Bacteriophages most widely used organism for amplifying the expression

Bacteriophages are type of viruses that infect and
kill the bacterial cells, which serve as their host with great efficacy and are
present in all ecosystems such as land, marine, air which can support the
growth of the bacteria itself (Elbreki M. et al, 2014). The international
Committee for Taxonomy of Viruses classifies phages in the order of
Caudovirales (Lavigne R. et al, 2011). Phages would have capsid which is a
protein heads, that carry and protect the genomic material of the viruses
itself. The genomic material could be varied in size and proportion,
arrangement (circular, linear, segmented) and structure (single stranded DNA
ssDNA, double stranded DNA dsDNA, single stranded RNA ssRNA, double stranded
RNA dsRNA) (Ackermann H, 2007). The true discoverer of bacteriophages is quite
contested issue between two persons (Felix d’Herelle and Frederick Twort in the
early 20th century) (Sulakvelidze A. et al, 2001) (Duckworth D., 1976),
d’Herelle is presently considered and called as the father of applied
bacteriophage science since Twort did not pursue his discoveries more further
(Bragg R.R. et al). During his time, he was the person responsible for
proposing 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 proteins
would require production of sufficient quantities of protein needed and usually
in milligram quantities which is relatively so small. This is small scale would
be as the first essential step. The natural expression levels of many proteins,
especially membrane proteins (Bernaudat F. et al, 2011) are frequently too low
and therefore an amplified expression of recombinant proteins must be achieved
according 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 used
organism for amplifying the expression of recombinant proteins and including
membrane proteins (Henderson P. et al, 2000). In theory according to Irshad
Ahmad and others, 2017, when we are using Escherichia coli, the recombinant
protein production is relatively straightforward  in which beginning with target identification,
cloning of the wanted gene into an appropriate vector, transformation of the competent
host cells, suitable strain using the set of construct earlier, induction for
amplified expression at the start of the promoter and then protein purification
and characterization by using sequencing, purity, structural integrity,
stability and the activity of the proteins. Various biocombinatorial peptide
libraries by assessing phage display technique, bacterial and yeast display
have been utilized to identify the peptides that can interact with inorganic
surfaces. 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 specific
binding to immobilized bivalent metal ions as stated by Porath J. et al, 1975
and Wong J.H. et al 2012.

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Phage display is a kind of technology that intended to
express foreign proteins or peptides as phage capsid fusion proteins so that
the surface – displayed proteins can be physically linked to their c DNA
inserts inside the same phage particles. It will need multi round phage selection
and enrichment and also amplification efficiently to enrich the clones
displaying 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 display
has been widely used to identify antibodies or short peptides with specific binding
activities from antibody libraries or random peptide libraries (Pande J. et al,
1985 and Smith G.P., 1985)