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Proc Natl Acad Sci U S A. 2012 Jun 5;109(23):8954-8. doi: 10.1073/pnas.1200966109. Epub 2012 May 18.

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

Author information

1
Architecture et Fonction des Macromolécules Biologiques, Aix-Marseille Université, Campus de Luminy, Case 932, 13288 Marseille Cedex 09, France. david.veesler@afmb.univ-mrs.fr

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 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.

PMID:
22611190
PMCID:
PMC3384155
DOI:
10.1073/pnas.1200966109
[Indexed for MEDLINE]
Free PMC Article

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