A new topology of the HK97-like fold revealed in Bordetella bacteriophage by cryoEM at 3.5 Å resolution

Xing Zhang; Huatao Guo; Lei Jin; Elizabeth Czornyj; Asher Hodes; Wong H Hui; Angela W Nieh; Jeff F Miller; Z Hong Zhou

doi:10.7554/eLife.01299

eLife (Dec 2013)

A new topology of the HK97-like fold revealed in Bordetella bacteriophage by cryoEM at 3.5 Å resolution

Xing Zhang,
Huatao Guo,
Lei Jin,
Elizabeth Czornyj,
Asher Hodes,
Wong H Hui,
Angela W Nieh,
Jeff F Miller,
Z Hong Zhou

Affiliations

Xing Zhang: California NanoSystems Institute, University of California, Los Angeles, Los Angeles, United States
Huatao Guo: Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, United States
Lei Jin: Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, United States
Elizabeth Czornyj: Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, United States
Asher Hodes: Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, United States
Wong H Hui: California NanoSystems Institute, University of California, Los Angeles, Los Angeles, United States
Angela W Nieh: Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, United States
Jeff F Miller: California NanoSystems Institute, University of California, Los Angeles, Los Angeles, United States; Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, United States; Molecular Biology Institute, University of California, Los Angeles, Los Angeles, United States
Z Hong Zhou: California NanoSystems Institute, University of California, Los Angeles, Los Angeles, United States; Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, United States; Molecular Biology Institute, University of California, Los Angeles, Los Angeles, United States

DOI: https://doi.org/10.7554/eLife.01299
Journal volume & issue: Vol. 2

Abstract

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Bacteriophage BPP-1 infects and kills Bordetella species that cause whooping cough. Its diversity-generating retroelement (DGR) provides a naturally occurring phage-display system, but engineering efforts are hampered without atomic structures. Here, we report a cryo electron microscopy structure of the BPP-1 head at 3.5 Å resolution. Our atomic model shows two of the three protein folds representing major viral lineages: jellyroll for its cement protein (CP) and HK97-like (‘Johnson’) for its major capsid protein (MCP). Strikingly, the fold topology of MCP is permuted non-circularly from the Johnson fold topology previously seen in viral and cellular proteins. We illustrate that the new topology is likely the only feasible alternative of the old topology. β-sheet augmentation and electrostatic interactions contribute to the formation of non-covalent chainmail in BPP-1, unlike covalent inter-protein linkages of the HK97 chainmail. Despite these complex interactions, the termini of both CP and MCP are ideally positioned for DGR-based phage-display engineering.

Published in eLife

ISSN: 2050-084X (Online)
Publisher: eLife Sciences Publications Ltd
Country of publisher: United Kingdom
LCC subjects: Medicine; Science: Biology (General)
Website: https://elifesciences.org

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