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Here we describe the production as well as the structural, functional, and immunological properties of a 9 kDa double\u2010stranded RNA\u2010binding domain (RBD3) fused to the structure of BLS. We demonstrate that the BLS and RBD3 modules are stably and independently folded in the structure of the chimera and form a decameric structure of 255 kDa as the native BLS oligomers. The polymeric display of RBD3 in the structure of BLS increases the dsRNA binding strength of this domain both in vitro and in vivo, and also enhances its immunogenicity to the point that it breaks the tolerance of mice to the RBD3 self\u2010antigen. Our results underscore the BLS display strategy as a powerful tool for biotechnological and therapeutic applications. Proteins 2005. \u00a9 2005 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/prot.20635","type":"journal-article","created":{"date-parts":[[2005,9,28]],"date-time":"2005-09-28T20:46:26Z","timestamp":1127940386000},"page":"1089-1100","source":"Crossref","is-referenced-by-count":23,"title":["Multiple display of a protein domain on a bacterial polymeric scaffold"],"prefix":"10.1002","volume":"61","author":[{"given":"P. O.","family":"Craig","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P. M.","family":"Berguer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"N.","family":"Ainciart","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"V.","family":"Zylberman","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M. 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