Yeast Surface Display of Antheraea pernyi Lysozyme Revealed α-Helical Antibacterial Peptides in Its N-Terminal Domain

The present study investigated a novel lysozyme ApLyz from the Chinese oak silkmoth, Antheraea pernyi, for its active expression with N- or C-terminus fused to the yeast cell surface, and the antimicrobial activities of the corresponding expressed lysozymes were evaluated. The bactericidal activity of C-terminal fusion of ApLyz surpassed that of the N-terminal fusion, which revealed the implication of an N-terminal stretch of ApLyz in the bactericidal function based on the structural mobility of this region. Two N-terminal peptides of ApLyz (residues 1–15 and 1–32), which primarily consist of amphiphilic α-helices, exerted similar bactericidal efficacy and had a strong preference for the Gram-negative strains. Further investigation revealed that the N-terminal peptides are membrane-targeting peptides causing cell permeabilization and also possess nonmembrane disturbing bactericidal mechanism. Overall, in addition to the key findings of novel bactericidal peptides from silkmoth lysozyme, this work laid the...