Natural activity of the antimicrobial peptide Defensin includes execution of tumour cell death by tumour necrosis factor in Drosophila.

A rapid absorption and retention of antimicrobial peptides by dead Escherichia coli cells can increase the survivability of the cell population in a "cooperative" fashion.

While antimicrobial cocktails are highly effective for defence against pathogenic microbes, the innate immune response may instead employ highly specific peptidic antibiotics to combat certain natural enemies.

The attempt to manipulate a microbiome in planta to study the ecological consequences under field conditions leaves plants and their microbes surprisingly unimpressed.

Proline/glycine kink in the helical peptides affects the peptide ability to form membrane pores by stabilising toroidal pore structures but disrupting barrel-stave pore structures.

A novel innate defense mechanism of cell lysis involves the coordinated oligomerization of a defensin by interaction with the membrane lipid, phosphatidylinositol 4,5-bisphosphate.

Receptor recognition of antimicrobial peptides is important for Salmonellae to survive inside macrophages and cause disease.

A better understanding of the mechanisms underpinning the growth of mycobacteria could help identify targets for new antibiotics.

Uncovering a mechanism for how inflammatory signaling is opposed by a phosphatase identifies a potential druggable target to treat E. coli sepsis.