# HERPESVIRUS PROTEIN SYNTHESIS AND VIRION ASSEMBLY

> **NIH NIH R01** · JOHNS HOPKINS UNIVERSITY · 1993 · $283,448

## Abstract

The long term objective of this research is to understand the
molecular basis of cytomegalovirus (CMV) replication and use that
information to develop new ways to diagnose and treat CMV-related
diseases of man.  This will be accomplished by identifying and studying
the synthesis, structure, and function of specific viral proteins that
are essential for virus replication.
     In this application for renewed support, two general sets of studies
are proposed.  One represents a continuation of ongoing work to learn
more about proteins that are already under investigation.  The other will
pursue leads generated during the last grant period to better define two
new sets of proteins.  A major emphasis is placed on learning more about
a "scaffoldinglike" protein, referred to as the assembly protein and
suspected to have a key role in capsid formation and possibly
DNA-packaging.  Experiments are outlined to identify, characterize, and
genetically map the protease responsible for cleaving the precursor form
of this protein.  Chemical mutagenesis of the cloned assembly protein
gene will be used in an attempt to generate temperature-sensitive mutants
that will aid functional studies.
     Four proteins of the virion tegument will also be investigated.  Two
of these, referred to as the basic phosphoprotein and the lower matrix
protein, appear to interact directly with proteins of the capsid and
envelope.  The nature of these associations will be explored by chemical,
immunological, and genetic approaches.  Two other tegument proteins,
referred to as the high molecular weight protein and the 115K protein,
cosediment as a possible heterodimer and are speculated to be related to
the herpes simplex DNA cleavage/packaging complex.  Experiments based on
chemical dissociation, rate-velocity sedimentation, band-shift assays,
and DNA-affinity chromatography are described to characterize the complex
and determine whether it has properties of a cleavage/packaging enzyme.
Studies of a more exploratory nature will try to identify the proteins
encoded by three newly discovered HCMV genes that are homologous to
cellular G protein-coupled receptors, and determine by recombinant DNA
methods whether they are required for growth of the virus in cell
culture.

## Key facts

- **NIH application ID:** 3125541
- **Project number:** 5R01AI013718-17
- **Recipient organization:** JOHNS HOPKINS UNIVERSITY
- **SAM.gov UEI:** FTMTDMBR29C7
- **Principal Investigator:** D Wade Gibson
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1993
- **Award amount:** $283,448
- **Award type:** 5
- **Project period:** 1977-09-01 → 1996-07-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3125541

## Citation

> US National Institutes of Health, RePORTER application 3125541, HERPESVIRUS PROTEIN SYNTHESIS AND VIRION ASSEMBLY (5R01AI013718-17). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3125541. Licensed CC0.

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