Cassava common mosaic virus (CsCMV) is the primary causal agent of cassava mosaic disease. Its capsid protein (CP) plays a crucial role in virus-plant interactions during infection. Glutaredoxins (GRXs) are low molecular weight thiol oxidoreductases, among which CC-type GRXs are key regulators of plant disease resistance. Given that CP is a key pathogenicity factor of CsCMV involved in modulating host immune responses, this study investigated whether CsCMV CP interacts with MeGRXC3 (a CC-type GRX) to synergistically regulate redox homeostasis and thereby modulate viral infection. Using yeast two-hybrid (Y2H), bimolecular fluorescence complementation (BiFC), and subcellular localization assays, the interaction between CsCMV CP and MeGRXC3 was examined. Y2H results confirmed their interaction in yeast cells. BiFC assays, performed by co-expressing the corresponding vectors in Nicotiana benthamiana epidermal cells, revealed distinct green fluorescent signals upon 488 nm excitation, indicating interaction in planta. Furthermore, subcellular localization analysis demonstrated co-localization of CsCMV CP with MeGRXC3 in tobacco epidermal cells upon co-expression, providing additional evidence for their interaction. Collectively, these results demonstrate that CsCMV CP interacts with MeGRXC3 in both yeast and plant cells. This finding lays the groundwork for further elucidating the molecular mechanisms by which CP facilitates CsCMV infection.