Influenza virus is a medically significant respiratory virus with recurring seasonal infections. As a segmented RNA virus, influenza is prone to antigenic drift and antigenic shift, which may render current vaccines or prospective antivirals ineffective. Several broad-spectrum antibodies have been discovered that target major entry, egress and structural antigens, such as hemagglutinin (HA), neuraminidase (NA) and M2, respectively; however, these remain prone to escape mutations. In this work, we developed a panel of bispecific antibodies (BsAbs) that target HA, NA and M2 ectodomain (M2e) to assess their binding and neutralising ability. Our panel consisted of combinations of leading antibodies such as FI6V3 (HA-stem targeting), FNI9 (NA targeting) and 14C2 (M2e targeting). To engineer the BsAbs, ScFv domains were linked to the Fc segment of a mAb via a flexible linker. This design allowed for successful dual-variable domain display and binding of multiple antigenic targets. However, size-exclusion profiles and SDS-PAGE demonstrated some aggregation and a subpopulation of cleaved heavy chain products likely missing the scFv region. Next, we demonstrated that FI6V3+FNI9 and FNI9+14C2 BsAbs provided comparable neutralisation levels to the parental mAbs against H1N1 virus. Interestingly, when assessed against H3N2 virus, these BsAbs provided a significant increase in neutralisation over the parental antibodies. Furthermore, FI6V3+FNI9 provided increased neutralisation of pseudotyped H5N1 virus compared to FI6V3 or FNI9 alone. We speculate that the synergistic neutralisation effects observed may be due to (i) increased valency due to aggregation, (ii) neutralisation of virus at different timepoints in the lifecycle or (iii) better accessibility to otherwise obscured epitopes. To address this, future experiments should optimise the bispecific design to alleviate aggregation. Together, these findings serve as proof-of-concept for the use of BsAbs as next-generation, broad spectrum immunotherapies for influenza.