Discrete fracture patterns of virus shells reveal mechanical building blocks.

Abstract:

:Viral shells are self-assembled protein nanocontainers with remarkable material properties. They combine simplicity of construction with toughness and complex functionality. These properties make them interesting for bionanotechnology. To date we know little about how virus structure determines assembly pathways and shell mechanics. We have here used atomic force microscopy to study structural failure of the shells of the bacteriophage Φ29. We observed rigidity patterns following the symmetry of the capsid proteins. Under prolonged force exertion, we observed fracture along well-defined lines of the 2D crystal lattice. The mechanically most stable building block of the shells was a trimer. Our approach of "reverse engineering" the virus shells thus made it possible to identify stable structural intermediates. Such stable intermediates point to a hierarchy of interactions among equal building blocks correlated with distinct next-neighbor interactions. The results also demonstrate that concepts from macroscopic materials science, such as fracture, can be usefully employed in molecular engineering.

authors

Ivanovska IL,Miranda R,Carrascosa JL,Wuite GJ,Schmidt CF

doi

10.1073/pnas.1105586108

subject

Has Abstract

pub_date

2011-08-02 00:00:00

pages

12611-6

issue

31

eissn

0027-8424

issn

1091-6490

pii

1105586108

journal_volume

108

pub_type

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