Abstract
Cytokines can be functionally active across species barriers. Bovine IL-10 has an amino acid sequence identity with human IL-10 of 76.8%. Therefore, the aim of this study was to evaluate whether bovine IL-10 has immunomodulatory activities on human monocytes and dendritic cells. Peripheral blood monocytes were isolated from healthy donors, and used directly or allowed to differentiate to dendritic cells under the influence of IL-4 and GM-CSF. Recombinant bovine IL-10 inhibited TLR induced activation of monocytes, and dose-dependently inhibited LPS-induced activation of monocyte-derived DCs comparable to human IL-10. By using blocking antibodies to either bovine IL-10 or the human IL-10 receptor it was demonstrated that inhibition of monocyte activation by bovine IL-10 was dependent on binding of bovine IL-10 to the human IL-10R. These data demonstrate that bovine IL-10 potently inhibits the activation of human myeloid cells in response to TLR activation. Bovine IL-10 present in dairy products may thus potentially contribute to the prevention of necrotizing enterocolitis and allergy, enhance mucosal tolerance induction and decrease intestinal inflammation and may therefore be applicable in infant foods and in immunomodulatory diets.
Highlights
Dietary components are capable of modulating intestinal immune responses [1,2]
The results obtained with the IL-10 receptor (IL-10R) blocking antibody showed a similar inhibition as the results from the bovine IL-10 blocking antibody. These results clearly demonstrate that bovine IL-10 inhibits TLR induced cytokine production by human monocytes, through binding to the human IL-10R
The data presented here demonstrate that bovine IL-10 is able to modulate TLR induced cytokine production by human monocytes
Summary
Dietary components are capable of modulating intestinal immune responses [1,2]. Dairy products, including cow’s milk, are widely consumed in Western societies and contain a wide range of immunoprotective factors such as immunoglobulins, lactoferrin, anti-microbial enzymes and cytokines. Bovine IL-10 was found to have an amino acid sequence identity of 76.8% with human IL-10, indicating that bovine IL-10 may exert functional effects on human immune cells [3,4,5,6]. Functional cross species activity of cytokines has been reported for chicken IFN-c and turkey IL-2 [5,6], and both porcine IL-2 and human IL-2 were reported to enhance proliferation of human, bovine, porcine and murine cells in vitro [3]. Human IL-10 is functionally active on a mouse mast cell line, but mouse IL-10 was not functionally active on a human B cell line [7] Together these findings indicate that cytokines can be functionally active across species. The potential cross-species bioactivity of IL-10 depends mostly on the sequence identity of the IL-10 receptor (IL-10R) binding sites [4] and three dimensional structure of the proteins involved
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