%0 Journal Article %A Surowy, Teresa K %A Leary, Thomas P. %A Carrick, Robert J. %A Knigge, Mark F. %A Pilot-Matias, Tami J. %A Heynen, Cynthia %A Gutierrez, Robin A. %A Desai, Suresh M. %A Dawson, George J. %A Mushahwar, Isa K. %T GB virus C E2 glycoprotein: expression in CHO cells, purification and characterization %D 1997 %J Journal of General Virology, %V 78 %N 8 %P 1851-1859 %@ 1465-2099 %R https://doi.org/10.1099/0022-1317-78-8-1851 %I Microbiology Society, %X A 315 amino acid recombinant segment of the GB virus C (GBV-C) E2 envelope glycoprotein (E2-315) was expressed and secreted from CHO cells. E2-315 was purified by affinity chromatography using a monoclonal antibody directed to a FLAG sequence genetically engineered onto the C terminus of the recombinant protein. The secreted protein had a molecular mass of 48–56 kDa and was shown to be N-glycosylated. Amino acid sequencing confirmed the expected N-terminal sequence. Purified E2-315 was used to develop an ELISA for detection of E2 antibodies in human sera. Antibodies to GBV-C E2 appeared to be directed toward conformational epitopes since human sera reactivity was detected in ELISA using native E2-315, but it was extremely weak or non-existent with denatured E2 protein. The use of an ELISA which can detect human GBV-C E2 antibodies will be important in further understanding of the clinical significance and epidemiology of GBV-C. %U https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-78-8-1851