Expression of the receptor for IgM (FcμR) by bovine neutrophils

Bovine neutrophils possess a particular set of receptors for immunoglobulins. They have been shown to express a distinctive receptor for IgG₂, and it has long been known that they interact poorly with IgG₁ but that they can use IgM antibodies as opsonins. We show that the binding of labeled IgM was inhibited by unlabeled IgM but not by IgA, suggesting that bovine neutrophils express a specific IgM receptor. The binding of non-aggregated IgM is strong at 4 °C, but shedding occurs at 37 °C. We designed anti-peptide antibodies based on the sequence of the FcμR, the newly described receptor for IgM. These antibodies bound to bovine neutrophils at 4 °C. At 37 °C, labeling was lost, but the loss was inhibited by pretreatment with cytochalasin D, indicating internalization of the receptor after cross-linking by antibodies. Neutrophils that had internalized the receptor were no longer able to bind IgM. Eosinophils showed a low level of FcμR expression. FcμR expression by neutrophils was not increased by stimulation with Toll-like receptor agonists or the complement anaphylatoxin C5a, and decreased by TNF-α. Exposure of neutrophils to IFN-γ for 18 h increased FcμR expression without augmenting the binding of IgG₁ or IgG₂. We confirmed that bovine neutrophils can use IgM to phagocytose and kill bacteria without the help of Complement. Neutrophils that have migrated into the lumen of inflamed lactating mammary glands expressed the FcμR. These results indicate that bovine neutrophils express an IgM receptor, the FcμR, which is functional to contribute to the opsonophagocytosis of bacteria at inflammatory sites. Expression of the FcμR by neutrophils gives IgM a particular importance for the immune defense in the bovine species.