Backbone NMR assignment of Staphylococcus aureus DltC
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Methicillin-resistant Staphylococcus aureus (MRSA) remains a major cause of difficult-to-treat infections, due to cell-envelope remodeling pathways that reduce susceptibility to antibiotics and host defenses. One key pathway is D-alanylation of teichoic acids, mediated by the DltABCD system, which reduces the net negative charge of the cell wall and thereby contributes resistance to antimicrobial peptides and multiple antibiotic classes. Within this pathway, the adenylation enzyme DltA first activates D-alanine, which is then transferred to the carrier protein DltC via its 4’ -phosphopantetheine (Ppant) cofactor for subsequent transport from the cytosol to the cell surface. Here, we report the expression, purification, and backbone NMR resonance assignment of S. aureus DltC. The assignments provide a solution-state framework for probing DltC dynamics and for mapping its interfaces with binding partners, including DltA and DltB. Our work lays the groundwork for future structural and functional studies targeting the Dlt pathway as a route to new anti-staphylococcal therapeutics.
Abstract
Methicillin-resistant Staphylococcus aureus (MRSA) remains a major cause of difficult-to-treat infections, due to cell-envelope remodeling pathways that reduce susceptibility to antibiotics and host defenses. One key pathway is D-alanylation of teichoic acids, mediated by the DltABCD system, which reduces the net negative charge of the cell wall and thereby contributes resistance to antimicrobial peptides and multiple antibiotic classes. Within this pathway, the adenylation enzyme DltA first activates D-alanine, which is then transferred to the carrier protein DltC via its 4’ -phosphopantetheine (Ppant) cofactor for subsequent transport from the cytosol to the cell surface. Here, we report the expression, purification, and backbone NMR resonance assignment of S. aureus DltC. The assignments provide a solution-state framework for probing DltC dynamics and for mapping its interfaces with binding partners, including DltA and DltB. Our work lays the groundwork for future structural and functional studies targeting the Dlt pathway as a route to new anti-staphylococcal therapeutics.