bioRxiv Science⌕ Search

Biology subjects

Sztanko, K. M.

Publications and source records attributed to Sztanko, K. M..

2 recordsLinked to original sources

Prophages express a type IV pilus component to provide anti-phage defence

Phage genomes integrated within bacterial genomes, known as prophages, frequently encode proteins that provide defence against further phage infection. These proteins often function at the cell surface and prevent phages from attaching to their host receptor. Here, we describe the discovery of prophage-encoded proteins that resemble FimU, a component of the Pseudomonas aeruginosa type IV pilus. These phage FimU proteins are incorporated into the pilus without altering its function, yet they mediate robust protection against infection by phages that bind to the tip of the pilus, where FimU is likely located. The phage FimU proteins and the phage tail proteins that interact with FimU are highly diverse, suggesting that evolution in this system is driven by phage versus phage competition. To our knowledge, this is the first example of anti-phage defence mediated by replacement of a bacterial cell surface component with a phage-encoded protein.

microbiology↗

Bacteria defend against phages through type IV pilus glycosylation

Bacterial surface structures such as type IV pili are common receptors for phage. Strains of the opportunistic pathogen Pseudomonas aeruginosa express one of five different major type IV pilin alleles, two of which are glycosylated with either lipopolysaccharide O-antigen units or polymers of D-arabinofuranose. Here we show that both these post-translational modifications protect P. aeruginosa from a variety of pilus-specific phages. We identified a phage capable of infecting strains expressing both non-glycosylated and glycosylated pilins, and through construction of a chimeric phage, traced this ability to its unique tail proteins. Alteration of pilin sequence, or masking of binding sites by glycosylation, both block phage infection. The energy invested by prokaryotes in glycosylating thousands of pilin subunits is thus explained by the protection against phage predation provided by these common decorations.\n\nSIGNIFICANCEPost-translational modification of bacterial and archaeal surface structures such as pili and flagella is widespread, but the function of these decorations is not clear. We propose that predation by bacteriophages that use these structures as receptors selects for strains that mask potential phage binding sites using glycosylation. Phages are of significant interest as alternative treatments for antibiotic-resistant pathogens, but the ways in which phage interact with host receptors are not well understood. We show that specific phage tail proteins allow for infection of strains with glycosylated pili, providing a foundation for the creation of designer phages that can circumvent first-line bacterial defenses.

microbiology↗