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A versatile nano display platform from bacterial spore coat proteins

Author

Listed:
  • I-Lin Wu

    (Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health)

  • Kedar Narayan

    (Laboratory of Cell Biology, National Cancer Institute, National Institutes of Health)

  • Jean-Philippe Castaing

    (Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health)

  • Fang Tian

    (College of Medicine, Pennsylvania State University)

  • Sriram Subramaniam

    (Laboratory of Cell Biology, National Cancer Institute, National Institutes of Health)

  • Kumaran S. Ramamurthi

    (Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health)

Abstract

Dormant bacterial spores are encased in a thick protein shell, the ‘coat’, which contains ∼70 different proteins. The coat protects the spore from environmental insults, and is among the most durable static structures in biology. Owing to extensive cross-linking among coat proteins, this structure has been recalcitrant to detailed biochemical analysis, so molecular details of how it assembles are largely unknown. Here, we reconstitute the basement layer of the coat atop spherical membranes supported by silica beads to create artificial spore-like particles. We report that these synthetic spore husk-encased lipid bilayers (SSHELs) assemble and polymerize into a static structure, mimicking in vivo basement layer assembly during sporulation in Bacillus subtilis. In addition, we demonstrate that SSHELs may be easily covalently modified with small molecules and proteins. We propose that SSHELs may be versatile display platforms for drugs and vaccines in clinical settings, or for enzymes that neutralize pollutants for environmental remediation.

Suggested Citation

  • I-Lin Wu & Kedar Narayan & Jean-Philippe Castaing & Fang Tian & Sriram Subramaniam & Kumaran S. Ramamurthi, 2015. "A versatile nano display platform from bacterial spore coat proteins," Nature Communications, Nature, vol. 6(1), pages 1-8, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms7777
    DOI: 10.1038/ncomms7777
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