Abstract Leukocyte recruitment in acute and chronic inflammation is characterized by sequential cell adhesion and activation events. E-, P- and L-selectins mediate initial leukocyte–endothelial-cell adhesion events required for this process. Each selectin recognizes related but distinct counter-receptors displayed by leukocytes and/or the endothelium. These counter-receptors correspond to specific glycoproteins whose ‘activity’ is enabled by carefully controlled post-translational modifications. Characterization of the glycans associated with E- and P-selectin counter-receptors, and of mice with targeted deletions of glycosyltransferase and sulfotransferase genes, disclose that neutrophil E- and/or P-selectin counter-receptor activities derive, minimally, from essential synthetic collaborations amongst polypeptide N-acetylgalactosaminyltransferase(s), a β- N-acetylglucosaminyltransferase that assembles core-2-type O-glycans, β-1,4-galactosyltransferase(s), protein tyrosine sulfotransferase(s), α-2,3-sialyltransferases, and a pair of α-1,3-fucosyltransferases.