Structure and Function of Bacteriophage T4

Yap, Moh Lan; Rossmann, Michael G.

doi:10.2217/fmb.14.91

Cited by 131 publications

(101 citation statements)

References 143 publications

(146 reference statements)

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“…After the individual wedges have assembled, six wedges assemble around the central hub (12) to form the dome-shaped baseplate ( Fig. 4B and Movie S2).…”

Section: Discussionmentioning

confidence: 99%

“…Crystals of hubless baseplates that diffracted X-rays to 4.2 Å resolution (12,33) were dissolved in 50 mM Tris, 100 mM NaCl buffer at pH 8 to a concentration of 2 μg/mL. Aliquots of 3 μL of sample were loaded on glow-discharged C-Flat grids (CF-1.2/1.3-4C-50, CF-2/2-4C-50).…”

Section: Methodsmentioning

confidence: 99%

“…A total of 134 protein subunits from 15 different proteins form the ∼6.5-MDa baseplate (Table S1) (8,11). The structure of the T4 baseplate has been studied extensively by cryoelectron microscopy (cryo-EM) of the whole virus and X-ray crystallography of individual proteins (12). Cryo-EM maps of the baseplate when in the dome-(9) and starshaped (10) conformations were previously reported to 12 Å and 16 Å resolution, respectively.…”

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confidence: 99%

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Role of bacteriophage T4 baseplate in regulating assembly and infection

Yap

Klose

Arisaka

et al. 2016

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

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Bacteriophage T4 consists of a head for protecting its genome and a sheathed tail for inserting its genome into a host. The tail terminates with a multiprotein baseplate that changes its conformation from a "high-energy" dome-shaped to a "low-energy" star-shaped structure during infection. Although these two structures represent different minima in the total energy landscape of the baseplate assembly, as the dome-shaped structure readily changes to the star-shaped structure when the virus infects a host bacterium, the dome-shaped structure must have more energy than the star-shaped structure. Here we describe the electron microscopy structure of a 3.3-MDa in vitro-assembled star-shaped baseplate with a resolution of 3.8 Å. This structure, together with other genetic and structural data, shows why the high-energy baseplate is formed in the presence of the central hub and how the baseplate changes to the lowenergy structure, via two steps during infection. Thus, the presence of the central hub is required to initiate the assembly of metastable, high-energy structures. If the high-energy structure is formed and stabilized faster than the low-energy structure, there will be insufficient components to assemble the low-energy structure.bacteriophage T4 | cryo-EM reconstruction | baseplate assembly | conformational changes | near-atomic resolution M ost bacteriophages have a tail. At the distal end of the tail there is usually a baseplate that is decorated by some fibers (1). The baseplate initiates infection when the tail fibers bind to a host cell. Signals are transmitted from the tail fibers via the baseplate to the tail that then trigger the ejection of the phage genome from the head into the host cell through the tail tube. Two evolutionary related structures, of pyocin (2, 3) and of the type VI secretion system (4, 5), are found in bacteria as defense systems to kill competing bacteria. These structures are remarkably similar to the tail baseplate structure of bacteriophages, suggesting that tail baseplate-like structures are effective organelles for infecting bacteria (6, 7).T4 is a member of the Myoviridae family of bacteriophages. These phages have a sheath around the tail tube that contracts during infection (Fig. 1) (8). T4 has a complex baseplate that is essential for assuring a highly efficient infection mechanism (8). After recognition of an Escherichia coli host cell by some of the six long-tail fibers (LTF), the short-tail fibers (STF) that are a part of the baseplate, bind irreversibly to the cell. This process is accompanied by a large conformational change in the baseplate from a "high-energy" dome-to a "low-energy" star-shaped structure (9, 10), although each of these structures represent an energy minimum in the energy landscape of the baseplate assembly. This change triggers contraction of the tail sheath, driving the tail tube into the outer host cell membrane and further across the periplasmic space to the inner membrane. The genomic DNA is then ejected into the host's cytoplasm. Hence, the base...

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“…After the individual wedges have assembled, six wedges assemble around the central hub (12) to form the dome-shaped baseplate ( Fig. 4B and Movie S2).…”

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

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Role of bacteriophage T4 baseplate in regulating assembly and infection

Yap

Klose

Arisaka

et al. 2016

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

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“…gp15 has been shown to interact with the neck protein gp14, the tail tube terminator (gp3), and the last row of gp18 molecules. In the contracted tail, the last interaction helps to maintain the integrity of the tail in its contracted form (72). Taken together, the data on the analysis of ArV1 structural proteins presented in the previous section and summarized in Table 3 indicate that while the myophage ArV1 does, in fact, share certain components with the tails of the 3 most-researched myoviruses, T4, P2, and Mu, the inner core of the ArV1 tail is much more related to the Siphoviridae family.…”

Section: Arthrobacter Myovirus Vb_artm-arv1mentioning

confidence: 99%

Molecular Analysis of Arthrobacter Myovirus vB_ArtM-ArV1: We Blame It on the Tail

Kalinienė

Šimoliūnas

Truncaitė

et al. 2017

J Virol

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This is the first report on a myophage that infects Arthrobacter. A novel virus, vB_ArtM-ArV1 (ArV1), was isolated from soil using Arthrobacter sp. strain 68b for phage propagation. Transmission electron microscopy showed its resemblance to members of the family Myoviridae: ArV1 has an isometric head (ϳ74 nm in diameter) and a contractile, nonflexible tail (ϳ192 nm). Phylogenetic and comparative sequence analyses, however, revealed that ArV1 has more genes in common with phages from the family Siphoviridae than it does with any myovirus characterized to date. The genome of ArV1 is a linear, circularly permuted, double-stranded DNA molecule (71,200 bp) with a GC content of 61.6%. The genome includes 101 open reading frames (ORFs) yet contains no tRNA genes. More than 50% of ArV1 genes encode unique proteins that either have no reliable identity to database entries or have homologues only in Arthrobacter phages, both sipho-and myoviruses. Using bioinformatics approaches, 13 ArV1 structural genes were identified, including those coding for head, tail, tail fiber, and baseplate proteins. A further 6 ArV1 ORFs were annotated as encoding putative structural proteins based on the results of proteomic analysis. Phylogenetic analysis based on the alignment of four conserved virion proteins revealed that Arthrobacter myophages form a discrete clade that seems to occupy a position somewhat intermediate between myo-and siphoviruses. Thus, the data presented here will help to advance our understanding of genetic diversity and evolution of phages that constitute the order Caudovirales. IMPORTANCE Bacteriophages, which likely originated in the early Precambrian Era, represent the most numerous population on the planet. Approximately 95% of known phages are tailed viruses that comprise three families: Podoviridae (with short tails), Siphoviridae (with long noncontractile tails), and Myoviridae (with contractile tails). Based on the current hypothesis, myophages, which may have evolved from siphophages, are thought to have first emerged among Gram-negative bacteria, whereas they emerged only later among Gram-positive bacteria. The results of the molecular characterization of myophage vB_ArtM-ArV1 presented here conform to the aforementioned hypothesis, since, at a glance, bacteriophage vB_ArtM-ArV1 appears to be a siphovirus that possesses a seemingly functional contractile tail. Our work demonstrates that such "chimeric" myophages are of cosmopolitan nature and are likely characteristic of the ecologically important soil bacterial genus Arthrobacter.KEYWORDS Arthrobacter, Myoviridae, Siphoviridae, bacterial viruses, bacteriophage evolution, tailed viruses, vB_ArtM-ArV1

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“…The basic phage structure is made up of a hexagonal head, which harbors the phage doublestranded DNA (dsDNA), together known as capsid, a tail and a connector between head and tail ( Figure 1A) [29]. The head is anchored to a tail sheath via a neck and a collar and ends into a hexagonal base plate.…”

Section: Lytic Bacteriophage Structurementioning

confidence: 99%

Physiology and Pathology of Multidrug-Resistant Bacteria: Phage-Related Therapy

Jiang¹,

Saxena²,

Wu³

2017

Physiology and Pathology of Immunology

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Multidrug-resistant bacteria (MDR) are spreading rapidly across the world that outpace development of new antibiotics. Options other than antibiotics treatment are urgently needed. In this chapter, we review the current status of nonantibiotics-based strategies including phage therapy and phage-derived protein therapy for targeting Gram-positive strains (methicillin-resistant Staphylococcus aureus and vancomycin-resistant Enterococcus faecium) and MDR Gram-negative strains (Acinetobacter baumannii and Pseudomonas aeruginosa).

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Structure and Function of Bacteriophage T4

Cited by 131 publications

References 143 publications

Role of bacteriophage T4 baseplate in regulating assembly and infection

Role of bacteriophage T4 baseplate in regulating assembly and infection

Molecular Analysis of Arthrobacter Myovirus vB_ArtM-ArV1: We Blame It on the Tail

Physiology and Pathology of Multidrug-Resistant Bacteria: Phage-Related Therapy

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