Presentation of the hydrophilic domains of hepatitis C viral E2 envelope glycoprotein on hepatitis B surface antigen particles

Ihl Hee Lee, Chun Hyung Kim, Wang Shick Ryu

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

Subviral particles of hepatitis B virus have been used to present foreign epitopes. We attempted to present the hydrophilic domains of E2 envelope protein of hepatitis C virus (HCV) as a fusion protein with hepatitis B virus surface antigen (HBsAg). The five hydrophilic domains of HCV E2 antigen were inserted into HBsAS such that the inserted hydrophilic domains were presented on the outer surface of HBV subviral particles. In addition, a fusion encoding the hypervariable region (HVR) of E2 antigen was also made. Cell lysate and culture medium were analyzed for the synthesis and secretion of the fusion proteins by immunoprecipitation with polyclonal anti-HBsAg antibody using recombinant vaccinia virus system. The results showed that the fusion proteins containing these six E2 domains were made in the cell, but only two out of six fusion proteins were secreted into culture medium. Further, cesium chloride density gradient analysis and electron microscopy revealed that these fusions were secreted into culture media as particles. It will be of interest to test immunogenicity of the HBsAg fusion particles containing the HCV E2 domains in animal model.

Original languageEnglish
Pages (from-to)145-151
Number of pages7
JournalJournal of Medical Virology
Volume50
Issue number2
DOIs
Publication statusPublished - 1996 Oct 1

Fingerprint

Hepatitis C
Hepatitis B Surface Antigens
Hepatitis B virus
Glycoproteins
Hepacivirus
Culture Media
Proteins
Vaccinia virus
Protein C
Immunoprecipitation
Epitopes
Electron Microscopy
Animal Models
Cell Culture Techniques
Antibodies
CD99 Antigen

All Science Journal Classification (ASJC) codes

  • Virology
  • Infectious Diseases

Cite this

@article{b88c6b0517014e0bb27894ceeac3313b,
title = "Presentation of the hydrophilic domains of hepatitis C viral E2 envelope glycoprotein on hepatitis B surface antigen particles",
abstract = "Subviral particles of hepatitis B virus have been used to present foreign epitopes. We attempted to present the hydrophilic domains of E2 envelope protein of hepatitis C virus (HCV) as a fusion protein with hepatitis B virus surface antigen (HBsAg). The five hydrophilic domains of HCV E2 antigen were inserted into HBsAS such that the inserted hydrophilic domains were presented on the outer surface of HBV subviral particles. In addition, a fusion encoding the hypervariable region (HVR) of E2 antigen was also made. Cell lysate and culture medium were analyzed for the synthesis and secretion of the fusion proteins by immunoprecipitation with polyclonal anti-HBsAg antibody using recombinant vaccinia virus system. The results showed that the fusion proteins containing these six E2 domains were made in the cell, but only two out of six fusion proteins were secreted into culture medium. Further, cesium chloride density gradient analysis and electron microscopy revealed that these fusions were secreted into culture media as particles. It will be of interest to test immunogenicity of the HBsAg fusion particles containing the HCV E2 domains in animal model.",
author = "Lee, {Ihl Hee} and Kim, {Chun Hyung} and Ryu, {Wang Shick}",
year = "1996",
month = "10",
day = "1",
doi = "10.1002/(SICI)1096-9071(199610)50:2<145::AID-JMV7>3.0.CO;2-A",
language = "English",
volume = "50",
pages = "145--151",
journal = "Journal of Medical Virology",
issn = "0146-6615",
publisher = "Wiley-Liss Inc.",
number = "2",

}

Presentation of the hydrophilic domains of hepatitis C viral E2 envelope glycoprotein on hepatitis B surface antigen particles. / Lee, Ihl Hee; Kim, Chun Hyung; Ryu, Wang Shick.

In: Journal of Medical Virology, Vol. 50, No. 2, 01.10.1996, p. 145-151.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Presentation of the hydrophilic domains of hepatitis C viral E2 envelope glycoprotein on hepatitis B surface antigen particles

AU - Lee, Ihl Hee

AU - Kim, Chun Hyung

AU - Ryu, Wang Shick

PY - 1996/10/1

Y1 - 1996/10/1

N2 - Subviral particles of hepatitis B virus have been used to present foreign epitopes. We attempted to present the hydrophilic domains of E2 envelope protein of hepatitis C virus (HCV) as a fusion protein with hepatitis B virus surface antigen (HBsAg). The five hydrophilic domains of HCV E2 antigen were inserted into HBsAS such that the inserted hydrophilic domains were presented on the outer surface of HBV subviral particles. In addition, a fusion encoding the hypervariable region (HVR) of E2 antigen was also made. Cell lysate and culture medium were analyzed for the synthesis and secretion of the fusion proteins by immunoprecipitation with polyclonal anti-HBsAg antibody using recombinant vaccinia virus system. The results showed that the fusion proteins containing these six E2 domains were made in the cell, but only two out of six fusion proteins were secreted into culture medium. Further, cesium chloride density gradient analysis and electron microscopy revealed that these fusions were secreted into culture media as particles. It will be of interest to test immunogenicity of the HBsAg fusion particles containing the HCV E2 domains in animal model.

AB - Subviral particles of hepatitis B virus have been used to present foreign epitopes. We attempted to present the hydrophilic domains of E2 envelope protein of hepatitis C virus (HCV) as a fusion protein with hepatitis B virus surface antigen (HBsAg). The five hydrophilic domains of HCV E2 antigen were inserted into HBsAS such that the inserted hydrophilic domains were presented on the outer surface of HBV subviral particles. In addition, a fusion encoding the hypervariable region (HVR) of E2 antigen was also made. Cell lysate and culture medium were analyzed for the synthesis and secretion of the fusion proteins by immunoprecipitation with polyclonal anti-HBsAg antibody using recombinant vaccinia virus system. The results showed that the fusion proteins containing these six E2 domains were made in the cell, but only two out of six fusion proteins were secreted into culture medium. Further, cesium chloride density gradient analysis and electron microscopy revealed that these fusions were secreted into culture media as particles. It will be of interest to test immunogenicity of the HBsAg fusion particles containing the HCV E2 domains in animal model.

UR - http://www.scopus.com/inward/record.url?scp=0030003344&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030003344&partnerID=8YFLogxK

U2 - 10.1002/(SICI)1096-9071(199610)50:2<145::AID-JMV7>3.0.CO;2-A

DO - 10.1002/(SICI)1096-9071(199610)50:2<145::AID-JMV7>3.0.CO;2-A

M3 - Article

C2 - 8915880

AN - SCOPUS:0030003344

VL - 50

SP - 145

EP - 151

JO - Journal of Medical Virology

JF - Journal of Medical Virology

SN - 0146-6615

IS - 2

ER -