Cecropin A improves the antibacterial activity of hen egg white lysozyme against challenging Salmonella enterica serovars

Hani A. Alhadrami, Ahmed M. Sayed, Hossam M. Hassan, Mostafa E. Rateb*, Karim Abdelkader*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

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The prevalence of multidrug-resistant Salmonella enterica among animal- and plant-derived food products threatens global healthcare and economic sectors. Hen egg white lysozyme is widely exploited as a food preservative against Gram-positive pathogens. Nevertheless, its limited penetration of the outer membrane renders it ineffective against Gram-negative bacteria. Herein, we present a safe and effective approach to facilitate HEWL access to peptidoglycan layers using cecropin A. In silico analysis of cecropin A peptide revealed an amphipathic α-helical peptide with potential outer membrane permeabilizing activity through its interaction with both hydrophobic and ionic stabilizing forces. Evaluation of HEWL/cecropin A combination showed a cecropin A dose-dependent bacterial count reduction up to 4.16 and 3.18 ± 0.26 log units against Salmonella enterica ATCC 35664 at the logarithmic and stationary growth phases, respectively. Moreover, the combination displayed antibacterial activity of 2.1 ± 0.31 and ~1 log-unit reductions against Salmonella enterica serovars Kentucky, Typhimurium, and Enteritidis, respectively, whereas Hato and Shangani were found irresponsive. The cytotoxicity assay revealed compatibility of cecropin A with oral epithelial cells. These observations suggest HEWL/cecropin A combination as an effective and safe alternative to lysozyme against Salmonella enterica.
Original languageEnglish
Article number2201
Number of pages15
Issue number10
Publication statusPublished - 16 Oct 2022


  • Salmonella enterica
  • hen egg white lysozyme
  • cecropin A
  • amphipathic helix
  • food preservative


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