Structure of the cell-puncturing device of bacteriophage T4

Kanamaru, Shuji; Leiman, P.G.; Kostyuchenko, V.A.; Chipman, Paul R.; Mesyanzhinov, Vadim V.; Arisaka, Fumio; Rossmann, Michael G.

doi:10.1038/415553a

Cited by 353 publications

(358 citation statements)

References 17 publications

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“…In this article, we present evidence that the V. cholerae T6SS likely builds a structure that is predicted to be similar to the tail spike protein complex of the E. coli bacteriophage T4 (24). One of the proteins predicted to be in the T6SS complex (VgrG-1) encodes an enzyme that covalently cross-links host cell actin, and we show here that it is responsible for T6SS-dependent macrophage cytotoxicity.…”

mentioning

confidence: 94%

Type VI secretion system translocates a phage tail spike-like protein into target cells where it cross-links actin

Pukatzki

Revel

et al. 2007

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

632

879

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Genes encoding type VI secretion systems (T6SS) are widely distributed in pathogenic Gram-negative bacterial species. In Vibrio cholerae, T6SS have been found to secrete three related proteins extracellularly, VgrG-1, VgrG-2, and VgrG-3. VgrG-1 can covalently cross-link actin in vitro, and this activity was used to demonstrate that V. cholerae can translocate VgrG-1 into macrophages by a T6SS-dependent mechanism. Protein structure search algorithms predict that VgrG-related proteins likely assemble into a trimeric complex that is analogous to that formed by the two trimeric proteins gp27 and gp5 that make up the baseplate ''tail spike'' of Escherichia coli bacteriophage T4. VgrG-1 was shown to interact with itself, VgrG-2, and VgrG-3, suggesting that such a complex does form. Because the phage tail spike protein complex acts as a membrane-penetrating structure as well as a conduit for the passage of DNA into phage-infected cells, we propose that the VgrG components of the T6SS apparatus may assemble a ''cellpuncturing device'' analogous to phage tail spikes to deliver effector protein domains through membranes of target host cells.bacteriophage ͉ cytotoxicity ͉ Vibrio cholerae ͉ virulence

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mentioning

confidence: 94%

Type VI secretion system translocates a phage tail spike-like protein into target cells where it cross-links actin

Pukatzki

Revel

et al. 2007

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

632

879

View full text Add to dashboard Cite

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“…HHpred also predicted that the ORF71 protein shares structural similarity (98% similarity) with a prophage MUSO2 43-kDa tail protein (PDB 3CDD). This protein is structurally similar to phage T4 gp27 (50), to lactococcal phage p2 ORF16 protein (49), to SPP1 gp21 (51), and to TP901-1 Tal (ORF47 protein) (52). According to these predicted similarities, we then fit the phage p2 Dit-Tal complex (ORF15-ORF16) (49), a 1/1 assembly of Dit hexamer and Tal trimer, in the EM density of the Araucaria HAD ( Fig.…”

Section: Genome Characteristics Of Mycobacteriophagementioning

confidence: 99%

The First Structure of a Mycobacteriophage, the Mycobacterium abscessus subsp. bolletii Phage Araucaria

Sassi

Bebeacua

Drancourt

et al. 2013

J Virol

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The unique characteristics of the waxy mycobacterial cell wall raise questions about specific structural features of their bacteriophages. No structure of any mycobacteriophage is available, although ϳ3,500 have been described to date. To fill this gap, we embarked in a genomic and structural study of a bacteriophage from Mycobacterium abscessus subsp. bolletii, a member of the Mycobacterium abscessus group. This opportunistic pathogen is responsible for respiratory tract infections in patients with lung disorders, particularly cystic fibrosis. M. abscessus subsp. bolletii was isolated from respiratory tract specimens, and bacteriophages were observed in the cultures. We report here the genome annotation and characterization of the M. abscessus subsp. bolletii prophage Araucaria, as well as the first single-particle electron microscopy reconstruction of the whole virion. Araucaria belongs to Siphoviridae and possesses a 64-kb genome containing 89 open reading frames (ORFs), among which 27 could be annotated with certainty. Although its capsid and connector share close similarity with those of several phages from Gram-negative (Gram ؊ ) or Gram ؉ bacteria, its most distinctive characteristic is the helical tail decorated by radial spikes, possibly host adhesion devices, according to which the phage name was chosen. Its host adsorption device, at the tail tip, assembles features observed in phages binding to protein receptors, such as phage SPP1. All together, these results suggest that Araucaria may infect its mycobacterial host using a mechanism involving adhesion to cell wall saccharides and protein, a feature that remains to be further explored.

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“…58 GpD belongs to the same protein domain family (pfam05954: Phage_GPD) as Mu gp44, which forms a trimer with an overall structure like that of the T4 gp27 trimer that forms the central hub of the T4 baseplate. 64,65 Control of late gene expression P2 late promoters share a conserved DNA sequence that is centered 55 base pairs upstream of the transcription start 66,67 and required for late gene expression. 68,69 These sequences are recognized and bound by the 72 amino acid P2 Ogr protein, a zinc-binding transcription factor 70 which interacts with the C-terminal domain of the a subunit of E. coli RNA polymerase to stimulate late transcription.…”

Section: The Lysis Genesmentioning

confidence: 99%