DOI: 10.1101/515445Jan 8, 2019Paper

Phage-encoded cationic antimicrobial peptide used for outer membrane disruption in lysis

BioRxiv : the Preprint Server for Biology
Ashley HoltRy Young

Abstract

Spanins are required for the last step in bacteriophage lysis: the disruption of the outer membrane. Bioinformatic analysis has shown that ~15% of phages lack a spanin gene, which suggests an alternate mechanism of outer membrane disruption. To address this, we selected virulent podophage ϕKT as a spaninless exemplar and tested ϕKT genes for outer membrane disruption during lysis. Hypothetical novel gene 28 causes outer membrane disruption when coexpressed with ϕKT lysis genes and complements the lysis defect of a λ spanin mutant. Gp28 is a 56 aa cationic peptide with predicted amphipathic helical structure and is associated with the particulate fraction after lysis. Urea and KCl washes did not release gp28 from the particulate, suggesting a strong hydrophobic interaction with the membrane. Super high-resolution microscopy supports a primarily outer membrane localization for the peptide. Additionally, holin function is not required for gp28-mediated lysis. Gp28 is similar in size, charge, predicted fold, and membrane association to the human cathelicidin antimicrobial peptide LL-37. In standard assays to measure bactericidal and inhibitory effects of antimicrobial peptides on bacterial cells, synthesized gp28 performed equivale...Continue Reading

Related Concepts

Bacteriophages
Division of Adhesions
Genes
Lysis
Peptides
Potassium Chloride
Antimicrobial Cationic Peptides
Neutrophil basic proteins
Cathelicidin antimicrobial peptide
Size

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