Sequential assembly in vivo of the bacteriophage P22 genome translocation channel
- 1Yale University
Abstract
Bacteriophage P22 ejects four internal proteins into infected cells to assemble a channel for genome translocation across the cell envelope. However, how these proteins cooperate to build the trans-envelope channel remains enigmatic. Using in situ single-particle cryogenic electron microscopy, we determined near-atomic in vivo structures of P22 infection intermediates, revealing how the tail hub protein gp10 templates the sequential assembly of three internal proteins gp7*, gp20 and gp16 into a ~50-nm trans-envelope channel that extends from the virion into the host cytoplasm. Functional analyses explain why phage DNA can be detected in supernatant fluids during infection by channel-defective mutants. Our structures also provide a mechanistic basis for the long-standing observation that a P22 virion lacking gp16 can be complemented, extra-cytoplasmically, by a co-infecting virion lacking gp20, thereby allowing the genome in the gp16-deficient particle to enter the host cytoplasm.
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BibTeX
@misc{yu2026sequential,
title = {{Sequential assembly in vivo of the bacteriophage P22 genome translocation channel}},
author = {H. Yu and J. Yue and T. Park and c. wang and M. Chen and J. Liu and I. J. Molineux},
howpublished = {bioRxiv},
year = {2026},
month = sep,
doi = {10.64898/2026.09.03.749273},
url = {https://www.biorxiv.org/content/10.64898/2026.09.03.749273v1},
note = {CC BY},
}
RIS
TY - UNPB
TI - Sequential assembly in vivo of the bacteriophage P22 genome translocation channel
AU - H. Yu
AU - J. Yue
AU - T. Park
AU - c. wang
AU - M. Chen
AU - J. Liu
AU - I. J. Molineux
PY - 2026
DA - 2026/09/03
PB - bioRxiv
DO - 10.64898/2026.09.03.749273
UR - https://www.biorxiv.org/content/10.64898/2026.09.03.749273v1
AB - Bacteriophage P22 ejects four internal proteins into infected cells to assemble a channel for genome translocation across the cell envelope. However, how these proteins cooperate to build the trans-envelope channel remains enigmatic. Using in situ single-particle cryogenic electron microscopy, we determined near-atomic in vivo structures of P22 infection intermediates, revealing how the tail hub protein gp10 templates the sequential assembly of three internal proteins gp7*, gp20 and gp16 into a ~50-nm trans-envelope channel that extends from the virion into the host cytoplasm. Functional analyses explain why phage DNA can be detected in supernatant fluids during infection by channel-defective mutants. Our structures also provide a mechanistic basis for the long-standing observation that a P22 virion lacking gp16 can be complemented, extra-cytoplasmically, by a co-infecting virion lacking gp20, thereby allowing the genome in the gp16-deficient particle to enter the host cytoplasm.
ER -