Origin and function of the two major tail proteins of bacteriophage SPP1

Auzat, Isabelle; Dröge, Anja; Weise, Frank; Lurz, Rudi; Tavares, Paulo

doi:10.1111/j.1365-2958.2008.06435.x

Cited by 47 publications

(102 citation statements)

References 43 publications

(68 reference statements)

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“…It is likely that the exceeding ϳ190 MTP residues form Araucaria's tail protrusions. Such protrusions were already reported for phage and phage SPP1 (62,63). In phage , the MTP (gpV) counts 246 amino acids.…”

Section: Discussionmentioning

confidence: 81%

“…The N-terminal domain (gpV N 1-159) forms the MTP rings (64), while residues 160 to 246 (gpV C ) belong to an Ig-like domain, probably involved with host cell wall saccharide interactions (63). In SPP1, the MTP-coding gene (orf17.1) is subject to a frameshift alternative reading, leading either to an MTP of 159 residues, the core, or to a longer form of 266 residues (62). Here again, the additional domain has a fold of an adhesin, probably involved in saccharide binding.…”

Section: Discussionmentioning

confidence: 99%

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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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Section: Discussionmentioning

confidence: 81%

Section: Discussionmentioning

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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“…1,600-Å-long helical tail to the connector completes the formation of the HTI (7,16). The capsid-distal region of the tail features an adsorption apparatus.…”

mentioning

confidence: 99%

“…The capsid-distal region of the tail features an adsorption apparatus. Binding of this apparatus to the host cell receptor YueB (17, 18) triggers a domino-like cascade of conformational changes within the gp17.1/gp17.1* tail tube (7,16,19), signaling for opening of the gp16 stopper to initiate delivery of the SPP1 genome to the host cell.…”

mentioning

confidence: 99%

Structural rearrangements in the phage head-to-tail interface during assembly and infection

Chaban

Lurz

Brasilès

et al. 2015

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

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Many icosahedral viruses use a specialized portal vertex to control genome encapsidation and release from the viral capsid. In tailed bacteriophages, the portal system is connected to a tail structure that provides the pipeline for genome delivery to the host cell. We report the first, to our knowledge, subnanometer structures of the complete portal-phage tail interface that mimic the states before and after DNA release during phage infection. They uncover structural rearrangements associated with intimate protein-DNA interactions. The portal protein gp6 of bacteriophage SPP1 undergoes a concerted reorganization of the structural elements of its central channel during interaction with DNA. A network of protein-protein interactions primes consecutive binding of proteins gp15 and gp16 to extend and close the channel. This critical step that prevents genome leakage from the capsid is achieved by a previously unidentified allosteric mechanism: gp16 binding to two different regions of gp15 drives correct positioning and folding of an inner gp16 loop to interact with equivalent loops of the other gp16 subunits. Together, these loops build a plug that closes the channel. Gp16 then fastens the tail to yield the infectious virion. The gatekeeper system opens for viral genome exit at the beginning of infection but recloses afterward, suggesting a molecular diaphragm-like mechanism to control DNA efflux. The mechanisms described here, controlling the essential steps of phage genome movements during virus assembly and infection, are likely to be conserved among long-tailed phages, the largest group of viruses in the Biosphere.DNA gatekeeper | viral infection | bacteriophage | allosteric mechanism | hybrid methods

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“…The tail of Bacillus subtilis phage SPP1 includes two TTPs, gp17.1 (19.1 kDa) and gp17.1* (28.3 kDa), that share a common N-terminal sequence (11). A programmed translational frameshift of gene 17.1 leads to the production of gp17.1*, which contains an additional C-terminal domain as compared with gp17.1.…”

mentioning

confidence: 99%