Bacteriophages are type of viruses that infect andkill the bacterial cells, which serve as their host with great efficacy and arepresent in all ecosystems such as land, marine, air which can support thegrowth of the bacteria itself (Elbreki M. et al, 2014). The internationalCommittee for Taxonomy of Viruses classifies phages in the order ofCaudovirales (Lavigne R. et al, 2011). Phages would have capsid which is aprotein heads, that carry and protect the genomic material of the virusesitself.
The genomic material could be varied in size and proportion,arrangement (circular, linear, segmented) and structure (single stranded DNAssDNA, double stranded DNA dsDNA, single stranded RNA ssRNA, double strandedRNA dsRNA) (Ackermann H, 2007). The true discoverer of bacteriophages is quitecontested issue between two persons (Felix d’Herelle and Frederick Twort in theearly 20th century) (Sulakvelidze A. et al, 2001) (Duckworth D., 1976),d’Herelle is presently considered and called as the father of appliedbacteriophage science since Twort did not pursue his discoveries more further(Bragg R.
R. et al). During his time, he was the person responsible forproposing the name of bacteriophage, a combination of bacteria and phagein,which means ‘to eat’ in Greek (Bragg R.R. et al).
Structural and functional studies on protein proteinswould require production of sufficient quantities of protein needed and usuallyin milligram quantities which is relatively so small. This is small scale wouldbe as the first essential step. The natural expression levels of many proteins,especially membrane proteins (Bernaudat F. et al, 2011) are frequently too lowand therefore an amplified expression of recombinant proteins must be achievedaccording to Irshad Ahmad and others, 2017.
Several characteristics of Escherichia coli such as easy accessibility,genetic manipulation and handling are the most preferred and most widely usedorganism for amplifying the expression of recombinant proteins and includingmembrane proteins (Henderson P. et al, 2000). In theory according to IrshadAhmad and others, 2017, when we are using Escherichia coli, the recombinantprotein production is relatively straightforward in which beginning with target identification,cloning of the wanted gene into an appropriate vector, transformation of the competenthost cells, suitable strain using the set of construct earlier, induction foramplified expression at the start of the promoter and then protein purificationand characterization by using sequencing, purity, structural integrity,stability and the activity of the proteins. Various biocombinatorial peptidelibraries by assessing phage display technique, bacterial and yeast displayhave been utilized to identify the peptides that can interact with inorganicsurfaces. The presence of a small peptide tag such as hexa – histidine at the C– terminal or N – terminal end of the recombinant protein allows the specificbinding to immobilized bivalent metal ions as stated by Porath J. et al, 1975and Wong J.H.
et al 2012. Phage display is a kind of technology that intended toexpress foreign proteins or peptides as phage capsid fusion proteins so thatthe surface – displayed proteins can be physically linked to their c DNAinserts inside the same phage particles. It will need multi round phage selectionand enrichment and also amplification efficiently to enrich the clonesdisplaying the proteins with specific binding or functional activities (Kehoe J.W.et al, 2005 and Paschke M., 2006). Since its first discovery in 1985, phage displayhas been widely used to identify antibodies or short peptides with specific bindingactivities from antibody libraries or random peptide libraries (Pande J.
et al,1985 and Smith G.P., 1985)