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VanA-type resistance to glycopeptide antibiotics in clinical enterococci is regulated by the VanS A R A  two-component signal transduction system. The nature of the molecular ligand that is recognised by the VanS A  sensory component has not hitherto been identified. Here we employ purified, intact and active VanS A  membrane protein (henceforth referred to as VanS) in analytical ultracentrifugation experiments to study VanS oligomeric state and conformation in the absence and presence of vancomycin. A combination of sedimentation velocity and sedimentation equilibrium in the analytical ultracentrifuge (SEDFIT, SEDFIT-MSTAR and MULTISIG analysis) showed that VanS in the absence of the ligand is almost entirely monomeric (molar mass  M  = 45.7 kDa) in dilute aqueous solution with a trace amount of high molar mass material ( M  ~ 200 kDa). The sedimentation coefficient  s  suggests the monomer adopts an extended conformation in aqueous solution with an equivalent aspect ratio of ~(12 ± 2). In the presence of vancomycin over a 33% increase in the sedimentation coefficient is observed with the appearance of additional higher  s  components, demonstrating an interaction, an observation consistent with our circular dichroism measurements. The two possible causes of this increase in  s  – either a ligand induced dimerization and/or compaction of the monomer are considered.

Hydrodynamics of the VanA-type VanS histidine kinase: an extended solution conformation and first evidence for interactions with vancomycin