Structural highlights
Function
H_BPPHS Probably triggers with protein G the injection of the phage DNA into the host upon conformational changes induced by virus-host receptor interaction.[1] [2]
Publication Abstract from PubMed
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 PhiX174-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 PhiX174 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 A resolution crystal structure of the in vitro assembled H protein's central domain consists of a 170 A-long alpha-helical barrel. The tube is constructed of ten alpha-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.
Icosahedral bacteriophage PhiX174 forms a tail for DNA transport during infection.,Sun L, Young LN, Zhang X, Boudko SP, Fokine A, Zbornik E, Roznowski AP, Molineux IJ, Rossmann MG, Fane BA Nature. 2013 Dec 15. doi: 10.1038/nature12816. PMID:24336205[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Inagaki M, Tanaka A, Suzuki R, Wakashima H, Kawaura T, Karita S, Nishikawa S, Kashimura N. Characterization of the binding of spike H protein of bacteriophage phiX174 with receptor lipopolysaccharides. J Biochem. 2000 Apr;127(4):577-83. PMID:10739948
- ↑ Inagaki M, Wakashima H, Kato M, Kaitani K, Nishikawa S. Crucial role of the lipid part of lipopolysaccharide for conformational change of minor spike H protein of bacteriophage phiX174. FEMS Microbiol Lett. 2005 Oct 15;251(2):305-11. PMID:16143459 doi:http://dx.doi.org/10.1016/j.femsle.2005.08.014
- ↑ Sun L, Young LN, Zhang X, Boudko SP, Fokine A, Zbornik E, Roznowski AP, Molineux IJ, Rossmann MG, Fane BA. Icosahedral bacteriophage PhiX174 forms a tail for DNA transport during infection. Nature. 2013 Dec 15. doi: 10.1038/nature12816. PMID:24336205 doi:http://dx.doi.org/10.1038/nature12816