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

  • David Veesler
  • , Silvia Spinelli
  • , Jennifer Mahony
  • , Julie Lichière
  • , Stéphanie Blangy
  • , Gérard Bricogne
  • , Pierre Legrand
  • , Miguel Ortiz-Lombardia
  • , Valérie Campanacci
  • , Douwe Van Sinderen
  • , Christian Cambillau

Research output: Contribution to journalArticlepeer-review

Abstract

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 Ca2+ to reach its active state. In vivo infection experiments confirmed these structural observations by demonstrating that Ca2+ 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.

Original languageEnglish
Pages (from-to)8954-8958
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume109
Issue number23
DOIs
Publication statusPublished - 5 Jun 2012

Keywords

  • Bacteriophage
  • Crystal structure
  • Lactococcus lactis
  • Siphoviridae
  • Viral infection

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