Fibrinogen αC-Domain derived from Group 1 Allergen of Dermatophagoides microceras modulates cell adhesion in human bronchial epithelial Cells

Transcriptomic analysis, including RNA sequencing (RNA-seq) and gene set enrichment analysis (GSEA), revealed that both Der m 1-derived FCPs and the αC domain induced similar transcriptional responses, particularly in pathways related to cell adhesion, extracellular matrix organization, and integrin signaling. Notably, integrin αV (ITGAV) was identified as a central regulatory hub, suggesting that Der m 1-derived FCPs influence cell adhesion through integrin-mediated mechanisms.

To explore this further, integrin-mediated adhesion was evaluated using Cilengitide, a cyclic RGD peptide that antagonizes αVβ3 and αVβ5 integrins. Co-treatment with Cilengitide significantly suppressed the pro-adhesive effects of both FCPs and αC domain, confirming an integrin αV-dependent mechanism. These findings reveal a novel interaction between the protease allergens of HDMs and host proteins.

Specifically, they demonstrated that Der m 1 not only cleaves fibrinogen but also generates bioactive fragments that regulate epithelial cell adhesion and signaling. This study sheds new light on the role of HDMs allergen-derived proteases in airway remodeling and allergic asthma pathogenesis, highlighting potential therapeutic opportunities targeting Der m 1 proteolytic activity and its bioactive cleavage products.