INVESTIGADORES
BOCCACCIO Graciela Lidia
artículos
Título:
Multiple display of a protein domain on a bacterial polymeric protein
Autor/es:
CRAIG P,; BERGUER P,; AINCIART N,; ZYLBERMAN V,; MARTINEZ TOSAR L,; BULLOJ A,; THOMAS G,; BOCCACCIO G; GOLDBAUM F
Revista:
PROTEINS: STRUCTURE, FUNCTION AND GENETICS
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.