IRIS publication 191490370
The lactococcal phages Tuc2009 and TP901-1 incorporate two alternate forms of their tail fibre into their virions for infection specialization
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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 -
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@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} }
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AUTHORS | 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. | ||
YEAR | 2013 | ||
MONTH | January | ||
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TITLE | The lactococcal phages Tuc2009 and TP901-1 incorporate two alternate forms of their tail fibre into their virions for infection specialization | ||
STATUS | Validated | ||
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ABSTRACT | 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. | ||
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ISBN_ISSN | 1083-351X (Electronic) 00 | ||
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URL | http://www.ncbi.nlm.nih.gov/pubmed/23300085http://www.ncbi.nlm.nih.gov/pubmed/23300085 | ||
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