Physical, Biochemical, and Immunological Properties of Coliphage MS-2 Particles

Rohrmann, George F.; Krueger, Robert G.

doi:10.1128/jvi.6.3.269-279.1970

Cited by 17 publications

(2 citation statements)

References 32 publications

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“…capsid; the capsid has been shown to sediment at about 45S and to be RNase resistant (6,17,22). The 45S structure described here is RNase insensitive, is not infectious, contains no RNA (Fig.…”

Section: S Samples Represents the Complete Phagementioning

confidence: 77%

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Intermediates of Bacteriophage MS2 Assembly In Vivo

Bonner

1974

J Virol

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The in vivo process of virion assembly was studied in rifampin-treated, MS2-infected Escherichia coli during late times of infection-after 18 min postinfection. Differential sucrose gradient sedimentation of infected-cell lysates taken at various times after radioactive labeling indicated a definite temporal order of appearance of phage-specific protein in assembly-related structures. Labeled MS2 protein appears first as a low-molecular-weight peak at the tops of gradients, then as a peak at 40S and as a large number of almost unseparable structures between 40 and 80S, and finally as 80S mature phage particles. During the chase of a short labeling period, radioactive phage protein was found to disappear from gradients in the same temporal order as it appeared; the soluble peak disappears first, followed by the 40 to 70S region. The chased label appears

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Section: S Samples Represents the Complete Phagementioning

confidence: 77%

“…Assembly can continue through addition of postulated coat protein capsomeres to this first intermediate. The nature of the coat protein capsomeres is not clear; they could be monomers, dimers (16,17), trimers, or even pentamers and hexamers (26). This paper is concerned with studies on the in vivo assembly process of MS2.…”

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confidence: 99%

Intermediates of Bacteriophage MS2 Assembly In Vivo

Bonner

1974

J Virol

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Escherichia coli‐based cell‐free synthesis of virus‐like particles

Bundy

Franciszkowicz

Swartz

2007

Biotech & Bioengineering

167

150

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Virus-like particles (VLP) have received considerable attention for vaccine, drug delivery, gene therapy and material science applications. Although the number of unique VLP and their applications are rapidly growing, the positive impact of VLP applications is limited by the current diverse, expensive, and typically low-yielding production technologies available. These technologies, when scaled, often result in structurally and compositionally inconsistent products. We present Escherichia coli-based cell-free protein synthesis as a production technology to overcome many of the limitations of current VLP production processes. Using this technique, the MS2 bacteriophage coat protein VLP was produced at a yield 14 times the best published production yield. Also, a C-terminally truncated Hepatitis B core protein VLP was produced at similarly high yields (6 x 10(13) VLP/mL). These VLP were found to have comparable characteristics to those produced in vivo. The scalability of this technology was tested without loss in production yields. To our knowledge, this is the first time a prokaryote-based in vitro transcription/translation system has generated a virus-like particle.

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Polyconfiguron-model for the A-protein of coliphage MS2

Quinn

1978

Biochemical and Biophysical Research Communications

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Physical, Biochemical, and Immunological Properties of Coliphage MS-2 Particles

Cited by 17 publications

References 32 publications

Intermediates of Bacteriophage MS2 Assembly In Vivo

Intermediates of Bacteriophage MS2 Assembly In Vivo

Escherichia coli‐based cell‐free synthesis of virus‐like particles

Polyconfiguron-model for the A-protein of coliphage MS2

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