# HIGH RESOLUTION STRUCTURE OF A MULTI COMPONENT VIRUS

> **NIH NIH R01** · PURDUE UNIVERSITY · 1987 · $85,748

## Abstract

Viruses are obligate parasites causing a wide variety of diseases in
humans, ranging from the common cold to cancer.  There is no antiviral
agent available for widespread therapeutic application.  Typically the
defense against virus disease is the immune system of the host.  The most
promising solution to viral diseases in humans and other higher animals is
the development of vaccines based on synthetic polypeptides from regions of
the antigen that evoke strong response from the immune system.  To develop
a rational strategy for such vaccines the relationship between the antibody
and antigen must be known in detail.  How is a virus neutralized by an
antibody?  Will an antibody produced by any region of the antigen lead to
neutralization?  It is possible for regions of the antigen that do not
normally evoke antibody response to bind an antibody if it is elicited by
the same antigen amino acid sequence in a synthetic polypeptide?  What is
the role of primary and tertiary structure in binding of the antibody to
the antigen.

The objectives of this proposal are designed to answer these questions.
The structure of cowpea mosaic virus (CpMV) will first be solved at 2.8
Angstroms resolution using single crystal X-ray diffraction.  The virus
crystallizes in space group I23 a = 3.17 Angstroms.  The structure will be
refined using the Hendrickson Konnert procedure.  Currently the structure
has been solved at 5.5 Angstroms resolution using a single isomorphous
derivative and real space electron density and phase refinement.  When the
structure has been fully interpreted a reproducible crystal form of CpmV
(P6122 a = 450; c = 1038 Angstroms) containing 300 Angstrom channels
parallel to the crystal axes will be used to study the binding of
monoclonal antibodies to the virus particle.  Approximately thirty to forty
antigenic sites should be exposed in the hexagonel crystals.  Conditions
must be found in which antibodies bind without disturbing the crystal
lattice.  The antibody-virus complex will be solved using the virus
structure determined at 2.8 Angstroms in the cubic cell as the phasing
model.  Data to 3.5 Angstroms have previously been collected from the
native virus in the hexagonal cell.

CpMV displays protein sequence homology with the animal picorna viruses in
the nonstructural proteins (polymerase, VpG, and protease).  Extensive
comparisons will be made between the CpMV structure and the polio and
rhinovirus structures.

## Key facts

- **NIH application ID:** 3128177
- **Project number:** 5R01AI018764-06
- **Recipient organization:** PURDUE UNIVERSITY
- **SAM.gov UEI:** YRXVL4JYCEF5
- **Principal Investigator:** John Emil Johnson
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1987
- **Award amount:** $85,748
- **Award type:** 5
- **Project period:** 1982-04-01 → 1989-03-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3128177

## Citation

> US National Institutes of Health, RePORTER application 3128177, HIGH RESOLUTION STRUCTURE OF A MULTI COMPONENT VIRUS (5R01AI018764-06). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3128177. Licensed CC0.

---

*[NIH grants dataset](/datasets/nih-grants) · CC0 1.0*