Influenza A virus infects billions of people worldwide resulting in 500,000 deaths every year. Current vaccines target the receptor-binding domain (RBD) of the viral surface hemagglutinin (HA) protein. This region is antigenically dominant and is prone to mutations that leave current vaccines ineffective at neutralizing virus, thus requiring the design of new vaccines every year. Furthermore, antibodies generated to the RBD of HA from one strain of influenza typically lack the ability to cross-react with and neutralize infection by other strains of influenza A. We have designed a platform technology to elicit protective antibodies against class-1 viral fusion proteins in vivo. These antibodies target conserved regions of the viral HA protein that are involved in large conformation changes during the infection process. Therefore, any mutations in this region that may produce escape mutants are also likely to produce inactive viruses that are unable to infect host cells. Since this region is conserved across multiple strains of influenza, the antibodies derived from our immunogen exhibit enhanced cross-reactivity. Our platform technology consists of a synthetic two-stranded alpha-helical coiled-coil peptide template with Ile and Leu residues buried in the hydrophobic core a and d positions of the repeating heptad sequence (abcdefg)n to provide maximum stability to the coiled-coil structure. The resulting peptide immunogen is further stabilized with an interchain disulfide-bridge. An alpha-helical sequence from a native protein of interest is inserted into the template to expose the helical surface of the native protein (positions b, c, e, f and g). Antibodies to our lead peptide possess broad cross-reactivity among distant strains of influenza virus (Group1 H1, H2 and H5 and Group2 H3 and H7). Hence, this technology is a robust means of generating cross-reactive antibodies in vivo and should protect against any new pandemic strains.