| Title |
Expression and characterisation of rubella virus capsid protein in yeast cells / |
| Translation of Title |
Raudonukės viruso kapsidės baltymo sintezė mielėse ir jo charakterizavimas. |
| Authors |
Petraitytė, Rasa ; Sasnauskas, Kęstutis |
| Full Text |
|
| Is Part of |
Biologija. 2006, Nr. 3, p. 4-7.. ISSN 1392-0146 |
| Keywords [eng] |
Rubella virus ; Recombinant capsid protein ; Yeast ; Indirect IgG ELISA |
| Abstract [eng] |
In the present study, we expressed rubella virus (RV) capsid protein (C) in yeast S. cerevisiae cells. Two different methods for purification of recombinant C protein were employed: CsCl gradient ultracentrifugation and nickel chelation chromatography. The yield of recombinant C protein was approximately 3.2 mg of purified protein from 1g of wet yeast biomass. The antigenic characteristics of recombinant C protein purified in different ways were further evaluated by indirect IgG ELISA with RV-positive and RV-negative human serum specimens. Recombinant C protein purified using CsCl gradient ultracentrifugation possessed a higher antigenicity as compared to that purified by nickel chelate chromatography. The results indicate that the recombinant C protein has a potential for use in detection of human IgG antibodies against RV. The yeast-expressed rubella C protein is a promising antigen for the development of diagnostic tools in serology. |
| Type |
Journal article |
| Language |
English |
| Publication date |
2006 |
