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Nature. 2014 Jan 16;505(7483):432-5. doi: 10.1038/nature12816. Epub 2013 Dec 15.

Icosahedral bacteriophage ΦX174 forms a tail for DNA transport during infection.

Author information

1
1] Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA [2].
2
1] School of Plant Sciences and the BIO5 Institute, University of Arizona, Tucson, Arizona 85721, USA [2].
3
1] Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA [2] The Research Department, Shriner's Hospital for Children, Portland, Oregon 97239, USA.
4
Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA.
5
School of Plant Sciences and the BIO5 Institute, University of Arizona, Tucson, Arizona 85721, USA.
6
Molecular Genetics and Microbiology, Institute for Cell and Molecular Biology, The University of Texas at Austin, Austin, Texas 78712, USA.

Abstract

Prokaryotic viruses have evolved various mechanisms to transport their genomes across bacterial cell walls. Many bacteriophages use a tail to perform this function, whereas tail-less phages rely on host organelles. However, the tail-less, icosahedral, single-stranded DNA ΦX174-like coliphages do not fall into these well-defined infection processes. For these phages, DNA delivery requires a DNA pilot protein. Here we show that the ΦX174 pilot protein H oligomerizes to form a tube whose function is most probably to deliver the DNA genome across the host's periplasmic space to the cytoplasm. The 2.4 Å resolution crystal structure of the in vitro assembled H protein's central domain consists of a 170 Å-long α-helical barrel. The tube is constructed of ten α-helices with their amino termini arrayed in a right-handed super-helical coiled-coil and their carboxy termini arrayed in a left-handed super-helical coiled-coil. Genetic and biochemical studies demonstrate that the tube is essential for infectivity but does not affect in vivo virus assembly. Cryo-electron tomograms show that tubes span the periplasmic space and are present while the genome is being delivered into the host cell's cytoplasm. Both ends of the H protein contain transmembrane domains, which anchor the assembled tubes into the inner and outer cell membranes. The central channel of the H-protein tube is lined with amide and guanidinium side chains. This may be a general property of viral DNA conduits and is likely to be critical for efficient genome translocation into the host.

PMID:
24336205
DOI:
10.1038/nature12816
[Indexed for MEDLINE]

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