Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions

Jiang, Wen; Li, Zongli; Zhang, Zhixian; Baker, Matthew L.; Prevelige, Peter E.; Chiu, Wah

doi:10.1038/nsb891

Cited by 190 publications

(214 citation statements)

References 26 publications

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“…The capsid protein is organized into a T ¼ 4 icosahedral lattice and has a HK97 fold. This fold of the capsid protein has been observed in all tailed phages (12)(13)(14)(15)(16)(17)(18). The short C1 tail is surrounded by a skirt of 12 long appendages, each terminating with a flexible globular domain, unlike those of tailed phages studied previously.…”

mentioning

confidence: 73%

Structural investigations of a Podoviridae streptococcus phage C1, implications for the mechanism of viral entry

Aksyuk

Bowman

Kaufmann

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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The Podoviridae phage C1 was one of the earliest isolated bacteriophages and the first virus documented to be active against streptococci. The icosahedral and asymmetric reconstructions of the virus were calculated using cryo-electron microscopy. The capsid protein has an HK97 fold arranged into a T ¼ 4 icosahedral lattice. The C1 tail is terminated with a φ29-like knob, surrounded by a skirt of twelve long appendages with novel morphology. Several C1 structural proteins have been identified, including a candidate for an appendage. The crystal structure of the knob has an N-terminal domain with a fold observed previously in tube forming proteins of Siphoviridae and Myoviridae phages. The structure of C1 suggests the mechanisms by which the virus digests the cell wall and ejects its genome. Although there is little sequence similarity to other phages, conservation of the structural proteins demonstrates a common origin of the head and tail, but more recent evolution of the appendages.bacteriophage C1 tail | tail knob | X-ray crystallography

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mentioning

confidence: 73%

Structural investigations of a Podoviridae streptococcus phage C1, implications for the mechanism of viral entry

Aksyuk

Bowman

Kaufmann

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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“…The fold of these secondary structural elements is reminiscent of a canonical fold first identified in the HK97 head protein gp5 (Fig. 3C) (11) and, subsequently, found in the major capsid proteins of many DNA viruses, including epsilon15 (6, 7), P22 (12), and herpesvirus capsid (13). A BLAST search for BPP-1 protein homologs identified that Bbp17 has 35% sequence identify to HK97 gp5.…”

mentioning

confidence: 99%

Three-dimensional structure of tropism-switching Bordetella bacteriophage

Dai¹,

Hodes²,

Hui³

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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Bacteriophage BPP-1, which infects Bordetella species, can switch its specificity by mutations to the ligand-binding surface of its major tropism-determinant protein, Mtd. This targeted mutagenesis results from the activity of a phage-encoded diversity-generating retroelement. Purified Mtd binds its receptor with low affinity, yet BPP-1 binding and infection of Bordettella cells are efficient because of high-avidity binding between phage-associated Mtd and its receptor. Here, using an integrative approach of three-dimensional (3D) structural analyses of the entire phage by cryo-electron tomography and single-prticle cryo-electron microscopy, we provide direct localization of Mtd in the phage and the structural basis of the high-avidity binding of the BPP-1 phage. Our structure shows that each BPP-1 particle has a T = 7 icosahedral head and an unusual tail apparatus consisting of a short central tail "hub," six short tail spikes, and six extended tail fibers. Subtomographic averaging of the tail fiber maps revealed a two-lobed globular structure at the distal end of each long tail fiber. Tomographic reconstructions of immuno-gold-labeled BPP-1 directly localized Mtd to these globular structures. Finally, our icosahedral reconstruction of the BPP-1 head at 7Å resolution reveals an HK97-like major capsid protein stabilized by a smaller cementing protein. Our structure represents a unique bacteriophage reconstruction with its tail fibers and ligand-binding domains shown in relation to its tail apparatus. The localization of Mtd at the distal ends of the six tail fibers explains the high avidity binding of Mtd molecules to cell surfaces for initiation of infection.avidity | Bordetella phage | cryo-electron microscopy | tropism-determinant protein

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“…Figure 4 shows the 3D structure of a HK97 subunit superimposed on a cryo-EM image of a P22 subunit. Jiang et al [7] have shown that the major helices of P22 undergo significant movement during the maturation transition as shown in figure 5. Whether the major helices of HK97 undergo a similar motion has not yet been unambiguously resolved [3].…”

Section: Analysis and Datamentioning

confidence: 99%

“…These processes were first studied with phages T4 and lambda using optical diffraction of negatively stained micrographs [6,13]. Subsequently, these processes have been studied at higher resolution by cryo-electron microscopy [1,7,9,10,12]. For phage P22, the hexagonal array of subunits at local six-fold axes are distinctively skewed, with a hole in the centre.…”

Section: Introductionmentioning

confidence: 99%

Lattice Transformations and Subunit Conformational Changes in Phage Capsid Maturation

Gossard

King

2005

Computational and Mathematical Methods in Medicine

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A general feature of the pathways for the assembly of double-stranded DNA phages and viruses is the assembly of coat and scaffolding subunits into a precursor shell or procapsid, followed by packaging of the genomic DNA into the shell. Coupled to this DNA packaging process is the loss of the scaffolding subunits and expansion and re-organization of the procapsid lattice to the lattice of the mature virus. Such lattice transitions have also been observed with adenoviruses and herpesviruses. In re-organizing into the mature capsid lattice, each subunit of the precursor lattice must change its conformation, or its relationship with its neighbours, or both. We briefly review here recent structural data for phages P22 and HK97, and describe the motions and conformational changes associated with this lattice transition. Possible functions of such constrained transformations within the virus life-cycle are discussed.

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Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions

Cited by 190 publications

References 26 publications

Structural investigations of a Podoviridae streptococcus phage C1, implications for the mechanism of viral entry

Structural investigations of a Podoviridae streptococcus phage C1, implications for the mechanism of viral entry

Three-dimensional structure of tropism-switching Bordetella bacteriophage

Lattice Transformations and Subunit Conformational Changes in Phage Capsid Maturation

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