# ASSEMBLY OF ENVELOPED VIRUSES

> **NIH NIH R01** · WAKE FOREST UNIVERSITY · 1993 · $186,818

## Abstract

Many enveloped viruses contain an internal matrix (M) protein as part of
the viral envelope.  The M protein plays a central role in virus assembly
by binding the nucleoprotein core (nucleocapsid to the cytoplasmic
surface of the plasma membrane during the budding process.  The objective
of the proposed experiments is to determine the mechanisms by which the M
protein of vesicular stomatitis virus (VSV) binds the viral nucleocapsid
and envelope glycoprotein (G protein) in virus assembly.  The approach is
to use novel biochemical and biophysical assays for viral protein
interactions in vitro correlated with results of genetic manipulation of
viral protein function in vivo.  The first Specific Aim is to determine
the factors that induce M protein binding to nucleocapsids.  In vitro
assays for M protein binding to nucleocapsids will be used to
characterize the effects of mutations in the M protein on virus assembly
in vivo.  The questions to be addressed include the nature of the steps
involved in initiation of assembly and the role of different M protein
subpopulations in inducing condensation of the nucleocapsid into the
tightly coiled, bullet-shaped structure found in virions.  The second
Specific Aim is to determine the role of M protein phosphorylation in
virus assembly.  This will be accomplished by characterizing the function
of M proteins containing mutations that abolish the ability of M protein
to be phosphorylated.  The third Specific Aim is to determine the
mechanism of binding of the M protein to the G protein.  A recently
developed binding assay for the interaction of M protein with G .protein
in vitro will be used to determine the structural features of these
proteins. involved in binding.  The binding of M protein to other viral
envelope glycoproteins will be studied to determine the mechanisms
involved in phenotypic mixing of viral envelope proteins.  The
experiments are designed to address questions about virus assembly that
have existed for many years.  These include the nature of the signals
that initiate virus assembly at the plasma membrane, the mechanism by
which the M protein provides the virions with its distinctive morphology,
the basis of phenotypic mixing of viral envelope glycoproteins, and the
mechanism of the often hypothesized but elusive interaction between viral
envelope and matrix proteins.

## Key facts

- **NIH application ID:** 3126470
- **Project number:** 2R01AI015892-13A2
- **Recipient organization:** WAKE FOREST UNIVERSITY
- **SAM.gov UEI:** MBU6HCLNZ431
- **Principal Investigator:** DOUGLAS S. LYLES
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1993
- **Award amount:** $186,818
- **Award type:** 2
- **Project period:** 1979-05-01 → 1998-01-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3126470

## Citation

> US National Institutes of Health, RePORTER application 3126470, ASSEMBLY OF ENVELOPED VIRUSES (2R01AI015892-13A2). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3126470. Licensed CC0.

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