Purpose of review: Several advances have been made in characterization of the molecule that carries human neutrophil antigen (HNA)-2a, NB1 glycoprotein, the gene that encodes NB1 glycoprotein, CD177, and the role of antibodies to HNA-2a in transfusion reactions.

Recent findings: NB1 glycoprotein binds to the endothelial cell adhesion molecule, platelet endothelial cell adhesion molecule-1 (PECAM-1), and participates in neutrophil transmigration. The overexpression of neutrophil CD177 mRNA has become a useful, but nonspecific biomarker of myeloproliferative diseases, especially polycythemia vera. CD177 mRNA overexpression is also a biomarker of a subset of patients with essential thrombocythemia who are at increased risk of thromboembolic complications. In patients with myeloproliferative disorders CD177 mRNA overexpression is secondary to a gain-of-function mutation in JAK2, JAK2 V617F. NB1 glycoprotein is co-localized on neutrophil plasma membranes with proteinase 3 and a complex of NB1 glycoprotein and proteinase 3 may initiate the activation of neutrophils by antineutrophil cytoplasmic antibodies in patients with Wegener's granulomatosis. The inadvertent transfusion of antibodies to HNA-2a with blood components frequently causes pulmonary transfusion reactions.

Summary: The expression of CD177 is an important biomarker of myeloproliferative diseases, NB1 glycoprotein is a ligand for PECAM-1 and it may have a role in Wegener's granulomatosis, and antibodies to HNA-2a frequently cause pulmonary transfusion reactions.