The β1,2-glucans produced by bacteria are important in invasion, survival and
immunomodulation in infected hosts be they mammals or plants. However, there has been a
lack of information on proteins which recognize these molecules. This is partly due to the
extremely limited availability of the sequence-defined oligosaccharides and derived probes
for use in the study of their interactions. Here we have used the cyclic β1,2-glucan (CβG) of
the bacterial pathogen Brucella abortus, after removal of succinyl side chains, to prepare
linearized oligosaccharides which were used to generate microarrays. We describe optimized
conditions for partial depolymerization of the cyclic glucan by acid hydrolysis and conversion
of the β1,2-gluco-oligosaccharides, with degrees of polymerization 2-13, to neoglycolipids for
the purpose of generating microarrays. By microarray analyses we show that the C-type lectin
receptor DC-SIGNR, like the closely related DC-SIGN we investigated earlier, binds to the
β1,2-gluco-oligosaccharides, as does the soluble immune effector serum mannose-binding
protein. Exploratory studies with DC-SIGN are suggestive of the recognition also of the intact
CβG by this receptor. These findings open the way to unravelling mechanisms of
immunomodulation mediated by β1,2-glucans in mammalian systems.