E-cadherin mediates adhesion of Aspergillus fumigatus to non-small cell lung cancer cells.

Abstract

A spergillus fumigatus is a widely distributed microorganism, and recently, A. fumigatus culture filtrate has been shown to trigger apoptotic cell death in several human cancer cell lines, including non-small lung cancer (NSCLC) cells, A549. Nevertheless, the molecular adhesion of A. fumigatus to these cancer cells to trigger cell death remains unknown. Here, we knocked down E-cadherin in A549 cells and examined its effects on A. fumigatus. The blastospores of A. fumigatus were incubated with the complete protein extracts from A549 cells, using an affinity purification procedure. Preliminary exploration of E-cadherin-interacting protein on the surface of Aspergillus fumigates was done by immunoprecipitation and mass spectrometry analysis. We found that the adhesion of the blastospores to A549 cells was significantly reduced by E-cadherin suppression in A549 cells, suggesting that E-cadherin of A549 cells may mediate the surface adhesion of A. fumigatus blastospore. Mass spectrometry (MS) analysis predicted two binding proteins for E-cadherin on A. fumigatus, AfA24A6.130c and XP_747789. Finally, the growth of E-cadherin-depleted A549 cells significantly increased by infection of A. fumigatus in vivo. Thus, our study suggests that E-cadherin mediates adhesion of A. fumigatus to NSCLC cells to trigger cell death and provides molecular evidence for the treatment of NSCLC with controlled A. fumigatus infection.