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Structure of phage P22 cell envelope–penetrating needle

Nature Structural & Molecular Biology volume 14, pages 12211226 (2007) | Download Citation

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Abstract

Bacteriophage P22 infects Salmonella enterica by injecting its genetic material through the cell envelope. During infection, a specialized tail needle, gp26, is injected into the host, likely piercing a hole in the host cell envelope. The 2.1-Å crystal structure of gp26 reveals a 240-Å elongated protein fiber formed by two trimeric coiled-coil domains interrupted by a triple β-helix. The N terminus of gp26 plugs the portal protein channel, retaining the genetic material inside the virion. The C-terminal tip of the fiber exposes β-hairpins with hydrophobic tips similar to those seen in class II fusion peptides. The α-helical core connecting these two functionally polarized tips presents four trimerization octads with consensus sequence IXXLXXXV. The slender conformation of the gp26 fiber minimizes the surface exposed to solvent, which is consistent with the idea that gp26 traverses the cell envelope lipid bilayers.

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Acknowledgements

We thank N. Walker for technical help. We are grateful to V. Stojanoff at the NSLS and to the macCHESS staff for beam time and assistance in data collection. This work was supported in part by US National Science Foundation grant MCB-990526 to S.C.

Author information

Affiliations

  1. Department of Biochemistry and Molecular Biology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, New York 13210, USA.

    • Adam S Olia
    •  & Gino Cingolani
  2. Department of Pathology, University of Utah Medical School, Salt Lake City, Utah 84112, USA.

    • Sherwood Casjens

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Contributions

A.S.O. and G.C. contributed to the structural and biochemical studies. S.C. participated in the design and coordination of the study. A.S.O., S.C. and G.C. wrote the manuscript.

Corresponding author

Correspondence to Gino Cingolani.

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DOI

https://doi.org/10.1038/nsmb1317

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