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Purification and diagnostic utility of a recombinant hepatitis E virus capsid protein expressed in insect larvae
, P.S. Malik, S. Jameel
Published in
PMID: 12509981
Volume: 27
Issue: 1
Pages: 27 - 34
We report here the expression and purification of a truncated form of the hepatitis E virus ORF2 protein (ORF2Δ111/ΔTM), from the fat bodies of Spodoptera litura larvae infected with a recombinant baculovirus. The purified protein migrated as a doublet of ∼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. © 2002 Elsevier Science (USA). All rights reserved.
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