Lipomannan (LM), a glycophospholipid
found on the cell surface
of mycobacteria, involves the virulence and survival in host cells.
However, there is little to no information on how exactly mannan alignment,
including the number of mannose units and the branched motif of LM,
affects protein engagement during host–pathogen interactions.
In this study, we synthesized the exact substructures of the LM glycans
that consist of an α(1,6) mannan core, with and without the
complete α(1,2) mannose branching, and comparatively studied
their protein–carbohydrate interactions. The synthetic LM glycans
were equipped with a thiol linker for immobilizations on the surfaces
of microarrays. As per our findings, the presence of the branching
α(1,2) mannose on the LM glycans increases their binding toward
the dendritic cell-specific intercellular adhesion molecule-3 grabbing
non-integrin receptor. An increase in the number of mannose units
on the glycans also increases the binding with the mannose receptor.
Thus, the set of synthetic glycans can serve as a useful tool to study
the biological activities of LM and can provide a better understanding
of host–pathogen interactions.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.