Uniform dimensions and genetic tractability make filamentous viruses attractive templates for the display of functional groups used in materials science, sensor applications, and vaccine development. However, active virus replication and recombination often limit the usefulness of these viruses for such applications. To circumvent these limitations, genetic modifications of selected negatively charged intersubunit carboxylate residues within the coat protein of tobacco mosaic virus (TMV) were neutralized so as to stabilize the assembly of rod-shaped virus-like particles (VLPs) within bacterial expression systems. Here we show that TMV-VLP nanorods are easily purified, stable, and can be programmed in a variety of configurations to display functional peptides for antibody and small molecule binding.