title: F-Type Bacteriocins of Listeria monocytogenes: a New Class of Phage Tail-Like Structures Reveals Broad Parallel Coevolution between Tailed Bacteriophages and High-Molecular-Weight Bacteriocins.
abstract: Listeria monocytogenes is a significant foodborne human pathogen that can cause severe disease in certain high-risk individuals. L. monocytogenes is known to produce high-molecular-weight, phage tail-like bacteriocins, or "monocins," upon induction of the SOS system. In this work, we purified and characterized monocins and found them to be a new class of F-type bacteriocins. The L. monocytogenes monocin genetic locus was cloned and expressed in Bacillus subtilis, producing specifically targeted bactericidal particles. The receptor binding protein, which determines target cell specificity, was identified and engineered to change the bactericidal spectrum. Unlike the F-type pyocins of Pseudomonas aeruginosa, which are related to lambda-like phage tails, monocins are more closely related to TP901-1-like phage tails, structures not previously known to function as bacteriocins. Monocins therefore represent a new class of phage tail-like bacteriocins. It appears that multiple classes of phage tails and their related bacteriocins have coevolved separately in parallel.
  
  
  
  Phage tail-like bacteriocins (PTLBs) are structures widespread among the members of the bacterial kingdom that are evolutionarily related to the DNA delivery organelles of phages (tails). We identified and characterized "monocins" of Listeria monocytogenes and showed that they are related to the tail structures of TP901-1-like phages, structures not previously known to function as bacteriocins. Our results show that multiple types of envelope-penetrating machines have coevolved in parallel to function either for DNA delivery (phages) or as membrane-disrupting bacteriocins. While it has commonly been assumed that these structures were coopted from phages, we cannot rule out the opposite possibility, that ancient phages coopted complex bacteriocins from the cell, which then underwent adaptations to become efficient at translocating DNA.
authors.affiliation: AvidBiotics Corporation, South San Francisco, California, USA.
authors.forename: Grace
authors.initials: G
authors.lastname: Lee
authors.affiliation: AvidBiotics Corporation, South San Francisco, California, USA.
authors.forename: Urmi
authors.initials: U
authors.lastname: Chakraborty
authors.affiliation: AvidBiotics Corporation, South San Francisco, California, USA.
authors.forename: Dana
authors.initials: D
authors.lastname: Gebhart
authors.affiliation: AvidBiotics Corporation, South San Francisco, California, USA.
authors.forename: Gregory R
authors.initials: GR
authors.lastname: Govoni
authors.affiliation: Department of Microbiology, Immunology and Molecular Genetics, University of California, Los Angeles (UCLA), Los Angeles, California, USA.
authors.forename: Z Hong
authors.initials: ZH
authors.lastname: Zhou
authors.affiliation: AvidBiotics Corporation, South San Francisco, California, USA dean@avidbiotics.com.
authors.forename: Dean
authors.initials: D
authors.lastname: Scholl
mesh_terms: D001430:Bacteriocins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001435:Bacteriophages / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D005075:Biological Evolution; D008089:Listeria monocytogenes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008970:Molecular Weight; D017376:Viral Tail Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D001430:Bacteriocins; D017376:Viral Tail Proteins