances in Structural Virology via Cryo-EM)
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Abstract

In the tailed bacteriophages, DNA is packaged into spherical procapsids, leading to expansion into angular, thin-walled mature capsids. In many cases, this maturation is accompanied by cleavage of the major capsid protein (CP) and other capsid-associated proteins, including the scaffolding protein (SP) that serves as a chaperone for the assembly process. Staphylococcus aureus bacteriophage 80α is capable of high frequency mobilization of mobile genetic elements called S. aureus pathogenicity islands (SaPIs), such as SaPI1. SaPI1 redirects the assembly pathway of 80α to form capsids that are smaller than those normally made by the phage alone. Both CP and SP of 80α are N-terminally processed by a host-encoded protease, Prp. We have analyzed phage mutants that express pre-cleaved or uncleavable versions of CP or SP, and show that the N-terminal sequence in SP is absolutely required for assembly, but does not need to be cleaved in order to produce viable capsids. Mutants with pre-cleaved or uncleavable CP display normal viability. We have used cryo-EM to solve the structures of mature capsids from an 80α mutant expressing uncleavable CP, and from wildtype SaPI1. Comparisons with structures of 80α and SaPI1 procapsids show that capsid maturation involves major conformational changes in CP, consistent with a release of the CP N-arm by SP. The hexamers reorganize during maturation to accommodate the different environments in the 80α and SaPI1 capsids. View Full-Text
Keywords: Caudovirales; virus assembly; capsid size determination; cryo-electron microscopy; Staphylococcus aureus pathogenicity islands; SaPI1 Caudovirales; virus assembly; capsid size determination; cryo-electron microscopy; Staphylococcus aureus pathogenicity islands; SaPI1
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MDPI and ACS Style

Kizziah, J.L.; Manning, K.A.; Dearborn, A.D.; Wall, E.A.; Klenow, L.; Hill, R.L.L.; Spilman, M.S.; Stagg, S.M.; Christie, G.E.; Dokland, T. Cleavage and Structural Transitions during Maturation of Staphylococcus aureus Bacteriophage 80α and SaPI1 Capsids. Viruses 2017, 9, 384.

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