Topologically-guided continuous protein crystallization controls bacterial surface layer self-assembly

Colin J. Comerci, Jonathan Herrmann, Joshua Yoon, Fatemeh Jabbarpour, Xiaofeng Zhou, John F. Nomellini, John Smit, Lucy Shapiro, Soichi Wakatsuki () and W. E. Moerner ()
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Colin J. Comerci: Stanford University
Jonathan Herrmann: Stanford University
Joshua Yoon: Stanford University
Fatemeh Jabbarpour: Stanford University
Xiaofeng Zhou: Stanford University
John F. Nomellini: University of British Columbia
John Smit: University of British Columbia
Lucy Shapiro: Stanford University
Soichi Wakatsuki: Stanford University
W. E. Moerner: Stanford University

Nature Communications, 2019, vol. 10, issue 1, 1-10

Abstract: Abstract Many bacteria and most archaea possess a crystalline protein surface layer (S-layer), which surrounds their growing and topologically complicated outer surface. Constructing a macromolecular structure of this scale generally requires localized enzymatic machinery, but a regulatory framework for S-layer assembly has not been identified. By labeling, superresolution imaging, and tracking the S-layer protein (SLP) from C. crescentus, we show that 2D protein self-assembly is sufficient to build and maintain the S-layer in living cells by efficient protein crystal nucleation and growth. We propose a model supported by single-molecule tracking whereby randomly secreted SLP monomers diffuse on the lipopolysaccharide (LPS) outer membrane until incorporated at the edges of growing 2D S-layer crystals. Surface topology creates crystal defects and boundaries, thereby guiding S-layer assembly. Unsupervised assembly poses challenges for therapeutics targeting S-layers. However, protein crystallization as an evolutionary driver rationalizes S-layer diversity and raises the potential for biologically inspired self-assembling macromolecular nanomaterials.

Date: 2019
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DOI: 10.1038/s41467-019-10650-x

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