NDLI: Phage display of intact domains at high copy number: a system based on SOC, the small outer capsid protein of bacteriophage T4.

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Phage display of intact domains at high copy number: a system based on SOC, the small outer capsid protein of bacteriophage T4.

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Year: 1996 Volume: 5 Issue: 8

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Year: 1996 Volume: 5 Issue: 5

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Year: 1996 Volume: 5 Issue: 2

Year: 1996 Volume: 5 Issue: 1

Phage display of intact domains at high copy number: a system based on SOC, the small outer capsid protein of bacteriophage T4.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Black, L. W. Steven, A. C. Wingfield, P. T. Locke, E. G. Ren, Z. J. Lewis, G. K.
Description	Country affiliation: United States Author Affiliation: Ren ZJ ( Department of Biological Chemistry, University of Maryland School of Medicine, Baltimore 21201, USA.)
Abstract	Peptides fused to the coat proteins of filamentous phages have found widespread applications in antigen display, the construction of antibody libraries, and biopanning. However, such systems are limited in terms of the size and number of the peptides that may be incorporated without compromising the fusion proteins' capacity to self-assemble. We describe here a system in which the molecules to be displayed are bound to pre-assembled polymers. The polymers are T4 capsids and polyheads (tubular capsid variants) and the display molecules are derivatives of the dispensable capsid protein SOC. In one implementation, SOC and its fusion derivatives are expressed at high levels in Escherichia coli, purified in high yield, and then bound in vitro to separately isolated polyheads. In the other, a positive selection vector forces integration of the modified soc gene into a soc-deleted T4 genome, leading to in vivo binding of the display protein to progeny virions. The system is demonstrated as applied to C-terminal fusions to SOC of (1) a tetrapeptide; (2) the 43-residue V3 loop domain of gp120, the human immunodeficiency virus type-1 (HIV-1) envelope glycoprotein; and (3) poliovirus VP1 capsid protein (312 residues). SOC-V3 displaying phage were highly antigenic in mice and produced antibodies reactive with native gp120. That the fusion protein binds correctly to the surface lattice was attested in averaged electron micrographs of polyheads. The SOC display system is capable of presenting up to approximately 10(3) copies per capsid and > 10(4) copies per polyhead of V3-sized domains. Phage displaying SOC-VP1 were isolated from a 1:10(6) mixture by two cycles of a simple biopanning procedure, indicating that proteins of at least 35 kDa may be accommodated.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	9
Volume Number	5
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1996-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Antigens, Viral Immunology Bacteriophage T4 Capsid Animals Chemistry Metabolism Genetics Capsid Proteins Escherichia Coli Gene Expression Genetic Vectors Hiv Envelope Protein Gp120 Mice Mice, Inbred Balb C Recombinant Fusion Proteins Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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Phage display of intact domains at high copy number: a system based on SOC, the small outer capsid protein of bacteriophage T4.

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Phage display of intact domains at high copy number: a system based on SOC, the small outer capsid protein of bacteriophage T4.

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Phage display of intact domains at high copy number: a system based on SOC, the small outer capsid protein of bacteriophage T4.