Distantly related Alteromonas bacteriophages share tail fibers exhibiting properties of transient chaperone caps.

ABSTRACT: The host recognition modules encoding the injection machinery and receptor binding proteins (RBPs) of bacteriophages are predisposed to mutation and recombination to maintain infectivity towards co-evolving bacterial hosts. In this study, we reveal how Alteromonas mediterranea schitovirus A5 shares its host recognition module, including tail fiber and cognate chaperone, with phages from distantly related families including Alteromonas myovirus V22. While the V22 chaperone is essential for producing active tail fibers, here we demonstrate production of functional A5 tail fibers regardless of chaperone co-expression. AlphaFold-generated models of tail fiber and chaperone pairs from phages A5, V22, and other Alteromonas phages reveal how amino acid insertions within both A5-like proteins resu

SUBMITTER: Gonzalez-Serrano R 

PROVIDER: S-EPMC10579305 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature