# MECHANISMS IN POLYOMA VIRUS ASSEMBLY

> **NIH NIH R01** · DANA-FARBER CANCER INST · 1989 · $182,254

## Abstract

Polyoma virus assembly occurs by sequential addition of capsid
proteins to the viral minichromosome to form a complete T=7d
icosahedral virion.  The overall objective of this proposal is a
structure-function analysis of the polyma capsid proteins with
respect to three aspects of virion assembly:  1) the formation of
capsomeres and capsids, 2) their interaction with the viral
minichromosome, and 3) their transport to the site of virus
assembly in the nucleus.  The major capsid protein VP1, purified
after high level espression in E. coli, will be studied by electron
microscopy and physical chemical methods, and recombinant VP1
capsomeres will be crystallized for X-ray diffraction  analysis.
Protein domains of VP1 responsible for capsomere and capsid
assembly will be investigated using temperature-sensitive viruses
carrying mutations in VP1, and by altering the VP1 gene in vitro
using recombinant DNA techniques.  The ability of the
recombinant VP1 protein to assemble spontaneously into capsids
will be used to encapsidate viral DNA and minichromosomes in
vitro.  The protein domain of VP1 which facilitates its nuclear
transport will be studied using VP1-beta-galactosidase fusion
protein expression in yeast (S. cerevisiae) and by microinjection of
recombinant VP1 capsomeres into Xenopus oocytes.  The
expression in E. coli of the genes for the minor capsid proteins
VP2/VP3 will enable a similar structure-function analysis of these
proteins.  As a preliminary step towards the long range goal of
studying virus-receptor interactions, antibodies against the
putative mouse cell receptor protein for polyoma will be used to
clone the polyoma receptor gene.  We anticipate that our studies
will have significance for normal cell functions such as the
assembly of macromolecules and the subcellular localization of
proteins.  In addition, a more complete understanding of virus
assembly will be relevant to elucidating molecular mechanisms of
viral pathogenesis, and to designing and understanding anti-viral
chemotherapy.

## Key facts

- **NIH application ID:** 3175464
- **Project number:** 5R01CA037667-06
- **Recipient organization:** DANA-FARBER CANCER INST
- **SAM.gov UEI:** DPMGH9MG1X67
- **Principal Investigator:** Robert L Garcea
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1989
- **Award amount:** $182,254
- **Award type:** 5
- **Project period:** 1984-07-01 → 1992-05-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3175464

## Citation

> US National Institutes of Health, RePORTER application 3175464, MECHANISMS IN POLYOMA VIRUS ASSEMBLY (5R01CA037667-06). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3175464. Licensed CC0.

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