Molecular basis for polysaccharide recognition and modulated ATP hydrolysis by the O antigen ABC transporter

Nicholas Spellmon, Artur Muszyński, Ireneusz Górniak, Jiri Vlach, David Hahn, Parastoo Azadi and Jochen Zimmer ()
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Nicholas Spellmon: University of Virginia School of Medicine
Artur Muszyński: University of Georgia
Ireneusz Górniak: University of Virginia School of Medicine
Jiri Vlach: University of Georgia
David Hahn: University of Georgia
Parastoo Azadi: University of Georgia
Jochen Zimmer: University of Virginia School of Medicine

Nature Communications, 2022, vol. 13, issue 1, 1-14

Abstract: Abstract O antigens are ubiquitous protective extensions of lipopolysaccharides in the extracellular leaflet of the Gram-negative outer membrane. Following biosynthesis in the cytosol, the lipid-linked polysaccharide is transported to the periplasm by the WzmWzt ABC transporter. Often, O antigen secretion requires the chemical modification of its elongating terminus, which the transporter recognizes via a carbohydrate-binding domain (CBD). Here, using components from A. aeolicus, we identify the O antigen structure with methylated mannose or rhamnose as its cap. Crystal and cryo electron microscopy structures reveal how WzmWzt recognizes this cap between its carbohydrate and nucleotide-binding domains in a nucleotide-free state. ATP binding induces drastic conformational changes of its CBD, terminating interactions with the O antigen. ATPase assays and site directed mutagenesis reveal reduced hydrolytic activity upon O antigen binding, likely to facilitate polymer loading into the ABC transporter. Our results elucidate critical steps in the recognition and translocation of polysaccharides by ABC transporters.

Date: 2022
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DOI: 10.1038/s41467-022-32597-2

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