T4 Phage Display Library Construction on HOC & SOC Dual Display

As a long-term expert in delivering a full range of comprehensive services based on phage display technology, Creative Biolabs keeps paving the way to revolutionary scientific progress. Currently, we proudly introduce this novel dual display service through bipartite fusions to HOC and SOC of bacteriophage T4 to our global clients.

Phage display is an exponentially growing research area, which is being frequently applied in fields like immunology, cell biology, drug discovery and pharmacology. Molecules of interest, such as protein, peptide, and cDNA, can be displayed on the phage surface by genetically fusing to capsid proteins. In this way, a direct linkage between genotype and phenotype can be built up for further screening and analysis. Although filamentous phage display has always been a dominant choice and extensively utilized over decades, T4 phage display system recently emerges as a powerful approach for its unparalleled advantages.

Phage display platform based on bacteriophage T4 majorly employs two non-essential capsid proteins: HOC (39.1 kDa, 155 copies) and SOC (9 kDa, 810 copies). They are dispensable for capsid assembly and decorated into the phage particle during the last stage of maturation. Distinct from other structural capsids, HOC and SOC have no impact on the infectivity or viability of phage T4, hence confirmation changes of recombinant capsids due to foreign domain insertions will not interfere the phage assembly. On the other hand, because of the lytic life cycle of T4, progeny phages are assembled in the host cytoplasm and released by lysis of the cell envelope, avoiding the membrane extraction procedure which might cause host toxicity and protein misfolding.

T4 phage display platform using either HOC or SOC site has proved a great success in displaying large full-length proteins with considerate bioactivities, such as an antigen, antibody, receptor, enzyme, and so on. Here we present an exclusive HOC-SOC bipartite display system, which is able to simultaneously exhibit two different proteins on the T4 capsid surface. This novel platform has revealed tremendous potential for a variety of applications:

Antibody/peptide library construction: bacteriophage T4 is able to provide multiple choices of display site, each of which can tolerate large insertions and preserve intact confirmation. Up to 40 full-length and active IgG and CD4 receptor proteins have been successfully displayed per phage. Therefore, bipartite antibody/peptide libraries can ensure unparalleled capacity as well as considerate bioactivity for isolation of impeccable products with specific properties.
Protein-protein interactions: by dual-site display technique, we can design repertoires of ligands from scratches and study the biological characters of indicated domains using affinity selection. It is an attractive approach for discovering cytokine receptor agonists/inhibitors, drug receptor agonists/inhibitors, ligand binding site/active domain identification, etc.
Immunogen preparation: compared to single site display, HOC-SOC bipartite phage display constructs are proved to exhibit stronger immunogenicity both in vitro and in vivo, implying extensive potential to enhance the immunogenicity of bio-engineered proteins. Hence, this dual display system is well suitable for immunogen preparation, such as phage-based vaccine design and diagnosis kit development.

With state-of-the-art technologies and seasoned team of experts, Creative Biolabs is professional in delivering high-quality service based on our innovative dual-display platform. Our scientists are pleased to promise precisely tailored and goal-oriented protocols according to assist our customers’ specific research objectives.

Fig 1. Head structure of bacteriophage T4 (Fokine et al. 2011)

Reference

Fokine, A., Islam, M. Z., Zhang, Z., Bowman, V. D., Rao, V. B. and Rossmann, M. G. (2011) 'Structure of the three N-terminal immunoglobulin domains of the highly immunogenic outer capsid protein from a T4-like bacteriophage', Journal of virology, 85(16), 8141-8148.

All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.

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