The Lactococcal Phages Tuc2009 and TP901-1 Incorporate Two Alternate Forms of Their Tail Fiber into Their Virions for Infection Specialization

摘要: Lactococcal phages Tuc2009 and TP901-1 possess a conserved tail fiber called tail-associated lysin (referred to as Tal2009 for Tuc2009, Tal901-1 TP901-1), suspended from their tips that projects peptidoglycan hydrolase domain toward potential host bacterium. can undergo proteolytic processing mid-protein at the glycine-rich sequence GG(S/N)SGGG, removing C-terminal structural lysin. In this study, we show of these Tal proteins is an M23 peptidase exhibits d-Ala-d-Asp endopeptidase activity required efficient infection stationary phase cells. Interestingly, observed facilitates increased adsorption efficiencies resulting phages. This represents, best our knowledge, first example results in heterogeneous population two phage types. Phages full-length fiber, or truncated derivative, are better adapted efficiently infect cells with extensively cross-linked cell wall host-adsorption efficiencies, respectively.