TY  - JOUR
  - Stockdale, SR,Mahony, J,Courtin, P,Chapot-Chartier, MP,van Pijkeren, JP,Britton, RA,Neve, H,Heller, KJ,Aideh, B,Vogensen, FK,van Sinderen, D
  - 2013
  - January
  - The Journal of Biological Chemistry
  - The Lactococcal Phages Tuc2009 and TP901-1 Incorporate Two Alternate Forms of Their Tail Fiber into Their Virions for Infection Specialization
  - Validated
  - ()
  - LACTIC-ACID BACTERIA CONTROLLED GENE-EXPRESSION BACILLUS-SUBTILIS ELECTRON-MICROSCOPY MEMBRANE-RECEPTOR PEPTIDOGLYCAN STRUCTURE ESCHERICHIA-COLI LAMBDA-RECEPTOR TAPE MEASURE PROTEIN-GPJ
  - 288
  - 5581
  - 5590
  - 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.
  - DOI 10.1074/jbc.M112.444901
DA  - 2013/01
ER  - 

@article{V206307553,
   = {Stockdale,  SR and Mahony,  J and Courtin,  P and Chapot-Chartier,  MP and van Pijkeren,  JP and Britton,  RA and Neve,  H and Heller,  KJ and Aideh,  B and Vogensen,  FK and van Sinderen,  D },
   = {2013},
   = {January},
   = {The Journal of Biological Chemistry},
   = {The Lactococcal Phages Tuc2009 and TP901-1 Incorporate Two Alternate Forms of Their Tail Fiber into Their Virions for Infection Specialization},
   = {Validated},
   = {()},
   = {LACTIC-ACID BACTERIA CONTROLLED GENE-EXPRESSION BACILLUS-SUBTILIS ELECTRON-MICROSCOPY MEMBRANE-RECEPTOR PEPTIDOGLYCAN STRUCTURE ESCHERICHIA-COLI LAMBDA-RECEPTOR TAPE MEASURE PROTEIN-GPJ},
   = {288},
  pages = {5581--5590},
   = {{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.}},
   = {DOI 10.1074/jbc.M112.444901},
  source = {IRIS}
}