Interaction Analysis through Proteomic Phage Display

Abstract

Phage display is a powerful technique for profiling specificities of peptide binding domains. The method is suited for the identification of high-affinity ligands with inhibitor potential when using highly diverse combinatorial peptide phage libraries. Such experiments further provide consensus motifs for genome-wide scanning of ligands of potential biological relevance. A complementary but considerably less explored approach is to display expression products of genomic DNA, cDNA, open reading frames (ORFs), or oligonucleotide libraries designed to encode defined regions of a target proteome on phage particles. One of the main applications of such proteomic libraries has been the elucidation of antibody epitopes. This review is focused on the use of proteomic phage display to uncover protein-protein interactions of potential relevance for cellular function. The method is particularly suited for the discovery of interactions between peptide binding domains and their targets. We discuss the largely unexplored potential of this method in the discovery of domain-motif interactions of potential biological relevance.

Intriguing Interaction of Bacteriophage-Host Association: An Understanding in the Era of Omics

“…Structural proteomics can interpret the structure of proteins thereby determining the functions of novel genes. Lavigne et al (2006) described structural proteome of phiKMV, a lytic bacteriophage of Pseudomonas aeruginosa using SDS-PAGE, LC-ESI-MS/MS, and GC-MS. Nuclear magnetic resonance (NMR) (Horgan and Kenny, 2011) and X-ray crystallography (Drulis-Kawa et al, 2012) can be employed to investigate the interaction between phage-binding protein and receptor site on the bacterial host (Sundell and Ivarsson, 2014). …”

“…MS/MS spectra can be interpreted using SEQUEST (http://fields.scripps.edu/sequest/) or Mascot (Matrix Sciences) and classifying using DTASelect and Contrast softwares (Tabb et al, 2002). Proteomic phage display techniques are similarly employed to identify target proteins and consensus motifs (Sundell and Ivarsson, 2014). Whole phage shotgun analysis (WSA) is a recently developed technique for protein analysis using NGS platform.…”

Bacteriophages and their derivatives for the treatment and control of food-producing animal infections

“…The T4 phage allows the display of large peptides on its capsid proteins, Soc (small outer capsid protein; 960 copies per particle) and Hoc (highly antigenic outer capsid protein; 160 copies per particle) (Li et al, 2006). In the T7 phage, the fusion proteins are displayed on protein 10B (5-15 copies) of the major phage capsid (gp10), and in the lambda phage both the tail protein gpV (at least 5 copies) and the head protein gpD (405-420 copies) have been used for displaying foreign peptides (Sundell & Ivarsson, 2014). The M13 phage is a highly versatile system as distinct coat proteins can be used for peptide display.…”

“…The M13 phage is a highly versatile system as distinct coat proteins can be used for peptide display. Commonly, the pIII protein is used for low valency display (1-5 copies per phage) and the pVIII for high valency display (up to 1000 copies per phage) (Sundell & Ivarsson, 2014).…”

Phage-displayed peptides that mimic epitopes of hepatitis E virus capsid

“…Several studies has shown that phage display can be an important tool for epitope mapping, the development of vaccines, therapeutic drugs, diagnostic reagents, as well as in proteomic studies [31][32][33][34][35]. This technique is very useful to study viruses which do not replicate efficiently in tissue culture like HEV [36].…”