A capsid is the protein coat surrounding a virus' genome that ensures its protection and transport. The capsid
of murine polyomavirus (muPy) consists of one major (VP1) and two minor (VP2/3) proteins, from which just
VP1 is sufficient to form the capsid when expressed recombinantly (1). From a material engineering point of
view, viral capsids are of interest because they present a paradigm for complex self-assembly on the
nanometer scale. Understanding and controlling these assembly dynamics will allow the construction of
nanoscale structures using a self-assembly process. The first step in this direction was the discovery that
capsids of several viruses can be reversibly disassembled into their building blocks and reassembled using
the same building blocks by simply changing the buffer conditions (2, 3). Such capsids already find
applications as targeted in vivo delivery vectors for genes, proteins or small molecular drugs (4, 5), as optical
probes for biomedical imaging and sensing purposes with unprecedented resolution and sensitivity and can
potentially be used as templates for nanoelectronics (6, 7).
Here we show the controlled incorporation of inorganic gold nanoparticles into the capsid shell of muPy. This
incorporation is mediated by covalent sulfide bonds between the capsid proteins cysteine residues and the
molecular gold. The number of incorporated gold particles can be controlled during the assembly process
and the capsids retain their ability to transduce cells. These particles provide new tools for tracking of viral
particles in cells, and simultaneously allow the delivery of genes packages in the hollow capsid.
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