Related Experiment Video
Updated: Aug 19, 2026

Visualization of HIV-1 Gag Binding to Giant Unilamellar Vesicle (GUV) Membranes
Published on: July 28, 2016
Unmyristylated Moloney murine leukemia virus Pr65gag is excluded from virus assembly and maturation events
1Laboratory of Molecular Virology and Carcinogenesis, NCI-Frederick Cancer Research Facility, Frederick, Maryland 21701.
Abstract:
The gag precursor polyprotein of Moloney murine leukemia virus (MuLV) is normally modified by myristylation of the N-terminal glycine. Previous work showed that the Pr65gag lacking the myristylation site does not associate with cellular membranes or assemble into virus particles. We now report that it also is not cleaved to the mature gag cleavage products within the cell and that it sediments as a free 65-kilodalton monomer in detergent-free cell extracts containing 0.3 M NaCl. Even when the cells containing the mutant are productively infected with wild-type MuLV, the mutant Pr65gag is not processed into cleavage products and is not incorporated into the virions produced by these cells. Thus, the mutant gag molecules seem unable to participate in the normal processes of self-assembly and maturation. We propose that myristate-mediated membrane association is an essential first step in MuLV assembly. This association may also play a role in budding of MuLV.
Insights
Myristylation of the Moloney murine leukemia virus (MuLV) gag precursor polyprotein is essential for its membrane association, processing, and virus particle assembly. Without this modification, the gag protein fails to mature or incorporate into new virions.
Area of Science:
- Virology
- Molecular Biology
- Cellular Biology
Background:
- The gag precursor polyprotein (Pr65gag) of Moloney murine leukemia virus (MuLV) is typically modified by N-terminal myristylation.
- Previous studies indicated that Pr65gag lacking the myristylation site does not associate with cellular membranes or assemble into virus particles.
Purpose of the Study:
- To investigate the role of myristylation in the processing, assembly, and maturation of MuLV Pr65gag.
- To determine if myristylation is a prerequisite for MuLV assembly and budding.
Main Methods:
- Analysis of a mutant MuLV Pr65gag lacking the N-terminal myristylation site.
- Cellular fractionation and sedimentation assays in detergent-free extracts.
- Infection of cells expressing the mutant Pr65gag with wild-type MuLV.
Main Results:
- The mutant Pr65gag, lacking myristylation, was not cleaved into mature gag products within the cell.
- The mutant Pr65gag sedimented as a free 65-kilodalton monomer.
- Even in cells productively infected with wild-type MuLV, the mutant Pr65gag was not processed or incorporated into newly formed virions.
Conclusions:
- Myristylation of MuLV Pr65gag is crucial for its proper processing and maturation.
- Myristate-mediated membrane association appears to be a critical initial step for MuLV assembly.
- This membrane association may also be involved in the budding process of MuLV.
Related Concept Videos
Leaky Scanning
Intralumenal Vesicles and Multivesicular Bodies
Subviral Agents
Inhibitors of Virion Maturation and Assembly

