Summary The collectin surfactant protein D (SP‐D) is an important component of the pulmonary innate host defence. Up to now, little is known about the regulation of eosinophil function by SP‐D. Various murine models of pulmonary hypersensitivity suggest that SP‐D may be a potent anti‐allergic protein. We investigated the modulation of eosinophil chemotaxis and degranulation by human SP‐D. SP‐D markedly inhibited the chemotaxis of eosinophils triggered by eotaxin, a major tissue‐derived CC‐chemokine, as shown in a modified Boyden chamber assay. In addition, degranulation of ECP in response to Ca2+ ionophore, immobilized IgG and serum from allergic patients was inhibited by SP‐D. In a fixed‐cell enzyme linked immunosorbent assay and in flow cytometry, SP‐D bound to eosinophils. This binding was saturable and was inhibited by the addition of maltose and ethylenediaminetetraacetic acid, suggesting the involvement of the carbohydrate recognition domain of SP‐D. In addition, flow cytometry showed significant interaction of SP‐D with CD32 (FcγII receptor) on eosinophils, which might explain the inhibitory effect of SP‐D on the IgG and serum‐triggered eosinophil cationic protein degranulation of eosinophils. Our data further support the concept of an anti‐inflammatory function of SP‐D in the lung of patients with allergic diseases.