Structure of a bacterial virus DNA-injection protein complex reveals a decameric assembly with a constricted molecular channel
Abstract
The multi-layered cell envelope structure of Gram-negative bacteria represents significant physical and chemical barriers for short-tailed phages to inject phage DNA into the host cytoplasm. Here we show that a DNA-injection protein of bacteriophage Sf6, gp12, forms a 465-kDa, decameric assembly in vitro. The electron microscopic structure of the gp12 assembly shows a ~150-Å, mushroom-like architecture consisting of a crown domain and a tube-like domain, which embraces a 25-Å-wide channel that could precisely accommodate dsDNA. The constricted channel suggests that gp12 mediates rapid, uni-directional injection of phage DNA into host cells by providing a molecular conduit for DNA translocation. The assembly exhibits a 10-fold symmetry, which may be a common feature among DNA-injection proteins of P22-like phages and may suggest a symmetry mismatch with respect to the 6-fold symmetric phage tail. As a result, the gp12 monomer is highly flexible in solution, supporting a mechanism for translocation of the protein through the conduit of the phage tail toward the host cell envelope, where it assembles into a DNA-injection device.
- Authors:
-
- Univ. of Kansas, Lawrence, KS (United States)
- The Scripps Research Institute, La Jolla, CA (United States)
- SLAC National Accelerator Lab., Menlo Park, CA (United States)
- ContraFect Corp., Yonkers, NY (United States)
- Publication Date:
- Research Org.:
- SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC)
- OSTI Identifier:
- 1253628
- Grant/Contract Number:
- AC02-76SF00515
- Resource Type:
- Accepted Manuscript
- Journal Name:
- PLoS ONE
- Additional Journal Information:
- Journal Volume: 11; Journal Issue: 2; Journal ID: ISSN 1932-6203
- Publisher:
- Public Library of Science
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; bacteriophages; host cells; protein structure; negative staining; cell membranes; viral packaging; DNA structure; molecular structure
Citation Formats
Zhao, Haiyan, Speir, Jeffrey A., Matsui, Tsutomu, Lin, Zihan, Liang, Lingfei, Lynn, Anna Y., Varnado, Brittany, Weiss, Thomas M., Tang, Liang, and Schuch, Raymond. Structure of a bacterial virus DNA-injection protein complex reveals a decameric assembly with a constricted molecular channel. United States: N. p., 2016.
Web. doi:10.1371/journal.pone.0149337.
Zhao, Haiyan, Speir, Jeffrey A., Matsui, Tsutomu, Lin, Zihan, Liang, Lingfei, Lynn, Anna Y., Varnado, Brittany, Weiss, Thomas M., Tang, Liang, & Schuch, Raymond. Structure of a bacterial virus DNA-injection protein complex reveals a decameric assembly with a constricted molecular channel. United States. https://doi.org/10.1371/journal.pone.0149337
Zhao, Haiyan, Speir, Jeffrey A., Matsui, Tsutomu, Lin, Zihan, Liang, Lingfei, Lynn, Anna Y., Varnado, Brittany, Weiss, Thomas M., Tang, Liang, and Schuch, Raymond. Tue .
"Structure of a bacterial virus DNA-injection protein complex reveals a decameric assembly with a constricted molecular channel". United States. https://doi.org/10.1371/journal.pone.0149337. https://www.osti.gov/servlets/purl/1253628.
@article{osti_1253628,
title = {Structure of a bacterial virus DNA-injection protein complex reveals a decameric assembly with a constricted molecular channel},
author = {Zhao, Haiyan and Speir, Jeffrey A. and Matsui, Tsutomu and Lin, Zihan and Liang, Lingfei and Lynn, Anna Y. and Varnado, Brittany and Weiss, Thomas M. and Tang, Liang and Schuch, Raymond},
abstractNote = {The multi-layered cell envelope structure of Gram-negative bacteria represents significant physical and chemical barriers for short-tailed phages to inject phage DNA into the host cytoplasm. Here we show that a DNA-injection protein of bacteriophage Sf6, gp12, forms a 465-kDa, decameric assembly in vitro. The electron microscopic structure of the gp12 assembly shows a ~150-Å, mushroom-like architecture consisting of a crown domain and a tube-like domain, which embraces a 25-Å-wide channel that could precisely accommodate dsDNA. The constricted channel suggests that gp12 mediates rapid, uni-directional injection of phage DNA into host cells by providing a molecular conduit for DNA translocation. The assembly exhibits a 10-fold symmetry, which may be a common feature among DNA-injection proteins of P22-like phages and may suggest a symmetry mismatch with respect to the 6-fold symmetric phage tail. As a result, the gp12 monomer is highly flexible in solution, supporting a mechanism for translocation of the protein through the conduit of the phage tail toward the host cell envelope, where it assembles into a DNA-injection device.},
doi = {10.1371/journal.pone.0149337},
journal = {PLoS ONE},
number = 2,
volume = 11,
place = {United States},
year = {Tue Feb 16 00:00:00 EST 2016},
month = {Tue Feb 16 00:00:00 EST 2016}
}
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