title: The lactococcal phages Tuc2009 and TP901-1 incorporate two alternate forms of their tail fiber into their virions for infection specialization.
abstract: Lactococcal phages Tuc2009 and TP901-1 possess a conserved tail fiber called a tail-associated lysin (referred to as Tal(2009) for Tuc2009, and Tal(901-1) for TP901-1), suspended from their tail tips that projects a peptidoglycan hydrolase domain toward a potential host bacterium. Tal(2009) and Tal(901-1) can undergo proteolytic processing mid-protein at the glycine-rich sequence GG(S/N)SGGG, removing their C-terminal structural lysin. In this study, we show that the peptidoglycan hydrolase of these Tal proteins is an M23 peptidase that exhibits D-Ala-D-Asp endopeptidase activity and that this activity is required for efficient infection of stationary phase cells. Interestingly, the observed proteolytic processing of Tal(2009) and Tal(901-1) facilitates increased host adsorption efficiencies of the resulting phages. This represents, to the best of our knowledge, the first example of tail fiber proteolytic processing that results in a heterogeneous population of two phage types. Phages that possess a full-length tail fiber, or a truncated derivative, are better adapted to efficiently infect cells with an extensively cross-linked cell wall or infect with increased host-adsorption efficiencies, respectively.
authors.affiliation: Department of Microbiology, University College Cork, Cork, Ireland.
authors.forename: Stephen R
authors.initials: SR
authors.lastname: Stockdale
authors.forename: Jennifer
authors.initials: J
authors.lastname: Mahony
authors.forename: Pascal
authors.initials: P
authors.lastname: Courtin
authors.forename: Marie-Pierre
authors.initials: MP
authors.lastname: Chapot-Chartier
authors.forename: Jan-Peter
authors.initials: JP
authors.lastname: van Pijkeren
authors.forename: Robert A
authors.initials: RA
authors.lastname: Britton
authors.forename: Horst
authors.initials: H
authors.lastname: Neve
authors.forename: Knut J
authors.initials: KJ
authors.lastname: Heller
authors.forename: Bashir
authors.initials: B
authors.lastname: Aideh
authors.forename: Finn K
authors.initials: FK
authors.lastname: Vogensen
authors.forename: Douwe
authors.initials: D
authors.lastname: van Sinderen
mesh_terms: D000327:Adsorption; D001422:Bacterial Adhesion; D019295:Computational Biology / Q000379:methods; D006868:Hydrolysis; D013294:Lactococcus lactis / Q000821:virology*; D016296:Mutagenesis; D010457:Peptidoglycan / Q000737:chemistry; D010957:Plasmids / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D017906:Siphoviridae / Q000235:genetics / Q000378:metabolism*; D017376:Viral Tail Proteins / Q000737:chemistry / Q000378:metabolism; D014771:Virion / Q000378:metabolism
chemical_list: D010457:Peptidoglycan; D017376:Viral Tail Proteins