Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • On the Market
  • Published:

Selectively infective phage (SIP) technology: A novel method for in vivo selection of interacting protein–ligand pairs

This is a preview of subscription content, access via your institution

Access options

Buy this article

Prices may be subject to local taxes which are calculated during checkout

References

  1. Krebber, C., Moroney, S., plückthun, A. & schneider, C. European Patent Application EP 93102484 (1993).

  2. Duenas, M. & Borrebaeck, C.A.K. Clonal selection and amplification of phage displayed antibodies by linking antigen recognition and phage replication. Bio/Technology 12, 999–1002 (1994).

    Article  CAS  Google Scholar 

  3. Gramatikoff, K., Ceorgiev, O. & schaffner, W. Direct interaction rescue, a novel filamentous phage technique to study protein–protein interactions. Nucleic Acids Res. 22, 5761–5762 (1994).

    Article  CAS  Google Scholar 

  4. Krebber, C., Spada, S., Desplancq, D. & Plückthun, A. Co-selection of cognate antibody–antigen pairs by selectively-infective phages. FEBS Let. 377, 227–231 (1995).

    Article  CAS  Google Scholar 

  5. Duenas, M., Malmborg, A.-C., Casalvilla, R., Ohlin, M. & Borrebaeck, C.A.K. Selection of phage displayed antibodies based on kinetic constants. Mol. Immunol. 33, 279–285 (1996).

    Article  CAS  Google Scholar 

  6. Krebber, C. et al. Selectively-infective phage (SIP): A mechanistic dissection of a novel in vivo selection for protein–ligand interactions. J. Mol. Biol. 268, 619–630 (1997).

    Article  Google Scholar 

  7. Gramatikoff, K., Schaffner, W. & Georgiev, O. The leucine-zipper of c-Jun binds to ribosomal protein L18a: A role in Jun protein regulation? Biol. Chem. 376, 321–325 (1995).

    CAS  Google Scholar 

  8. Duenas, M. et al. In vitro immunization of naive human B cells yields high affinity immunoglobulin G antibodies as illustrated by phage display. Immunology 89, 1–7 (1996).

    Article  CAS  Google Scholar 

  9. Smith, G.P. Filamentous fusion phage: Novel expression vectors that display cloned antigens on the virion surface. Science 228, 1315–1317 (1985).

    Article  CAS  Google Scholar 

  10. Dunn, I.S. Phage display of proteins. Current Opin. Biotechnol. 7, 547–553 (1996).

    Article  CAS  Google Scholar 

  11. Adey, N.B., Mataragnon, A.H., Rider, J.E., Carter, J.M. & Kay, B.K. Characterization of phage that bind plastic from phage-displayed random peptide libraries. Gene 156, 27–31 (1995).

    Article  CAS  Google Scholar 

  12. Stengele, I., Bross, P., Garces, X., Giray, J. & Rasched, I. Dissection of functional domains in phage fd adsorption protein. J. Mol. Biol. 212, 143–149 (1990).

    Article  CAS  Google Scholar 

  13. Crameri, R. & Suter, M. Display of biologically active proteins on the surface of filamentous phages: cDNA cloning system for selection of functional gene products linked to the genetic information responsible for their production. Gene 137, 69–75 (1993).

    Article  CAS  Google Scholar 

  14. Bai, C. & Elledge, S.J. Gene identification using the yeast two-hybrid system. Methods Enzymol. 273, 331–347 (1996).

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Spada, S., Plückthun, A. Selectively infective phage (SIP) technology: A novel method for in vivo selection of interacting protein–ligand pairs. Nat Med 3, 694–696 (1997). https://doi.org/10.1038/nm0697-694

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1038/nm0697-694

This article is cited by

Search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing