GENE EXPRESSION OF HUMAN RESPIRATORY SYNCYTIAL VIRUS
Project Number1R29AI037938-01
Former Number1R29AI034960-01A1
Contact PI/Project LeaderBARIK, SAILEN
Awardee OrganizationUNIVERSITY OF SOUTH ALABAMA
Description
Abstract Text
The long-term goal of this project is to understand the molecular basis of
growth and pathogenicity of human respiratory syncytial virus (RSV), the
single most important agent of respiratory diseases in the young children
throughout the world and a probable agent of sudden infant death syndrome
(SIDS). A recurring cause of pneumonia-like disease characterized by
rhinitis, pharyngitis, and croup, it accounts for significant morbidity in
the first year of human life. It is now clear that a better understanding
of the regulation of viral growth at the molecular level is an essential
prerequisite to a successful control of this human pathogen, particularly
in view of the failure of immune therapy.
Although considerable information is available regarding the nucleotide
sequence of the viral genome and its constituent genes, our knowledge
about the molecular mechanism of expression of the genes remains poor.
Recently, we have taken an important step in this direction by
establishing an in vitro of transcription system of RSV which efficiently
synthesizes all viral mRNAs. The fidelity of the system is underscored by
our finding that the mRNAs are capped, methylated and polyadenylated. More
importantly, we have demonstrated an essential requirement of cellular
protein(s) in viral transcription. Recently, we have dissected the RSV
transcription apparatus even further: we have purified viral L protein,
phosphoprotein, and the N-RNA template from one another and reconstituted
functional transcription using these purified macromolecules.
The reconstituted system is now amenable to studies of structure and
function of its components. We have recently expressed RSV P protein in E.
coli in a phosphate-free form and shown that it can be phosphorylated by
cell kinase in vitro. Inhibition of the cell kinase also inhibited RSV
transcription suggesting an essential role for P protein phosphorylation
in its function. The immediate major goal is to use the reconstituted
system to understand the role of P protein phosphorylation in detail, and
to characterize the identity of the cellular protein (s) and determine its
exact role in RSV transcription. These studies should provide important
insights into the functioning of the viral transcription machinery which
is an essential component in RSV growth and pathogenesis.
National Institute of Allergy and Infectious Diseases
CFDA Code
DUNS Number
172750234
UEI
QB12VPNQQFE8
Project Start Date
01-August-1994
Project End Date
31-July-1999
Budget Start Date
01-August-1994
Budget End Date
31-July-1995
Project Funding Information for 1994
Total Funding
$94,344
Direct Costs
$64,619
Indirect Costs
$29,725
Year
Funding IC
FY Total Cost by IC
1994
National Institute of Allergy and Infectious Diseases
$94,344
Year
Funding IC
FY Total Cost by IC
Sub Projects
No Sub Projects information available for 1R29AI037938-01
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