Tobacco　mosaic　virus　(TMV)　is　a　classical　viral　nanoarchitecture　that　has　been　extensively　employed　as　a　promising　template　for　the　fabrication　of　novel　nanomaterials　and　nanostructures.　Despite　being　an　ideal　source,　the　Escherichia　coli-derived　TMV　nanorod　is　suffering　from　tenuous　assembly　capability　and　stability.　Inspired　by　the　disulfide　bond　widely　employed　in　biosystems,　here　we　rationally　introduce　a　cysteine　into　TMV　coat　protein　(TMV-CP)　to　enable　disulfide　bond　formation　between　adjacent　subunits,　thereby　radically　altering　the　behaviors　of　original　noncovalent　assembling　system　of　wild　type　TMV-CP.　The　dramatically　enhanced　self-assembly　capability　and　stability　of　the　engineered　TMV　nanorods　are　observed　and　the　essential　roles　of　disulfide　bonds　are　verified,　illustrating　a　promising　strategy　to　obtain　desired　genetic-modified　nanorods　that　are　inaccessible　in　plants.　We　expect　this　work　will　benefit　the　development　of　TMV-based　nanotechnology　and　encourage　the　utilization　of　disulfide　bonds　in　other　biomacromolecules　for　improved　properties　as　nanoscaffolds.　©　2013　American　Chemical　Society.