TY  - JOUR
  - Stockdale, S. R.,Mahony, J.,Courtin, P.,Chapot-Chartier, M. P.,van Pijkeren, J. P.,Britton, R. A.,Neve, H.,Heller, K. J.,Aideh, B.,Vogensen, F. K.,van Sinderen, D.
  - 2013
  - January
  - The lactococcal phages Tuc2009 and TP901-1 incorporate two alternate forms of their tail fibre into their virions for infection specialization
  - Validated
  - ()
  - Lactococcal phages Tuc2009 and TP901-1 possess a conserved tail fibre, called a Tail-Associated Lysin (referred to as Tal2009 for Tuc2009, and Tal901-1 for TP901-1), suspended from their tail tips that projects a Peptidoglycan-Hydrolase (PGH) domain towards a potential host bacterium. Tal2009 and Tal901-1 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 PGH of these Tal proteins is an M23 peptidase which 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 Tal2009 and Tal901-1 facilitates increased host adsorption efficiencies of the resulting phages. This represents, to the best of our knowledge, the first example of tail fibre proteolytic processing that results in a heterogeneous population of two phage types. Phages which possess a full-length tail fibre, or a truncated derivative, are better adapted to efficiently infect cells with extensively cross-linked cell wall, or infect with increased host-adsorption efficiencies, respectively.Lactococcal phages Tuc2009 and TP901-1 possess a conserved tail fibre, called a Tail-Associated Lysin (referred to as Tal2009 for Tuc2009, and Tal901-1 for TP901-1), suspended from their tail tips that projects a Peptidoglycan-Hydrolase (PGH) domain towards a potential host bacterium. Tal2009 and Tal901-1 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 PGH of these Tal proteins is an M23 peptidase which 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 Tal2009 and Tal901-1 facilitates increased host adsorption efficiencies of the resulting phages. This represents, to the best of our knowledge, the first example of tail fibre proteolytic processing that results in a heterogeneous population of two phage types. Phages which possess a full-length tail fibre, or a truncated derivative, are better adapted to efficiently infect cells with extensively cross-linked cell wall, or infect with increased host-adsorption efficiencies, respectively.
  - 1083-351X (Electronic) 00
  - http://www.ncbi.nlm.nih.gov/pubmed/23300085http://www.ncbi.nlm.nih.gov/pubmed/23300085
DA  - 2013/01
ER  - 

@article{V191490370,
   = {Stockdale,  S. R. and Mahony,  J. and Courtin,  P. and Chapot-Chartier,  M. P. and van Pijkeren,  J. P. and Britton,  R. A. and Neve,  H. and Heller,  K. J. and Aideh,  B. and Vogensen,  F. K. and van Sinderen,  D. },
   = {2013},
   = {January},
   = {The lactococcal phages Tuc2009 and TP901-1 incorporate two alternate forms of their tail fibre into their virions for infection specialization},
   = {Validated},
   = {()},
   = {{Lactococcal phages Tuc2009 and TP901-1 possess a conserved tail fibre, called a Tail-Associated Lysin (referred to as Tal2009 for Tuc2009, and Tal901-1 for TP901-1), suspended from their tail tips that projects a Peptidoglycan-Hydrolase (PGH) domain towards a potential host bacterium. Tal2009 and Tal901-1 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 PGH of these Tal proteins is an M23 peptidase which 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 Tal2009 and Tal901-1 facilitates increased host adsorption efficiencies of the resulting phages. This represents, to the best of our knowledge, the first example of tail fibre proteolytic processing that results in a heterogeneous population of two phage types. Phages which possess a full-length tail fibre, or a truncated derivative, are better adapted to efficiently infect cells with extensively cross-linked cell wall, or infect with increased host-adsorption efficiencies, respectively.Lactococcal phages Tuc2009 and TP901-1 possess a conserved tail fibre, called a Tail-Associated Lysin (referred to as Tal2009 for Tuc2009, and Tal901-1 for TP901-1), suspended from their tail tips that projects a Peptidoglycan-Hydrolase (PGH) domain towards a potential host bacterium. Tal2009 and Tal901-1 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 PGH of these Tal proteins is an M23 peptidase which 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 Tal2009 and Tal901-1 facilitates increased host adsorption efficiencies of the resulting phages. This represents, to the best of our knowledge, the first example of tail fibre proteolytic processing that results in a heterogeneous population of two phage types. Phages which possess a full-length tail fibre, or a truncated derivative, are better adapted to efficiently infect cells with extensively cross-linked cell wall, or infect with increased host-adsorption efficiencies, respectively.}},
  issn = {1083-351X (Electronic) 00},
   = {http://www.ncbi.nlm.nih.gov/pubmed/23300085http://www.ncbi.nlm.nih.gov/pubmed/23300085},
  source = {IRIS}
}