Abstract
Acinetobacter baumannii infections are associated with high mortality rates and an even higher prevalence of antimicrobial resistance. Understanding the lectin-glycan interactions mediating A. baumannii adhesion to cells will facilitate their exploitation in strategies to develop improved approaches to diagnosis and treatment. In this work, we use an established low-cost glycan-based agglutination assay to undertake a systematic structure-activity relationship screen of glycan ligands, and identify selective adhesion to α-GalNAc that is dependent upon both stereochemistry and presentation. Our work demonstrates how this approach can rapidly identify glycan motifs important to adhesion of understudied pathogens such as A. baumannii, information that is both therapeutically exploitable and furthers understanding of bacterial virulence.