INVESTIGADORES
BERGUER Paula Mercedes
artículos
Título:
A polymeric bacterial protein activates dendritic cells via TLR4.
Autor/es:
BERGUER PM, MUNDIÑANO J, PIAZZON I, GOLDBAUM FA.
Revista:
JOURNAL OF IMMUNOLOGY
Editorial:
American Association of Immunologists
Referencias:
Lugar: Baltimore; Año: 2006 vol. 176 p. 2366 - 2372
ISSN:
0022-1767
Resumen:
The enzyme lumazine synthase from Brucella spp. (BLS) is a highly
immunogenic protein that folds as a stable dimer of pentamers. It is
possible to insert foreign peptides and proteins at the 10 N terminus
of BLS without disrupting its general folding, and these chimeras are
very efficient to elicit systemic and oral immunity without adjuvants.
In this study, we show that BLS stimulates bone marrow dendritic cells
from mice in vitro to up-regulate the levels of costimulatory molecules
(CD40, CD80, and CD86) and major histocompatibility class II Ag.
Furthermore, the mRNA levels of several chemokines are increased, and
proinflammatory cytokine secretion is induced upon exposure to BLS. In
vivo, BLS increases the number of dendritic cells and their expression
of CD62L in the draining lymph node. All of the observed effects are
dependent on TLR4, and clearly independent of LPS contamination. The
described characteristics of BLS make this protein an excellent
candidate for vaccine development.