earticle

영어

Transgenic livestock animals such as goat and sleep have been generated for the production of recombinant protein in the milk. Chicken has also attracted great attention as an alternative animal for establishing so called transgenic bioreactor, since they have relatively short breeding time for sexual maturation. We previously reported production of erythropoietin (1) and a single chain immunoglobulin (2) in egg white of genetically manipulated chicken using a retroviral
vector. However, we found that terminal sialic acid and galactose were barely detected in N-linked glucan of these protein deposited in egg white, which may considerably reduce the biological activity of these biopharmaceuticals. In order to overcome this drawback in chicken
transgenic technology, we firstly analyzed galactosyltransferase in the chicken organs, and found that the expression of a major galactosyltransferase (GalT1) was low in magunum portion of the oviduct where majority of egg-white proteins are produced. Therefore, GalT1 gene was introduced to a transgenic chicken producing the single-chain immunoglobulin, and the expression of GalT1 in the golgi fraction of magnum cells was observed. It was also confirmed that the antibody deposited to the egg white of the GalT1-introduced chicken was heavily galactosylated. These results indicate that N-linked glucan of recombinant proteins produced by chicken can be modified by gene manipulation.