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Purification and diagnostic utility of a recombinant hepatitis E virus capsid protein expressed in insect larvae.
- Source :
-
Protein expression and purification [Protein Expr Purif] 2003 Jan; Vol. 27 (1), pp. 27-34. - Publication Year :
- 2003
-
Abstract
- We report here the expression and purification of a truncated form of the hepatitis E virus ORF2 protein (ORF2delta111/deltaTM), from the fat bodies of Spodoptera litura larvae infected with a recombinant baculovirus. The purified protein migrated as a doublet of approximately 56 kDa on SDS-PAGE and was found to be glycosylated by staining with concanavalin A-linked horseradish peroxidase. The protein was used in a sensitive and specific enzyme-linked immunosorbent assay (ELISA) for the detection of antibodies to HEV. The results showed complete concordance with those obtained using a commercial kit for the detection of anti-HEV antibodies. Antigen expression in the insect larvae system presents a rapid and low-cost method that obviates the need for expensive tissue culture scale-ups or special equipment.
- Subjects :
- Animals
Baculoviridae
Capsid Proteins genetics
Enzyme-Linked Immunosorbent Assay
Glycosylation
Hepatitis E immunology
Humans
Larva metabolism
Recombinant Proteins genetics
Spodoptera virology
Viral Proteins genetics
Capsid Proteins isolation & purification
Hepatitis E diagnosis
Hepatitis E virus chemistry
Recombinant Proteins isolation & purification
Viral Proteins isolation & purification
Subjects
Details
- Language :
- English
- ISSN :
- 1046-5928
- Volume :
- 27
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Protein expression and purification
- Publication Type :
- Academic Journal
- Accession number :
- 12509981
- Full Text :
- https://doi.org/10.1016/s1046-5928(02)00574-0