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Phage Therapy

Phage Therapy

What comes to mind when you hear the word “bacteria”? Most people, if not all, will answer “disease,” “sickness,” or “bad for the health.” What not all people know is there are actually both good and bad bacteria and some bacterial species are probiotic – bacteria that are helpful to its host. In fact, bacterial infections can be treated with bacteriophages: viruses that have the ability to infect and fight harmful bacteria, culminating in their destruction. Bacteriophage or phage therapy is therefore very useful in various fields like medicine, veterinary science, dentistry, and even agriculture.http://www.newbalanceoutlet.cc

History of Phage Therapy

Bacteriophages were discovered by two people: the English bacteriologist Frederick Twort in 1915 and the French-Canadian microbiologist Felix d’Herelle in 1917. Immediately after their discovery, the thought of using phages to fight bacterial infections was already apparent. D’Herelle began testing the therapeutic effects that phages may have on chickens and cows first and the tests were successful. Eventually, human tests were conducted and the development of phage therapy became more extensive especially with the foundation of the Eliavia Institute in 1923; the pharmaceutical company Eli Lilly began the commercialization of phage therapy in the US during the 1940s. During the Second World War, phages were used to treat bacterial diseases among soldiers of the Soviet Union, particularly gangrene and dysentery. The development of antibiotics in the 1950s led to a temporary setback on phage therapy as the use of antibiotics became more favourable. However, there has been a renewed interest in the development and employment of phage therapy in more applications.

Advantages over Antibiotics

Viruses and bacteria evolve over time and can develop a resistance to antibiotics. In theory, this resistance can also apply to phages, but it may be less difficult to overcome compared to antibiotics.

Because phages are target specific, meaning only a one or very few bacterial strains are targeted upon, it is easier to develop new phages than new antibiotics. A time period of only a few days or weeks is needed to acquire new phages for resistant strains of bacteria, whereas it can take years to obtain new antibiotics. When resisting bacteria evolve, the assigned phages also evolve, so when super bacterium appears, an equivalent super phage fights it as long as the phage is derived from the same environment.

Compared to antibiotics, phages go deeper into the infected area. Antibiotics, on the other hand, have concentration properties that quickly decrease as they go below the surface of the infection. The replication of phages is concentrated on the infected area where they are needed the most, while antibiotics are metabolized and removed from the body. In addition, secondary resistance does not happen among phages, but happens quite often among antibiotics. Secondary resistance is acquired and occurs when there aren’t enough blood drug levels.

Certain infections in people and experimentally infected animals have been proven to be more effectively treated with phage therapy than using antibiotics. Since 1966, the average success rate of studies that used phages in various ways (systematically, topically, intravenously, or orally) is from 80 to 95%, with minimal or no allergic and/or gastrointestinal side effects. The infections studied are from E. coli, Acinetobacter, Psuedomonas, and Staphylococcus aureus. Multiple side effects like allergies, intestinal disorders, and yeast infections have been observed when using antibiotics.

Applications

Fighting and destroying bacterial infections (both in humans and animals) are the primary applications of phage therapy, but it can also be employed for other uses. It can be the key to fighting the NDM-1, a gene that can be included in the DNA of bacteria, enabling them to resist antibiotics. Waste water from sewage systems are not really considered waste because it is a rich source of phage strains for various kinds of bacteria that lead to the most up-to-date medicines. Skin grafting for extensive wounds, trauma, burns, and skin cancer can also be improved by using phage therapy to lessen the Psuedomonas aeruginosa infection. Some experiments for cells in tissue culture have also discovered antitumor agents in phages. Bacteria cause food to spoil faster, and phages have been studied for their potential to increase the freshness of food and decrease the incidents of food spoilage.

Phage therapy has many other potential benefits and giving it ample support can pave the way to a healthier future.
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Phage Display

Phage Display Cycle

One of the laboratory techniques employed in studying different protein interactions is Phage Display. With this in vitro screening method, protein ligands and macromolecules can be easily identified and interactions between protein and protein, peptide and protein, & DNA and protein can be studied further.

History of Phage Display

The first described instance of Phage Display occurred in 1985, when George P. Smith fused a peptide with a gene III from a filamentous phage. He filed a patent detailing the process of generating phage display libraries in the same year. Eventually, further development of Phage Display technology led by different groups from the MRC Laboratory of Molecular Biology, as well as from The Scripps Research Institute, led to the possibility of displaying proteins for the purpose of therapeutic protein engineering. The technique has been continuously improved to screen and amplify huge collections of proteins showing the connection of phenotype and genotype better.

Structure

A filamentous phage has a diameter of around 6.5 nanometers, with a length that depends on the size of its genome. It comes from a huge family of bacterial viruses that also infect other forms of bacteria. It contains a small genome with an intergenic region containing the necessary sequences for the replication and encapsidation of DNA.

A phage particle consists of five coat proteins. The particle has a hollow tube that houses so many copies of the primary coat protein. There are also binding interactions between the adjacent subunits’ hydrophobic midsections. One end of the particle is blunt, and the other is sharp. The blunt end contains plenty of copies of the two tiniest ribosomally translated proteins, while the sharp end contains around only 5 copies of the pIII and pVI genes, which are necessary for the detachment of the phage from the cell membrane.

How it works

Phage Display is a method wherein a library of phage particles that express very diverse peptides is generated. The objective is to choose those that will bind a desired target; the target can be a protein, a peptide, or a piece of DNA.

The most often used vector to build a random peptide display is the filamentous phage M13. In this display, the DNA which encodes the peptide or protein of interest is integrated into the pIII or pVI gene. To make sure that the fragments are completely inserted into the three possible reading frames, multiple cloning sites are sometimes employed, allowing the proper translation of the cDNA in its correct frame. The DNA hybrid and the phage gene are then put inside E. coli bacterial cells. Examples of these bacterial cells include XL1-Blue E. coli, SS320, TG1, and ER2738. The peptide or protein of interest is eventually expressed in either the minor or major coat protein

If another kind of vector is used, for example, a phagemid vector or simplified display construct vector, a helper phage must infect the E. coli cells; otherwise, the phage particles will not be separated from the E. coli cells. A helper phage activates the packaging of the phage DNA and assembles the mature virions with their corresponding protein fragments, which are included in the outer coating of the minor or major protein coat.

The generated phage library is then screened by addition into a microtiter plate containing immobilised target proteins or DNA sequences. Phages displaying a protein that bind to one target will remain, while the other phages can be discarded through washing. The remaining phage particles can be used to multiply the phage by infecting them into bacteria, thus increasing the diversity of the peptide display library.

Applications

The fast isolation of particular ligands through phage display has a wide variety of applications like epitope mapping, analyzing different protein interactions, vaccine development, drug design, and therapeutic target validation. Phage display is also used to pick inhibitors for the active and allosteric sites of G-protein binding modulatory peptides, enzymes, and receptor antagonists and agonists.

Determining the proper protein partners can be useful to identify the functions of various proteins. For drug discovery and design, Phage Display is employed in protein engineering or in vitro protein evolution. Therapeutic targeting with phage display is also primarily used to diagnose and determine tumour antigens, which is useful for cancer research.

Antibody Phage Display significantly improved the discovery and development of antibody drugs. Phage display for antibody libraries paved the way for rapid vaccine design and therapy. These libraries are used to learn more about the human immune system and to create human antibodies in vitro with the use of diverse synthetic substances.

Phage Display can be used in conjunction with other techniques, and with enough support and studies, more applications for it can be discovered.
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