INVESTIGADORES
BERGUER Paula Mercedes
artículos
Título:
Multiple display of a protein domain on a bacterial polymeric scaffold.
Autor/es:
CRAIG PO, BERGUER PM, AINCIART N, ZYLBERMAN V, THOMAS MG, MARTINEZ TOSAR LJ, BULLOJ A, BOCCACCIO GL, GOLDBAUM FA
Revista:
PROTEINS: STRUCTURE, FUNCTION AND GENETICS
Editorial:
Wiley-Liss
Referencias:
Año: 2005 vol. 61 p. 1089 - 1100
ISSN:
0887-3585
Resumen:
The multiple display of protein domains on polymeric scaffolds is an
emerging technology for many applications. BLS is a highly immunogenic
protein that has an oligomeric structure formed by a 17.2 kDa subunit
arranged as a dimer of pentamers. Here we describe the production as
well as the structural, functional, and immunological properties of a 9
kDa double-stranded RNA-binding 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-antigen. Our results underscore the BLS
display strategy as a powerful tool for biotechnological and
therapeutic applications.