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Functional principle of Hyperphage Zoom

Functional principle of Hyperphage

Hyperphage M13 K07ΔpIII (5x2mL)

Provides helper phage function in packaging a common phage display phagemid. Infection of bacteria via pIII.

Discover more about the hyperphage system here.

Cat. No.: PRHYPE
Quantity:  5 x 2 mL (lyoph.)

Delivery Time: usually 1-7 working days

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Cat. No. Product Name Format Quantity Price

Hyperphage M13 K07ΔpIII (1x2mL)

2 mL (lyoph.)
Excl. VAT, excl. Shipping Cost

Product description

Purity PEG precipitation
Packing unit 5x2 mL (lyoph.)



An Effective Tool for the Isolation of Recombinant Antibodies, Proteins or Peptides from Hyperphage-Packed Libraries.


  • increases panning efficiency
  • allows panning with reduced amount of panning antigen
  • identifies high and low affinity binders


A helper phage technology ("Hyperphage System") was developed by Rondot et al. (Nature Biotechnology 19:75-81, 2001). The Hyperphage System allows to improve antibody presentation in phage display by increasing the number of antibodies displayed per phage particle (up to 5 vs. 0.01) and thereby the system offers great advantage in the fields of functional gene analysis and proteomics. Panning of phages can be performed with small amounts of antigen and higher efficiency. For example, the application of universal libraries for antibody isolation can be improved by employing panning of hyperphage-packed libraries on blots of protein spots after 2-dimensional gel electrophoresis.

More Applications

Large numbers of open reading frames (ORFs) can be analyzed by panning against synthetic membrane- bound peptide epitopes. In cancer research, the hyperphage-packed library could be a tool to discover new tumour markers by panning against cellular surfaces.

The Hyperphage System

Hyperphages carry a deletion in the pIII gene. They are generated by an E. coli packaging cell line producing functional pIII which is used to package a phage genome with a pIII deletion. The resulting hyperphages carry functional pIII on their surface but lack the pIII gene in their genome. These hyperphages can then be used to infect bacteria with a phagemid library. Each of the resulting display phages carries several copies of the antibody or peptide on its surface, thus dramatically increasing panning efficiency.

Example with pSEX Phagemid Antibody Gene Library

Antigen binding was enhanced by more than two orders of magnitude by using hyperphage. Further, since the antibody carrying plasmid (phagemid) encodes a protease cleavage site between pIII and scFv fragment, the hyperphage-packed library can be eluted by protease treatment, allowing to elute the highest affinity binders, plus restoring wild-type infectivity phenotype to optimize the recovery of the antibody gene of interest.



Original papers on successful use of hyperphage

Zantow, J. et al. Mining gut microbiome oligopeptides by functional metaproteome display. Sci. Rep. 6, 1–13 (2016).Zantow, J. et al. Mining gut microbiome oligopeptides by functional metaproteome display. Sci. Rep. 6, 1–13 (2016).

Connor, D. O., Zantow, J., Hust, M., Bier, F. F. & von Nickisch-Rosenegk, M. Identification of Novel Immunogenic Proteins of Neisseria gonorrhoeae by Phage Display. PLoS One 11, e0148986 (2016).

Miethe, S. et al. Development of Germline-Humanized Antibodies Neutralizing Botulinum Neurotoxin A and B. PLoS One 11, e0161446 (2016).

Blokzijl, A. et al. Single Chain Antibodies as Tools to Study transforming growth factor-β-Regulated SMAD Proteins in Proximity Ligation-Based Pharmacological Screens. Mol. Cell. Proteomics 15, 1848–56 (2016).

Rasetti-Escargueil, C. et al. Development of human-like scFv-Fc antibodies neutralizing Botulinum toxin serotype B. MAbs 7, 1161–77 (2015).

Miethe, S. et al. Development of Human-Like scFv-Fc Neutralizing Botulinum Neurotoxin E. PLoS One 10, e0139905 (2015).

Becker, M. et al. Application of M13 phage display for identifying immunogenic proteins from tick (Ixodes scapularis) saliva. BMC Biotechnol. 15, 43 (2015).

Avril, A. et al. Isolation of nanomolar scFvs of non-human primate origin, cross-neutralizing botulinum neurotoxins A1 and A2 by targeting their heavy chain. BMC Biotechnol. 15, 86 (2015).

Droste, P. et al. Structural differences of amyloid-β fibrils revealed by antibodies from phage display. BMC Biotechnol. 15, 57 (2015).

Kügler, J. et al. Generation and analysis of the improved human HAL9/10 antibody phage display libraries. BMC Biotechnol. 15, 10 (2015)

Hülseweh, B. et al. Human-like antibodies neutralizing Western equine encephalitis virus. MAbs 6, 718–27 (2014).

Trott, M. et al. Functional characterization of two scFv-Fc antibodies from an HIV controller selected on soluble HIV-1 Env complexes: a neutralizing V3- and a trimer-specific gp41 antibody. PLoS One 9, e97478 (2014).

Miethe, S. et al. Development of neutralizing scFv-Fc against botulinum neurotoxin A light chain from a macaque immune library. MAbs 6, 446–59 (2014).

Schirrmann, T. et al. Evaluation of human pancreatic RNase as effector molecule in a therapeutic antibody platform. MAbs 6, 367–80 (2014).

Steinwand, M. et al. The influence of antibody fragment format on phage display based affinity maturation of IgG. MAbs 6, 204–18 (2014). 

Zhou, M. et al. Identification of a new epitope for HIV-neutralizing antibodies in the gp41 membrane proximal external region by an Env-tailored phage display library. Eur. J. Immunol. 43, 499–509 (2013).

Meyer, T. et al. Identification of immunogenic proteins and generation of antibodies against Salmonella Typhimurium using phage display. BMC Biotechnol. 12, 29 (2012).

Wezler, X., Hust, M., Helmsing, S., Schirrmann, T. & Dübel, S. Human antibodies targeting CD30(+) lymphomas. Hum. Antibodies 21, 13–28 (2012).

Rülker, T. et al. Isolation and characterisation of a human-like antibody fragment (scFv) that inactivates VEEV in vitro and in vivo. PLoS One 7, e37242 (2012).

Colwill, K. et al. A roadmap to generate renewable protein binders to the human proteome. Nat. Methods 8, 551–558 (2011)

Kirsch, M. I. et al. Development of human antibody fragments using antibody phage display for the detection and diagnosis of Venezuelan equine encephalitis virus (VEEV). BMC Biotechnol. 8, 66 (2008).

Kügler, J. et al. Identification of immunogenic polypeptides from a Mycoplasma hyopneumoniae genome library by phage display. Appl. Microbiol. Biotechnol. 80, 447–458 (2008).

Pelat, T. et al. High-affinity, human antibody-like antibody fragment (single-chain variable fragment) neutralizing the lethal factor (LF) of Bacillus anthracis by inhibiting protective antigen-LF complex formation. Antimicrob. Agents Chemother. 51, 2758–64 (2007).

Soltes, G. et al. On the influence of vector design on antibody phage display. J. Biotechnol. 127, 626–37 (2007).

Hust, M. et al. Enrichment of open reading frames presented on bacteriophage M13 using Hyperphage. Biotechniques 41, 335–342 (2006).

Rondot, S., Koch, J., Breitling, F. & Dübel, S. A helper phage to improve single-chain antibody presentation in phage display. Nat. Biotechnol. 19, 75–78 (2001).



Hust M., Frenzel, A., Tomszak, F, Kügler, J & Dübel, S. (2014) Antibody Phage Display. In: Dübel, S. & Reichert, J.M. (eds.) Handbook of Therapeutic Antibodies, 2nd ed. Wiley-VCH, Weinheim, ISBN 978-3-527-32937-3 p. 43-76

Hust, M., Frenzel, A., Schirmann, T. and Dübel, S. (2014) Selection of recombinant antibodies from antibody gene libraries. Methods Mol Biol. 1101, 305-320.2

Hust, M., Frenzel, A., Meyer, T., Schirmann, T. and Dübel, S. (2012). Construction of human naive antibody gene libraries. In: Antibody Engineering: Methods and Protocols, Ed: Chames, P., Meth Mol Biol 907, 85-107

Breitling, F., Broders, O., Helmsing, S., Hust, M & Dübel, S (2010) Improving phage display throughput by using Hyperphage, miniaturised titration and pVIII (g8p) ELISA. In: Antibody Engineering (2nd ed) Springer Protocols. Vol. 1, ISBN 978-3-642-01143-6, p. 197-206

Broders, O., Breitling, F., and Dübel, S. (2003). Hyperphage - Improving Antibody Presentation in Phage Display. Methods Mol Biol 205, 295-302.


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