Molecular architecture of native fibronectin fibrils

Susanna Maria Früh, Ingmar Schoen (), Jonas Ries and Viola Vogel ()
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Susanna Maria Früh: Laboratory of Applied Mechanobiology, ETH Zurich
Ingmar Schoen: Laboratory of Applied Mechanobiology, ETH Zurich
Jonas Ries: European Molecular Biology Laboratory, Cell Biology and Biophysics Unit
Viola Vogel: Laboratory of Applied Mechanobiology, ETH Zurich

Nature Communications, 2015, vol. 6, issue 1, 1-10

Abstract: Abstract Fibronectin fibrils within the extracellular matrix play central roles in physiological and pathological processes, yet many structural details about their hierarchical and molecular assembly remain unknown. Here we combine site-specific protein labelling with single-molecule localization by stepwise photobleaching or direct stochastic optical reconstruction microscopy (dSTORM), and determine the relative positions of various labelled sites within native matrix fibrils. Single end-labelled fibronectin molecules in fibrils display an average end-to-end distance of ∼133 nm. Sampling of site-specific antibody epitopes along the thinnest fibrils (protofibrils) shows periodic punctate label patterns with ∼95 nm repeats and alternating N- and C-terminal regions. These measurements suggest an antiparallel 30–40 nm overlap between N-termini, suggesting that the first five type I modules bind type III modules of the adjacent molecule. Thicker fibres show random bundling of protofibrils without a well-defined line-up. This super-resolution microscopy approach can be applied to other fibrillar protein assemblies of unknown structure.

Date: 2015
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DOI: 10.1038/ncomms8275

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