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

Stephen R. S. R. Stockdale (1) , Jennifer J. Mahony (1) , Pascal P. Courtin (2) , Marie-Pierre M.-P. Chapot-Chartier (2) , Jan-Peter J.-P. van Pijkeren (3) , Robert A. R. A. Britton (3) , Horst H. Neve (4) , Knut J. K. J. Heller (4) , Bashir B. Aideh (5) , Finn K. F. K. Vogensen (5) , Douwe D. van Sinderen (1, 1)

1 UCC - University College Cork
2 MICALIS - MICrobiologie de l'ALImentation au Service de la Santé
3 Dept Microbiol & Mol Genet
4 Dept Microbiol & Biotechnol
5 UCPH FOOD - Department of Food Science [Copenhagen]

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.

Mots clés: LACTIC-ACBACTERIA; CONTROLLED GENE-EXPRESSION; BACILLUS-SUBTILIS; MEMBRANE-RECEPTOR; PEPTIDOGLYCAN STRUCTURE; ELECTRON-MICROSCOPY; ESCHERICHIA-COLI; LAMBDA-RECEPTOR; TAPE MEASURE; PROTEIN-GPJ

Domaines: Sciences agricoles

Stephen R. S. R. Stockdale, Jennifer J. Mahony, Pascal P. Courtin, Marie-Pierre M.-P. Chapot-Chartier, Jan-Peter J.-P. van Pijkeren, et al.. The Lactococcal Phages Tuc2009 and TP901-1 Incorporate Two Alternate Forms of Their Tail Fiber into Their Virions for Infection Specialization. Journal of Biological Chemistry, 2013, 288 (8), pp.5581 - 5590. ⟨10.1074/jbc.M112.444901⟩. ⟨hal-01001577⟩