# STRUCTURE OF HEPATITIS B ANTIGENS

> **NIH NIH R01** · VIRGINIA COMMONWEALTH UNIVERSITY · 1988 · $103,196

## Abstract

The objective is to obtain detailed information concerning the structure of
hepatitis B viral proteins, and to determine the relationship between their
protein structure and their antigenic function.  These studies will include
research on the HBsAg, including the pre-S gene products, HBeAg, HBcAg and
the "X" protein.  Studies of the HBsAg will include studies of the intact
particle and its protein and lipid components.  We will utilize our panel
of monoclonal anti-HBs antibodies (which contain anti-group specific and
anti-subtypes specific antibodies) in conjunction with amino acid sequence
analysis, chemical modification studies, synthetic peptides, immunoblotting
techniques, olignucleotide directed site, specific mutagenesis, and
eukaryotic expression vectors for the production of HBsAg from the cloned
viral gene to attempt to determine the physical structure of HBsAg and the
location and structure of the various antigenic determinants.  We will also
use physical techniques such as freeze ETCH and freeze fracture electron
microscopy low angle x-ray scattering, fourier transform infrared
spectorphotometry, and circular dichroism to gain information on the
number, arrangement, and secondary structure of the protein subunits with
HBsAg and how the lipid components are related to the maintenance of this
structure.  The role of the pre-S proteins in the particle structure and
antigenic activity will also be investigated.

The chemistry of the conversion of HBcAg to HBeAg will be studied and this
chemical conversion correlated with the antigenic alteration.  The location
of the relevant antigenic sites will be sought by the same methods as used
for HBsAg.  We will also use anti-synthetic peptide antibodies in an
attempt to characterize the product of the viral "X" gene.  Mammalian
expression vectors will be used in an effort to synthesize the protein for
further characterization.

The antibody produced in humans in response to HBV infection or to
immunization by the current vaccine (Heptavax) as well as that produced in
response to the experimental yeast HBsAg vaccines will be examined by
competition studies with our monoclonal antibodies to determine the
relative amounts and specificities of these human antibodies.  It is
expected that this will help define the major immunogenic determination
recognized by humans.

## Key facts

- **NIH application ID:** 3126510
- **Project number:** 5R01AI015955-09
- **Recipient organization:** VIRGINIA COMMONWEALTH UNIVERSITY
- **SAM.gov UEI:** MLQFL4JSSAA9
- **Principal Investigator:** Darrell L Peterson
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1988
- **Award amount:** $103,196
- **Award type:** 5
- **Project period:** 1979-08-01 → 1990-07-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3126510

## Citation

> US National Institutes of Health, RePORTER application 3126510, STRUCTURE OF HEPATITIS B ANTIGENS (5R01AI015955-09). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3126510. Licensed CC0.

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