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The RNA as a molecular chaperone (chaperna) activity is intrinsic to some ribozymes and is operational during viral infections. Our purpose was to test whether influenza hemagglutinin (HA) can be assembled in a soluble, trimeric, and immunologically activating conformation by means of an RNA molecular chaperone (chaperna) activity. An RNA\u2010interacting domain (RID) from the host being immunized was selected as a docking tag for RNA binding, which served as a transducer for the chaperna function for\n                    <jats:italic>de novo<\/jats:italic>\n                    folding and trimeric assembly of RID\u2010HA1. Mutations that affect tRNA binding greatly increased the soluble aggregation defective in trimer assembly, suggesting that RNA interaction critically controls the kinetic network in the folding\/assembly pathway. Immunization of mice resulted in strong hemagglutination inhibition and high titers of a neutralizing antibody, providing sterile protection against a lethal challenge and confirming the immunologically relevant HA conformation. The results may be translated into a rapid response to a new influenza pandemic. The harnessing of the novel chaperna described herein with immunologically tailored antigen\u2010folding functions should serve as a robust prophylactic and diagnostic tool for viral infections.\u2014Yang, S. W., Jang, Y. H, Kwon, S. B., Lee, Y. J., Chae, W., Byun, Y. H., Kim, P., Park, C., Lee, Y J., Kim, C. K, Kim, Y. S., Choi, S. I., Seong, B. L. Harnessing an RNA\u2010mediated chaperone for the assembly of influenza hemagglutinin in an immunologically relevant conformation. 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