Description

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Project description

Background

Antibody, also known as immunoglobulin, is a large, Y-shaped protein that is used by the immune system to neutralize pathogens such as bacteria and viruses in vertebrate. They are secreted mostly by differentiated B cells called plasma cells. The antibody recognizes a unique molecule of the agent, called an antigen, via the Fab's variable region. Monoclonal antibodies (mAb or moAb) are antibodies that are made by identical immune cells that are all clones of a unique parent cell. Since the first generation of monoclonal antibody produced in 1975, it has become a more and more important and essential tool in research, diagnosis and treatment, and will continue to be critical to both academic and industrial researchers in the near future.

Move

Traditional monoclonal antibody production relies upon lymphocyte fusion technology, also known as hybridoma technology. Although it’s the most widely used and an effective method in monoclonal antibody production, it is always laborious and time consuming and not suited for high throughput application. In the recent years, a number of new platforms and advanced technologies have been developed like phage display and recombinant antibodies technologies, however there still be lot of improvement to make especially in cost reduce and high throughput screening and producing.

Details

In this project, we developed an epitope library in E.coli system, which could be used in antigen producing and B cells capture in a high throughput manner. Combining with recombinant expression and MS-screen platforms, we can easily discover and produce recombinant antibody in a high throughput manner. In order to get our goal, we first developed an epitope designing software, which can design appropriate small peptide composed of 12~20 amino acids and two complementary oligos coding for the peptide automatically. Then the each part of complementary oligos (paired oligos) would annealed to form a double chain adapter, which would be sequentially constructed into our specialised plasmid in a high throughput manner to make the first epitope library for antigen producing. And meanwhile these double chain adapters would be constructed in another specialised plasmid to make a second epitope library which was used for surface display on E.coli and for B cell capture. And further, this E.coli strain was genetically engineered to express iron binding protein on its pili and hydrogenases to accumulate Fe irons and restore them into a reduction manner, so the strain changed to be magnetically attractive. So we can use the second E.coli library in which the surface of each E.coli express a unique peptide to capture and enrich the corresponding B cells which secret an antibody recognizing the right epitope. Finally we can get the epitope and its antibody sequences using ordinary PCR and sequencing technologies.

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