[논문]Der p 38 Is a Bidirectional Regulator of Eosinophils and Neutrophils in Allergy

Hong, Min Hwa; Kashif, Ayesha; Kim, Geunyeong; Park, Beom Seok; Lee, Na Rae; Yang, Eun Ju; Mun, Ji Young; Choi, Hyosun; Kim, Sang-Hoon; Kim, Hyun Jik; Lee, Soo Jin; Lee, Ji-Sook; Hong, Yujin; Kim, In Sik

doi:10.4049/jimmunol.2001144

[해외논문] Der p 38 Is a Bidirectional Regulator of Eosinophils and Neutrophils in Allergy 원문보기

The journal of immunology : official journal of the American Association of Immunologists, v.207 no.7, 2021년, pp.1735 - 1746

Hong, Min Hwa (Department of Senior Healthcare, Eulji University, Uijeongbu, Republic of Korea) , Kashif, Ayesha , Kim, Geunyeong (Department of Senior Healthcare, Eulji University, Uijeongbu, Republic of Korea) , Park, Beom Seok , Lee, Na Rae (Department of Senior Healthcare, Eulji University, Uijeongbu, Republic of Korea) , Yang, Eun Ju , Mun, Ji Young (Department of Senior Healthcare, Eulji University, Uijeongbu, Republic of Korea) , Choi, Hyosun , Kim, Sang-Hoon (Department of Biomedical Laboratory Science, College of Health Science, Eulji University, Uijeongbu, Republic of Korea) , Kim, Hyun Jik , Lee, Soo Jin (Department of Clinical Laboratory Science, Daegu Haany University, Gyeongsan, Republic of Korea) , Lee, Ji-Sook , Hong, Yujin (Neural Circuit Research Group, Korea Brain Research Institute, Daegu, Republic of Korea) , Kim, In Sik

Abstract ▼ AI-Helper

The house dust mite is the most common cause of allergic diseases, and TLR4 acts as an overarching receptor for allergic responses. This study aimed to identify novel allergen binding to TLR4 in house dust mites and unveil its unique role in allergic responses. Der p 38 was purified and characterized by liquid chromatography tandem mass spectrometry–based peptide mapping. Biolayer interferometry and structure modeling unveiled TLR4-binding activity and the structure of recombinant Der p 38. The allergenicity of Der p 38 was confirmed by a skin prick test, and basophil activation and dot blot assays. The skin prick test identified 24 out of 45 allergic subjects (53.3%) as Der p 38+ subjects. Der p 38–augmented CD203c expression was noted in the basophils of Der p 38+ allergic subjects. In animal experiments with wild-type and TLR4 knockout BALB/c mice, Der p 38 administration induced the infiltration of neutrophils as well as eosinophils and exhibited clinical features similar to asthma via TLR4 activation. Persistent Der p 38 administration induced severe neutrophil inflammation. Der p 38 directly suppressed the apoptosis of allergic neutrophils and eosinophils, and enhanced cytokine production in human bronchial epithelial cells, inhibiting neutrophil apoptosis. The mechanisms involved TLR4, LYN, PI3K, AKT, ERK, and NF-κB. These findings may contribute to a deep understanding of Der p 38 as a bridge allergen between eosinophilic and neutrophilic inflammation in the pathogenic mechanisms of allergy.Visual Abstract[Figure]Key PointsDer p 38 is a novel allergen binding to TLR4.Der p 38 drives mixed granulocyte asthma in the mouse model.Der p 38 induces antiapoptotic effects on leukocytes and cytokine secretion.

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