4.8 Article

Alternative mechanism for bacteriophage adsorption to the motile bacterium Caulobacter crescentus

Publisher

NATL ACAD SCIENCES
DOI: 10.1073/pnas.1012388108

Keywords

cryo-electron tomography; alpha-proteobacteria

Funding

  1. Emory University
  2. Children's Healthcare of Atlanta
  3. Georgia Research Alliance
  4. Human Frontier Science Program [RGP0051]
  5. National Institutes of Health [P01 GM066521]
  6. National Science Foundation through the Materials Research Science & Engineering Center (MRSEC)

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2D and 3D cryo-electron microscopy, together with adsorption kinetics assays of phi Cb13 and phi CbK phage-infected Caulobacter crescentus, provides insight into the mechanisms of infection. phi Cb13 and phi CbK actively interact with the flagellum and subsequently attach to receptors on the cell pole. We present evidence that the first interaction of the phage with the bacterial flagellum takes place through a filament on the phage head. This contact with the flagellum facilitates concentration of phage particles around the receptor (i.e., the pilus portals) on the bacterial cell surface, thereby increasing the likelihood of infection. Phage head filaments have not been well characterized and their function is described here. Phage head filaments may systematically underlie the initial interactions of phages with their hosts in other systems and possibly represent a widespread mechanism of efficient phage propagation.

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