期刊
NATURE IMMUNOLOGY
卷 21, 期 7, 页码 756-+出版社
NATURE PORTFOLIO
DOI: 10.1038/s41590-020-0698-1
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资金
- National Institute of Allergy and Infectious Diseases [U19AI070235, R01 AI083315]
- NIH [R56AI118791, R01AI127644, R01AI132590]
- Austrian Science Fund [DK W1248, SFB F4609]
- Erwin Schrodinger Fellowship of the Austrian Science Fund [J3332-B21]
- American Thoracic Society
- NIEHS [5T32ES007141]
- Austrian National Bank [17600]
- Operational Programme Research, Development and Education, the Call International Mobility of Researchers -MSCA - IF [CZ.02.2.69/0.0/0.0/17_050/0008014]
- Canadian Institutes of Health Research [DC0190GP]
The molecular basis for the propensity of a small number of environmental proteins to provoke allergic responses is largely unknown. Herein, we report that mite group 13 allergens of the fatty acid-binding protein (FABP) family are sensed by an evolutionarily conserved acute-phase protein, serum amyloid A1 (SAA1), that promotes pulmonary type 2 immunity. Mechanistically, SAA1 interacted directly with allergenic mite FABPs (Der p 13 and Blo t 13). The interaction between mite FABPs and SAA1 activated the SAA1-binding receptor, formyl peptide receptor 2 (FPR2), which drove the epithelial release of the type-2-promoting cytokine interleukin (IL)-33 in a SAA1-dependent manner. Importantly, the SAA1-FPR2-IL-33 axis was upregulated in nasal epithelial cells from patients with chronic rhinosinusitis. These findings identify an unrecognized role for SAA1 as a soluble pattern recognition receptor for conserved FABPs found in common mite allergens that initiate type 2 immunity at mucosal surfaces.
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