Structure of the phage TP901-1 1.8 MDa baseplate suggests an alternative host adhesion mechanism

Typeset version

 

TY  - JOUR
  - Veesler, D.,Spinelli, S.,Mahony, J.,Lichiere, J.,Blangy, S.,Bricogne, G.,Legrand, P.,Ortiz-Lombardia, M.,Campanacci, V.,van Sinderen, D.,Cambillau, C.
  - 2012
  - June
  - Structure of the phage TP901-1 1.8 MDa baseplate suggests an alternative host adhesion mechanism
  - Validated
  - ()
  - 109
  - 2323
  - 8954
  - 88954
  - Phages of the Caudovirales order possess a tail that recognizes the host and ensures genome delivery upon infection. The X-ray structure of the approximately 1.8 MDa host adsorption device (baseplate) from the lactococcal phage TP901-1 shows that the receptor-binding proteins are pointing in the direction of the host, suggesting that this organelle is in a conformation ready for host adhesion. This result is in marked contrast with the lactococcal phage p2 situation, whose baseplate is known to undergo huge conformational changes in the presence of Ca(2+) to reach its active state. In vivo infection experiments confirmed these structural observations by demonstrating that Ca(2+) ions are required for host adhesion among p2-like phages (936-species) but have no influence on TP901-1-like phages (P335-species). These data suggest that these two families rely on diverse adhesion strategies which may lead to different signaling for genome release.Phages of the Caudovirales order possess a tail that recognizes the host and ensures genome delivery upon infection. The X-ray structure of the approximately 1.8 MDa host adsorption device (baseplate) from the lactococcal phage TP901-1 shows that the receptor-binding proteins are pointing in the direction of the host, suggesting that this organelle is in a conformation ready for host adhesion. This result is in marked contrast with the lactococcal phage p2 situation, whose baseplate is known to undergo huge conformational changes in the presence of Ca(2+) to reach its active state. In vivo infection experiments confirmed these structural observations by demonstrating that Ca(2+) ions are required for host adhesion among p2-like phages (936-species) but have no influence on TP901-1-like phages (P335-species). These data suggest that these two families rely on diverse adhesion strategies which may lead to different signaling for genome release.
  - 1091-6490 (Electronic) 00
  - http://www.ncbi.nlm.nih.gov/pubmed/22611190http://www.ncbi.nlm.nih.gov/pubmed/22611190
DA  - 2012/06
ER  - 
@article{V191490376,
   = {Veesler,  D. and Spinelli,  S. and Mahony,  J. and Lichiere,  J. and Blangy,  S. and Bricogne,  G. and Legrand,  P. and Ortiz-Lombardia,  M. and Campanacci,  V. and van Sinderen,  D. and Cambillau,  C. },
   = {2012},
   = {June},
   = {Structure of the phage TP901-1 1.8 MDa baseplate suggests an alternative host adhesion mechanism},
   = {Validated},
   = {()},
   = {109},
   = {2323},
  pages = {8954--88954},
   = {{Phages of the Caudovirales order possess a tail that recognizes the host and ensures genome delivery upon infection. The X-ray structure of the approximately 1.8 MDa host adsorption device (baseplate) from the lactococcal phage TP901-1 shows that the receptor-binding proteins are pointing in the direction of the host, suggesting that this organelle is in a conformation ready for host adhesion. This result is in marked contrast with the lactococcal phage p2 situation, whose baseplate is known to undergo huge conformational changes in the presence of Ca(2+) to reach its active state. In vivo infection experiments confirmed these structural observations by demonstrating that Ca(2+) ions are required for host adhesion among p2-like phages (936-species) but have no influence on TP901-1-like phages (P335-species). These data suggest that these two families rely on diverse adhesion strategies which may lead to different signaling for genome release.Phages of the Caudovirales order possess a tail that recognizes the host and ensures genome delivery upon infection. The X-ray structure of the approximately 1.8 MDa host adsorption device (baseplate) from the lactococcal phage TP901-1 shows that the receptor-binding proteins are pointing in the direction of the host, suggesting that this organelle is in a conformation ready for host adhesion. This result is in marked contrast with the lactococcal phage p2 situation, whose baseplate is known to undergo huge conformational changes in the presence of Ca(2+) to reach its active state. In vivo infection experiments confirmed these structural observations by demonstrating that Ca(2+) ions are required for host adhesion among p2-like phages (936-species) but have no influence on TP901-1-like phages (P335-species). These data suggest that these two families rely on diverse adhesion strategies which may lead to different signaling for genome release.}},
  issn = {1091-6490 (Electronic) 00},
   = {http://www.ncbi.nlm.nih.gov/pubmed/22611190http://www.ncbi.nlm.nih.gov/pubmed/22611190},
  source = {IRIS}
}
AUTHORSVeesler, D.,Spinelli, S.,Mahony, J.,Lichiere, J.,Blangy, S.,Bricogne, G.,Legrand, P.,Ortiz-Lombardia, M.,Campanacci, V.,van Sinderen, D.,Cambillau, C.
YEAR2012
MONTHJune
JOURNAL_CODE
TITLEStructure of the phage TP901-1 1.8 MDa baseplate suggests an alternative host adhesion mechanism
STATUSValidated
TIMES_CITED()
SEARCH_KEYWORD
VOLUME109
ISSUE2323
START_PAGE8954
END_PAGE88954
ABSTRACTPhages of the Caudovirales order possess a tail that recognizes the host and ensures genome delivery upon infection. The X-ray structure of the approximately 1.8 MDa host adsorption device (baseplate) from the lactococcal phage TP901-1 shows that the receptor-binding proteins are pointing in the direction of the host, suggesting that this organelle is in a conformation ready for host adhesion. This result is in marked contrast with the lactococcal phage p2 situation, whose baseplate is known to undergo huge conformational changes in the presence of Ca(2+) to reach its active state. In vivo infection experiments confirmed these structural observations by demonstrating that Ca(2+) ions are required for host adhesion among p2-like phages (936-species) but have no influence on TP901-1-like phages (P335-species). These data suggest that these two families rely on diverse adhesion strategies which may lead to different signaling for genome release.Phages of the Caudovirales order possess a tail that recognizes the host and ensures genome delivery upon infection. The X-ray structure of the approximately 1.8 MDa host adsorption device (baseplate) from the lactococcal phage TP901-1 shows that the receptor-binding proteins are pointing in the direction of the host, suggesting that this organelle is in a conformation ready for host adhesion. This result is in marked contrast with the lactococcal phage p2 situation, whose baseplate is known to undergo huge conformational changes in the presence of Ca(2+) to reach its active state. In vivo infection experiments confirmed these structural observations by demonstrating that Ca(2+) ions are required for host adhesion among p2-like phages (936-species) but have no influence on TP901-1-like phages (P335-species). These data suggest that these two families rely on diverse adhesion strategies which may lead to different signaling for genome release.
PUBLISHER_LOCATION
ISBN_ISSN1091-6490 (Electronic) 00
EDITION
URLhttp://www.ncbi.nlm.nih.gov/pubmed/22611190http://www.ncbi.nlm.nih.gov/pubmed/22611190
DOI_LINK
FUNDING_BODY
GRANT_DETAILS