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,
*
Department of Internal Medicine, University of Iowa, Iowa City, IA 52242;
Veteran Affairs Medical Center, Iowa City, IA 52246;
CpG ImmunoPharmaceuticals GmbH, Hilden, Germany; and
CpG ImmunoPharmaceuticals, Inc., Wellesly, MA 02481
The vertebrate immune system recognizes bacterial DNA based on the
presence of unmethylated CpG-dinucleotides in particular base contexts
("CpG motifs"). In contrast to mice, knowledge about CpG-mediated
effects on human B cells is poor. In the present study we identify and
determine an optimal human CpG motif. A phosphodiester oligonucleotide
containing this motif strongly stimulated CD86, CD40, CD54, and MHC
class II expression, IL-6 synthesis, and proliferation of primary human
B cells. These effects required internalization of the oligonucleotide
and endosomal maturation. The molecular mechanism of action of this CpG
motif was associated with the sustained induction of the NF-
B
p50/p65 heterodimer and of the transcription-factor complex AP-1.
Transcription-factor activation by CpG DNA was preceded by increased
phosphorylation of the stress kinases c-Jun N-terminal kinase and p38,
and of activating transcription factor-2. In contrast to CpG, signaling
through the B cell receptor led to activation of extracellular receptor
kinase and to phosphorylation of a different isoform of c-Jun
N-terminal kinase. These studies define the structure of a highly
active human CpG motif and characterize its molecular mechanism of
action in primary human B cells.
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