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J Virol, April 1998, p. 2738-2744, Vol. 72, No. 4
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Characterization of Hepatitis G Virus (GB-C Virus) Particles: Evidence for a Nucleocapsid and Expression of Sequences Upstream of the E1 Protein

Jinhua Xiang,1,2 Donna Klinzman,1 James McLinden,3 Warren N. Schmidt,1,2 Douglas R. LaBrecque,1,2 Robert Gish,4 and Jack T. Stapleton1,2,*

Departments of Internal Medicine, Iowa City Veterans Administration Medical Center,1 and The University of Iowa College of Medicine,2 Iowa City, Iowa 52242; American Biogenetic Sciences, Boston, Massachusetts 021183; and Department of Transplantation, California Pacific Medical Center, San Francisco, California 941154

Received 27 August 1997/Accepted 24 December 1997

Hepatitis G virus (HGV or GB-C virus) is a newly described virus that is closely related to hepatitis C virus (HCV). Based on sequence analysis and by evaluation of translational initiation codon preferences utilized during in vitro translation, HGV appears to have a truncated or absent core protein at the amino terminus of the HGV polyprotein. Consequently, the biophysical properties of HGV may be very different from those of HCV. To characterize HGV particle types, we evaluated plasma from chronically infected individuals with and without concomitant HCV infection by using sucrose gradient centrifugation, isopycnic banding in cesium chloride, and saline density flotation centrifugation. Similar to HCV, HGV particles included an extremely-low-density virion particle (1.07 to 1.09 g/ml) and a nucleocapsid of ~1.18 g/ml. One major difference between the particle types was that HGV was consistently more stable in cesium chloride than HCV. Plasma samples from chronically HGV-infected individuals and controls were assessed by a synthetic peptide-based immunoassay to determine if they contained HGV antibody specific for a conserved region in the coding region upstream of the E1 protein. Chronically HGV-infected individuals contained antibody to the HGV core protein peptide, whereas no binding to a hepatitis A virus peptide control was observed. Competitive inhibition of binding to the HGV peptide confirmed the specificity of the assay. These data indicate that HGV has a nucleocapsid and that at least part of the putative core region of HGV is expressed in vivo.

* Corresponding author. Mailing address: Department of Internal Medicine, SW 54, GH, The University of Iowa, Iowa City, IA 52242. Phone: (319) 356-3168. Fax: (319) 356-4600. E-mail: Jack-Stapleton{at}uiowa.edu.




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