Co-selection of cognate antibody-antigen pairs by selectively-infective phages.
We have developed a chloramphenicol resistant derivative of fd phage with which cognate pairs of antibodies and antigens can be selected. The phage genome encodes a fusion of single-chain antibody to the C-terminal domain of gIIIp, rendering the phage non-infective. The antigen fused to the N-terminal domains of gIIIp is encoded in the same phage genome. Antigen and antibody fusion interact with each other in the periplasm of the phage-producing cell, restoring infectivity. This system has a very low background and will allow simultaneous randomisation of antibody and antigen.
Biochemisches Institut, Universität Zürich, Switzerland.
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Krebber
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Spada
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Desplancq
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Plückthun
D000595:Amino Acid Sequence; D000936:Antigen-Antibody Complex / Q000235:genetics / Q000276:immunology*; D036022:Capsid Proteins; D002701:Chloramphenicol; D004268:DNA-Binding Proteins / Q000235:genetics / Q000276:immunology* / Q000378:metabolism; D005822:Genetic Vectors; D016679:Genome, Viral; D007128:Immunoglobulin Fragments / Q000235:genetics / Q000276:immunology; D017912:Inovirus / Q000235:genetics* / Q000276:immunology; D008969:Molecular Sequence Data; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000276:immunology; D014760:Viral Fusion Proteins; D014764:Viral Proteins / Q000235:genetics / Q000276:immunology* / Q000378:metabolism
D000936:Antigen-Antibody Complex; D036022:Capsid Proteins; D004268:DNA-Binding Proteins; D007128:Immunoglobulin Fragments; D011993:Recombinant Fusion Proteins; D014760:Viral Fusion Proteins; D014764:Viral Proteins; D002701:Chloramphenicol