Moesin binds to bacterial lipopolysaccharide

الملخص EN

Previous work has demonstrated a role for moesin (member of the ERM family proteins) in lipopolysaccharide mediated events; however, no physical binding to lipopolysaccharide has been reported.

Therefore, the aim of this experiment was to study the binding of moesin to lipopolysaccharide.

Moesin and radixin recombinant proteins, C- and Nterminus truncated proteins were used.

Native gel shift assays were performed using the recombinant proteins and purified E.

coli lipopolysaccharide strain O55:B5.

The results of the native Gel Shift assay showed that there was direct binding of moesin to lipopolysaccharide.

This binding was only evident with the moesin C-terminus recombinant protein.

This finding suggests further the important role of moesin in the initial recognition of lipopolysaccharide.