Inactivation of urea-treated phage T4 by phosphatidylglycerol

Baumann, Linda C.; Benz, Wendy C.; Wright, Andrew; Goldberg, Edward B.

doi:10.1016/0042-6822(70)90088-7

Cited by 21 publications

(6 citation statements)

References 8 publications

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“…Our asymmetric reconstructions of the fusion complex are consistent with the intact gp27 trimer being sandwiched between the tail tube and the cytoplasmic membrane, but structural predictions do not reveal any propensity of gp27 to bind the likely inner membrane receptor, phosphatidylglycerol (75,76). However, the gp29 tail tape measure protein has a strongly predicted transmembrane segment near the middle of its amino acid sequence.…”

Section: Long Tail Fibers Of Rapidly Adsorbing Phage Are In Two Distinctsupporting

confidence: 50%

Structural remodeling of bacteriophage T4 and host membranes during infection initiation

Margolin²,

Molineux

et al. 2015

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

201

195

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The first stages of productive bacteriophage infections of bacterial host cells require efficient adsorption to the cell surface followed by ejection of phage DNA into the host cytoplasm. To achieve this goal, a phage virion must undergo significant structural remodeling. For phage T4, the most obvious change is the contraction of its tail. Here, we use skinny E. coli minicells as a host, along with cryo-electron tomography and mutant phage virions, to visualize key structural intermediates during initiation of T4 infection. We show for the first time that most long tail fibers are folded back against the tail sheath until irreversible adsorption, a feature compatible with the virion randomly walking across the cell surface to find an optimal site for infection. Our data confirm that tail contraction is triggered by structural changes in the baseplate, as intermediates were found with remodeled baseplates and extended tails. After contraction, the tail tube penetrates the host cell periplasm, pausing while it degrades the peptidoglycan layer. Penetration into the host cytoplasm is accompanied by a dramatic local outward curvature of the cytoplasmic membrane as it fuses with the phage tail tip. The baseplate hub protein gp27 and/or the ejected tape measure protein gp29 likely form the transmembrane channel for viral DNA passage into the cell cytoplasm. Building on the wealth of prior biochemical and structural information, this work provides new molecular insights into the mechanistic pathway of T4 phage infection.phage T4 | cryo-ET | structure | infected cell | membrane curvature

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Section: Long Tail Fibers Of Rapidly Adsorbing Phage Are In Two Distinctsupporting

confidence: 50%

Structural remodeling of bacteriophage T4 and host membranes during infection initiation

Margolin²,

Molineux

et al. 2015

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

201

195

View full text Add to dashboard Cite

show abstract

“…This irreversible binding was sensitive to temperature and required energy (14). DNase-resistant infective centers remained susceptible to shear for more than 15 min after the mixing of DNA with competent cells (155).…”

Section: Lysozyme-edta Technique-mechanismmentioning

confidence: 99%

Transfection of Enterobacteriaceae and its applications.

Benzinger¹

1978

Microbiological Reviews

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“…Since phages have to inject their DNA into the host cyto-plasm, the interaction between the core tip of phage particles with the cytoplasmic membrane is supposed to be the next important event after the core insertion. Baumann et al showed that the DNA ejection from the contracted T4 is induced by phosphatidylglycerol (1). It was also suggested that a membrane potential across the cytoplasmic membrane is required for the entry of phage DNA into the host cytoplasm (11,13).…”

mentioning

confidence: 99%

Roles of cell surface components of Escherichia coli K-12 in bacteriophage T4 infection: interaction of tail core with phospholipids

Furukawa¹,

Mizushima²

1982

J Bacteriol

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The cell surface of Escherichia coli K-12, reconstituted from the OmpC protein, lipopolysaccharide, and the peptidoglycan layer, was active as a receptor for phage T4, resulting in the contraction of the tail sheath and the penetration of the core through the cell surface (Furukawa et al., J. Bacteriol. 140:1071--1080, 1979). In the present work the process of DNA ejection from the contracted T4 phage particle was studied. Contracted phage particles were adsorbed to phospholipid liposomes by the core tip. This adsorption resulted in ejection of phage DNA. Either phosphatidylglycerol or cardiolipin was active for the DNA ejection. A proton motive force across the liposome membrane was not required for these processes. The process of DNA ejection, however, was temperature dependent, whereas the adsorption of the core tip to liposomes took place at 4 degrees C. Based on these observations together with those in the previous paper, the process of T4 infection of E. coli K-12 cells is discussed with special reference to the roles of cell surface components.

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Inactivation of urea-treated phage T4 by phosphatidylglycerol

Cited by 21 publications

References 8 publications

Structural remodeling of bacteriophage T4 and host membranes during infection initiation

Structural remodeling of bacteriophage T4 and host membranes during infection initiation

Transfection of Enterobacteriaceae and its applications.

Roles of cell surface components of Escherichia coli K-12 in bacteriophage T4 infection: interaction of tail core with phospholipids

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