# TRANSFORMING GENE AND PROTEIN OF FUJINAMA SARCOMA VIRUS

> **NIH NIH R01** · UNIVERSITY OF CALIFORNIA, SAN DIEGO · 1987 · $106,999

## Abstract

We are interested in studying the mechanism of viral transformation by
retroviruses, an avian Fujinami sarcoma virus (FSV), as the model system.
Our long term goals are to understand how the transforming gene of FSV,
v-fps, evolves and how its product, the transforming protein, p140,
transforms cells and induces tumors.  In order to achieve this goal, we
propose to elucidate the structure and function relationship of the FSV
transforming protein, p140, and to explore how it interacts with other
cellular proteins.  This approach is based on our previous studies in which
we have defined the genetic structure of FSV, characterized the
transforming protein, p140, and analyzed the structure of proto-fps
(cellular homologue of v-fps).  We plan to take advantage of gene-splicing
techniques and site-directed mutagenesis to systematically construct
different mutants of p140 in vitro and to correlate structure and
function.  The putative domain and function relationship will be explored
by constructing various deletion mutants and by assessing the alterations
in the expression of transformation parameter and in host cell response as
a consequence of modification of p140.  We shall further characterize the
ts lesion in the pFL-5 FSV mutant, which is temperature sensitive for
transformation.  We have to establish changes in which amino acid
residue(s) affect the phosphorylation of p140 and alter its transforming
activity.  We will be able to assign the site(s) of phosphorylation and to
define the possible function(s) of each phosphorylation site(s) of p140.
Having assigned the phosphylation site(s) precisely, we plan to use the
site directed mutagenesis to construct mutants with altered specific
phosphorylation site(s) and to examine the functional consequence of such
alterations.  The combination of the studies of deletion mutants, ts
mutants and phosphorylation mutants, should clarify how the oncogene v-fps
product, p140, transforms cells.  Finally, we shall attempt to express p140
or its fragments in E. coli for purification of the p140 protein and its
further characterization.  We also plan to make antisera against synthetic
peptides deduced from p140 amino acid sequence and to use such antisera in
immunoaffinity chromatography to purify the p140 for further studies.
These antisera will be also useful in examining the expression of deletion
mutants described above.  The results from these studies should shed lights
on the biochemical properties of p140.

## Key facts

- **NIH application ID:** 3178629
- **Project number:** 5R01CA039537-03
- **Recipient organization:** UNIVERSITY OF CALIFORNIA, SAN DIEGO
- **SAM.gov UEI:** UYTTZT6G9DT1
- **Principal Investigator:** Wen-Hwa Lee
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1987
- **Award amount:** $106,999
- **Award type:** 5
- **Project period:** 1985-09-01 → 1988-08-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3178629

## Citation

> US National Institutes of Health, RePORTER application 3178629, TRANSFORMING GENE AND PROTEIN OF FUJINAMA SARCOMA VIRUS (5R01CA039537-03). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3178629. Licensed CC0.

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