Prediction of Regulatory Molecules for Enhancement of EGFR Overexpression Triggered by Signal Peptide of Ribonuclease 3

Abstract

Ribonuclease 3 (RNase3) is a member of the human RNaseA superfamily. It is led by a 27-residue signal peptide and secreted into body fluid to eliminate the infection of microbial pathogens in innate immune systems. The signal peptide of RNase3 (RNase3sp) not only directs protein secretion via endoplasmic reticulum (ER) and Golgi apparatus, but also its N-terminal 17 amino acid residues (RNase3sp1-17) induces the overexpression of epidermal growth factor receptor (EGFR). In this study, phage display technology was employed to screen the phage peptides which interacted with RNase3sp1-17. The peptide sequences were efficiently analyzed by proposed similarity search systems to retrieve potential candidates which possessed consensus residues conserved with the phage peptides. The retrieved potential candidates were subsequently input into the STRING database for discovering the interaction relationship among the candidates and EGFR. Finally, four potential RNase3sp1-17 interacting candidates, Notch1, GATA2, CBL, and RPX were selected, and the interaction network centered by Notch1 was generated. According to the interaction network and our 3 hypotheses, we attempt to solve the signaling pathway of EGFR overexpression triggered by RNase3sp1-17 by molecular biological experiments.

Characterizing the Role of Cell-Wall β-1,3-Exoglucanase Xog1p in Candida albicans Adhesion by the Human Antimicrobial Peptide LL-37

“…After three rounds of biopanning, sequencing templates were rapidly purified, and the sequences of selected LL-37-binding peptides were determined according to the manufacturer's instructions (New England BioLabs) and [66] . Twenty isolated blue plaques were transferred to E. coli ER2738 cultures (1 ml each).…”