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Team:Potsdam Bioware/Project/Part Antibody
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=== Aim of the Antibody Module === | === Aim of the Antibody Module === | ||
The idea of the antibody module is to create antibody constructs which will specifically be mutated and optimized by the AID (activation induces deaminase). Our two antibody constructs allow an easy handling and a straightforwardly integration into CHO cells. The use of Flp-In system realizes time saving incorporation into the CHO genome. A switch from surface presentation to secretion of the antibodies can be enabled by TEV protease and cre recombinase and permits a comfortable harvest of selected antibodies. | The idea of the antibody module is to create antibody constructs which will specifically be mutated and optimized by the AID (activation induces deaminase). Our two antibody constructs allow an easy handling and a straightforwardly integration into CHO cells. The use of Flp-In system realizes time saving incorporation into the CHO genome. A switch from surface presentation to secretion of the antibodies can be enabled by TEV protease and cre recombinase and permits a comfortable harvest of selected antibodies. | ||
| + | === A Short Review on Antibodies === | ||
| + | Antibodies are highly specific targeting reagents and are the key defense system for recognizing pathogens and toxins. Antibodies are Y shaped multi domain proteins with two antigen binding sites displaying the Fab fragment and one effector domain represented by the Fc domain. (Holliger, Hudson; 2005) The Fab fragment is composed of two antigen recognition sites with one variable light (VL) and constant light (VC) chain and one variable heavy (VH) and constant heavy (CH) chain each which allow the specific an affine binding of antigens. By interacting with the complement and the Fc receptor, the Fc domain is able to mediate cytotoxic effector functions. (Holliger, Hudson; 2005) | ||
| + | ==== Single Chain Fragment Variable ==== | ||
| + | A single chain fragment variable is a small unit of immunoglobulin and consists of the variable heavy (VH) and the variable light (VL) domains which are joined together by a flexible peptide linker. (Alitheen and Hamid et al.; 2012) The scFv is a very popular format that shows a high antigen binding capacity and can be easily expressed. | ||
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| + | picture | ||
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| + | ==== Nanobody ==== | ||
| + | A specific form of immunoglobulin is the single domain antibody fragment, so called nanobody by its inventor Ablynx. Nanobodies are derived from camellid antibodies that possess a single N-terminal domain, the VHH domain. The VHH domain is solely sufficient for a strong antigen binding and does not require a domain fusion. ( Harmsen, Haard; 2007) Thus, nanobodies have extremely small dimensions and show an elevated stability which both leads to the ability of recognizing epitopes that are not accessible for conventional antibody formats. ( de Marco; 2011) | ||
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Revision as of 00:11, 26 September 2012
Antibody Module
Contents |
Introduction
Aim of the Antibody Module
The idea of the antibody module is to create antibody constructs which will specifically be mutated and optimized by the AID (activation induces deaminase). Our two antibody constructs allow an easy handling and a straightforwardly integration into CHO cells. The use of Flp-In system realizes time saving incorporation into the CHO genome. A switch from surface presentation to secretion of the antibodies can be enabled by TEV protease and cre recombinase and permits a comfortable harvest of selected antibodies.
A Short Review on Antibodies
Antibodies are highly specific targeting reagents and are the key defense system for recognizing pathogens and toxins. Antibodies are Y shaped multi domain proteins with two antigen binding sites displaying the Fab fragment and one effector domain represented by the Fc domain. (Holliger, Hudson; 2005) The Fab fragment is composed of two antigen recognition sites with one variable light (VL) and constant light (VC) chain and one variable heavy (VH) and constant heavy (CH) chain each which allow the specific an affine binding of antigens. By interacting with the complement and the Fc receptor, the Fc domain is able to mediate cytotoxic effector functions. (Holliger, Hudson; 2005)
Single Chain Fragment Variable
A single chain fragment variable is a small unit of immunoglobulin and consists of the variable heavy (VH) and the variable light (VL) domains which are joined together by a flexible peptide linker. (Alitheen and Hamid et al.; 2012) The scFv is a very popular format that shows a high antigen binding capacity and can be easily expressed.
picture
Nanobody
A specific form of immunoglobulin is the single domain antibody fragment, so called nanobody by its inventor Ablynx. Nanobodies are derived from camellid antibodies that possess a single N-terminal domain, the VHH domain. The VHH domain is solely sufficient for a strong antigen binding and does not require a domain fusion. ( Harmsen, Haard; 2007) Thus, nanobodies have extremely small dimensions and show an elevated stability which both leads to the ability of recognizing epitopes that are not accessible for conventional antibody formats. ( de Marco; 2011)
