Morphogenesis of the T4 tail and tail fibers

Leiman, P.G.; Arisaka, Fumio; Raaij, Mark J. van; Kostyuchenko, V.A.; Aksyuk, Anastasia A.; Kanamaru, Shuji; Rossmann, Michael G.

doi:10.1186/1743-422x-7-355

Cited by 209 publications

(275 citation statements)

References 79 publications

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“…We suggest that TssK is likely interacting with TssG (MW = 38.4 kDa), which shares limited homology with T4 gp7 protein forming a link between the inner baseplate and the peripheral tail fiber network (Leiman et al , 2010; Taylor et al , 2016). TssK is also connected to the inner part of the baseplate wedge, likely the TssF dimer, through two fingerlike links (Fig 4C and D).…”

Section: Resultsmentioning

confidence: 98%

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Cryo‐ EM reconstruction of Type VI secretion system baseplate and sheath distal end

et al. 2017

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The bacterial Type VI secretion system (T6SS) assembles from three major parts: a membrane complex that spans inner and outer membranes, a baseplate, and a sheath–tube polymer. The baseplate assembles around a tip complex with associated effectors and connects to the membrane complex by TssK. The baseplate assembly initiates sheath–tube polymerization, which in some organisms requires TssA. Here, we analyzed both ends of isolated non‐contractile Vibrio cholerae sheaths by cryo‐electron microscopy. Our analysis suggests that the baseplate, solved to an average 8.0 Å resolution, is composed of six subunits of TssE/F2/G and the baseplate periphery is decorated by six TssK trimers. The VgrG/PAAR tip complex in the center of the baseplate is surrounded by a cavity, which may accommodate up to ~450 kDa of effector proteins. The distal end of the sheath, resolved to an average 7.5 Å resolution, shows sixfold symmetry; however, its protein composition is unclear. Our structures provide an important step toward an atomic model of the complete T6SS assembly.

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Section: Resultsmentioning

confidence: 98%

“…Volume‐to‐mass scale coefficient was calculated for the proteins with available X‐ray crystallographic structure (Leiman et al , 2010). …”

Section: Methodsmentioning

confidence: 99%

Cryo‐ EM reconstruction of Type VI secretion system baseplate and sheath distal end

et al. 2017

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“…It has been previously suggested for different tailed phages that a signal is propagated from the tail to the connector, changing its conformation and releasing the DNA (18,39,(52)(53)(54)(55). In C1 this trigger could propagate through the cylindrical tail part or could also come from the appendages, which interact directly with the connector.…”

Section: Resultsmentioning

confidence: 99%

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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“…The tail-spike of the podovirus P22 has been studied extensively in terms of carbohydrate binding, hydrolysis, folding, and assembly (17,18). Much is also known about assembly and function of the complex fibers of the myovirus T4 (19)(20)(21). Siphoviruses like T5 and λ contain less-studied side tail fibers (22, 23) which, like the T4 fibers, do not exhibit receptor-hydrolysis activity.…”

Section: Discussionmentioning

confidence: 99%

Structure of the receptor-binding carboxy-terminal domain of bacteriophage T7 tail fibers

Garcia-Doval

Raaij

2012

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

101

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The six bacteriophage T7 tail fibers, homo-trimers of gene product 17, are thought to be responsible for the first specific, albeit reversible, attachment to Escherichia coli lipopolysaccharide. The protein trimer forms kinked fibers comprised of an amino-terminal tail-attachment domain, a slender shaft, and a carboxyl-terminal domain composed of several nodules. Previously, we expressed, purified, and crystallized a carboxyl-terminal fragment comprising residues 371-553. Here, we report the structure of this protein trimer, solved using anomalous diffraction and refined at 2 Å resolution. Amino acids 371-447 form a tapered pyramid with a triangular cross-section composed of interlocked β-sheets from each of the three chains. The triangular pyramid domain has three α-helices at its narrow end, which are connected to a carboxyl-terminal three-blade β-propeller tip domain by flexible loops. The monomers of this tip domain each contain an eight-stranded β-sandwich. The exact topology of the β-sandwich fold is novel, but similar to that of knob domains of other viral fibers and the phage Sf6 needle. Several host-range change mutants have been mapped to loops located on the top of this tip domain, suggesting that this surface of the tip domain interacts with receptors on the cell surface.bacterial viruses | caudovirales | crystallography | infection | Podoviridae B acteriophages (bacterial viruses or phages) are important biological model systems and, because of the high specificity for their host bacteria, have found application in phage typing, food security, and phage therapy (1). Escherichia coli phage T7 is a member of the Podoviridae family of the Caudovirales (tailed phages) order (2). T7 is composed of an icosahedral capsid with a 20-nm short tail at one of the vertices (3, 4). The capsid is formed by the shell protein gene product (gp) 10 and encloses a DNA of 40 kb. A cylindrical structure composed of gp14, gp15, and gp16 is present inside the capsid (5), attached to the special vertex formed by the connector, a circular dodecamer of gp8 (6). Gp11 and gp12 form the tail; gp13, gp6.7, and gp7.3 have also been shown to be part of the virion and to be necessary for infection, although their location has not been established (7,8). Although extensive electron microscopy studies have been performed on phage T7 (3-6, 9), crystallographic studies have so far been limited to its nonstructural proteins.The main portion of the tail is composed of gp12, a large protein of which six copies are present (10); the small gp11 protein is also located in the tail (5). Attached to the tail are six fibers, each containing three copies of the gp17 protein. T7 tail fibers are elongated homo-trimers, which are responsible for initial, reversible, host cell recognition. A second, irreversible, decisionmaking interaction with the bacterial membrane is presumably mediated by one or more of the tail-tube proteins. DNA transfer into the host is then mediated by an extension formed by gp14-16 (7, 8, 11). Previously, we have reported t...

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Morphogenesis of the T4 tail and tail fibers

Cited by 209 publications

References 79 publications

Cryo‐ EM reconstruction of Type VI secretion system baseplate and sheath distal end

Cryo‐ EM reconstruction of Type VI secretion system baseplate and sheath distal end

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

Structure of the receptor-binding carboxy-terminal domain of bacteriophage T7 tail fibers

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