Analysis of the coliphage T5 DNA ejection process with free and liposome-associated TonA protein

Tosi, Francesca; Labedan, Bernard; Legault-Démare, J

doi:10.1128/jvi.50.1.213-219.1984

Cited by 11 publications

(6 citation statements)

References 21 publications

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“…Addition of T5 to the trans chamber, 15 min after the addition of FhuA to the cis chamber, did not modify the permeability of the membrane, suggesting that FhuA is incorporated into the lipid bilayer in only one orientation. Phage DNA ejection is temperature dependent (Tosi et al, 1984;Boulanger and Letellier, 1992;Killmann et al, 1995). However, channel activity of the FhuA-T5 complex was not significantly different when experiments were performed at 28°C instead of 20°C (data not shown).…”

Section: Resultsmentioning

confidence: 92%

FhuA, a transporter of the Escherichia coli outer membrane, is converted into a channel upon binding of bacteriophage T5.

et al. 1996

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The Escherichia coli outer membrane protein FhuA catalyzes the transport of Fe3+(‐)ferrichrome and is the receptor of phage T5 and phi 80. The purified protein inserted into planar lipid bilayers showed no channel activity. Binding of phage T5 and FhuA resulted in the appearance of high conductance ion channels. The electrophysiological characteristics of the channels (conductance, kinetic behavior, substates, ion selectivity including the effect of ferrichrome) showed similarities with those of the channel formed by a FhuA derivative from which the ‘gating loop’ (delta 322–355) had been removed. binding of phage T5 to FhuA in E.coli cells conferred SDS sensitivity to the bacteria, suggesting that such channels also exist in vivo. These data suggest that binding of T5 to loop 322–355 of FhuA, which constitutes the T5 binding site, unmasks an inner channel in FhuA. Both T5 and ferrichrome bind to the closed state of the channel but only T5 can trigger its opening.

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Section: Resultsmentioning

confidence: 92%

FhuA, a transporter of the Escherichia coli outer membrane, is converted into a channel upon binding of bacteriophage T5.

et al. 1996

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“…LS buffer was initially preferred for spermine addition because it was expected to maximize spermine effect. Since no difference in CD spectra was detected at 4 or 40 mM spermine (Figure A), HS buffer has been chosen for subsequent measurements because DNA release from T5, triggered by interaction of the phage with its receptor FhuA, requires HS conditions …”

Section: Resultsmentioning

confidence: 99%

“…For phage T5, DNA can be released from the phage by mixing the phage with its protein receptor FhuA. , This property allows us to measure CD spectra in full T5 (phages with confined DNA) and in empty T5 (phages with released DNA around). The comparison with purified DNA (DNA alone) is presented in Figure B.…”

Section: Resultsmentioning

confidence: 99%

Can Changes in Temperature or Ionic Conditions Modify the DNA Organization in the Full Bacteriophage Capsid?

et al. 2016

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We compared four bacteriophage species, T5, λ, T7, and Φ29, to explore the possibilities of DNA reorganization in the capsid where the chain is highly concentrated and confined. First, we did not detect any change in DNA organization as a function of temperature between 20 to 40 °C. Second, the presence of spermine (4+) induces a significant enlargement of the typical size of the hexagonal domains in all phages. We interpret these changes as a reorganization of DNA by slight movements of defects in the structure, triggered by a partial screening of repulsive interactions. We did not detect any signal characteristic of a long-range chiral organization of the encapsidated DNA in the presence and in the absence of spermine.

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“…Control of DNA exit from the virion during infection is important because after irreversible binding to the bacterial surface the phage must deal with crossing the bacterial cell wall and membrane(s) before delivering DNA to the cytoplasm. Phage binding to bacterial surface receptors is sufficient to trigger DNA ejection (Zarybnicky and Zarybnicka, 1973; Tosi et al ., 1984; São‐José et al ., 2006). Therefore, a strict co‐ordination of events is required between this interaction and the stage at which conditions are established to ensure correct routing of DNA to the cytoplasm.…”

Section: Discussionmentioning

confidence: 99%

The minor capsid protein gp7 of bacteriophage SPP1 is required for efficient infection of Bacillus subtilis

Vinga

Dröge

Stiege

et al. 2006

Molecular Microbiology

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SummaryGp7 is a minor capsid protein of the Bacillus subtilis bacteriophage SPP1. Homologous proteins are found in numerous phages but their function remained unknown. Deletion of gene 7 from the SPP1 genome yielded a mutant phage (SPP1del7) with reduced burst-size. SPP1del7 infections led to normal assembly of virus particles whose morphology, DNA and protein composition was undistinguishable from wild-type virions. However, only~25% of the viral particles that lack gp7 were infectious. SPP1del7 particles caused a reduced depolarization of the B. subtilis membrane in infection assays suggesting a defect in virus genome traffic to the host cell. A higher number of SPP1del7 DNA ejection events led to abortive release of DNA to the culture medium when compared with wild-type infections. DNA ejection in vitro showed that no detectable gp7 is co-ejected with the SPP1 genome and that its presence in the virion correlated with anchoring of released DNA to the phage particle. The release of DNA from wild-type phages was slower than that from SPP1del7 suggesting that gp7 controls DNA exit from the virion. This feature is proposed to play a central role in supporting correct routing of the phage genome from the virion to the cell cytoplasm.

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Analysis of the coliphage T5 DNA ejection process with free and liposome-associated TonA protein

Cited by 11 publications

References 21 publications

FhuA, a transporter of the Escherichia coli outer membrane, is converted into a channel upon binding of bacteriophage T5.

FhuA, a transporter of the Escherichia coli outer membrane, is converted into a channel upon binding of bacteriophage T5.

Can Changes in Temperature or Ionic Conditions Modify the DNA Organization in the Full Bacteriophage Capsid?

The minor capsid protein gp7 of bacteriophage SPP1 is required for efficient infection of Bacillus subtilis

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