# HIGH RESOLUTION STRUCTURE OF MULTI COMPONENT VIRUSES

> **NIH NIH R01** · PURDUE UNIVERSITY · 1992 · $129,476

## Abstract

Crystallographic and biophysical analyses of isometric viruses will
be performed to study virus stability, protein-nucleic acid
interactions, the interactions of antibodies with viruses, and the
evolution of spherical viruses.  The subjects of our study will be
comoviruses and nepoviruses.  Both these virus groups share many
properties with the animal picornaviruses.

Results from the previous funding period have shown that at least
one of the nucleoprotein components of the comovirus, beanpod
mottle virus (BPMV), has 20% of the RNA genome organized with
icosahedral symmetry.  A total of 11 contiguous ribonucleotides
were modeled in the icosahedral asymmetric unit of 3482
nucleotides.  This structure will be refined at 2.8 angstrom
resolution and structures of the empty capsid and the bottom
component (containing 5889 nucleotides) will be determined and
refined.  A third component, which is biologically identical to the
bottom component but has exchanged endogenous polyamines for cesium
ions, will also be investigated.  Crystals of all the components
are isomorphous and different to 2.6 angstrom resolution.

Collaboration arrangements with an immunologist have been made to
obtain monoclonal antibodies to cowpea mosaic virus (CPMV) and
BPMV.  Attempts will be made to co-crystallize Fab fragments with
the virus particles.  An extraordinary crystal form of CPMV, in
which FAB fragments have been successfully diffused, will also be
studied.

Collaborations with a molecular biologist have been made to study,
by site directed mutagenesis, factors affecting assembly, protein-
nucleic acid interactions and the effect of specific changes in the
coat protein on the host specificity in comoviruses.

The structure of tobacco ringspot virus (TRV) will be studied using
x-ray crystallography.  This nepovirus is similar to comoviruses,
but it contains one capsid proteins of 58kD.  Given its similarity
to comoviruses in size, component types, and genome sizes, it may
have ordered RNA and subunit is probably composed of 3 covalently
linked beta-barrel domains.

## Key facts

- **NIH application ID:** 3128181
- **Project number:** 5R01AI018764-11
- **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:** 1992
- **Award amount:** $129,476
- **Award type:** 5
- **Project period:** 1982-04-01 → 1994-03-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3128181

## Citation

> US National Institutes of Health, RePORTER application 3128181, HIGH RESOLUTION STRUCTURE OF MULTI COMPONENT VIRUSES (5R01AI018764-11). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3128181. Licensed CC0.

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