We have previously described a cell-free system that reconstitutes immature capsid assembly of Gag polypeptides from viruses belonging to three major primate lentiviral lineages, including HIV-1, HIV-2 and SIVagm. Studies described here examine a member of the SIVmac/Mne lineage, SIVMneCL8, using assays for virus production and infectivity as well as cellular events in capsid formation. We report that SIVMneCL8, a molecular clone with properties typical of transmitted viral variants, is less infectious per unit p27 Gag than another member of the SIVmac/Mne lineage, SIVmac239. SIVMneCL8 Gag polypeptides are arrested at an early stage of capsid assembly in the cell-free system. Additionally, SIVMneCL8 Gag polypeptides associate minimally with the host factor human HP68. This is the first report of a primate lentivirus that does not complete capsid assembly in the cell-free system.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1111/j.1600-0684.2004.00074.x | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Dynamic supramolecular snub cubes.
Nature
January 2025
Department of Chemistry, The University of Hong Kong, Hong Kong SAR, China.
Mimicking the superstructures and properties of spherical biological encapsulants such as viral capsids and ferritin offers viable pathways to understand their chiral assemblies and functional roles in living systems. However, stereospecific assembly of artificial polyhedra with mechanical properties and guest-binding attributes akin to biological encapsulants remains a formidable challenge. Here we report the stereospecific assembly of dynamic supramolecular snub cubes from 12 helical macrocycles, which are held together by 144 weak C-H hydrogen bonds.
View Article and Find Full Text PDFMaize Streak Virus: Single and Gemini Capsid Architecture.
Viruses
November 2024
Department of Biochemistry and Molecular Biology, College of Medicine Center for Structural Biology, McKnight Brain Institute, University of Florida, Gainesville, FL 32610-0245, USA.
are ssDNA plant viruses whose control has both economical and agricultural importance. Their capsids assemble into two distinct architectural forms: (i) a T = 1 icosahedral and (ii) a unique twinned quasi-isometric capsid. Described here are the high-resolution structures of both forms of the maize streak virus using cryo-EM.
View Article and Find Full Text PDFVirus-like Particles Produced in Plants: A Promising Platform for Recombinant Vaccine Development.
Plants (Basel)
December 2024
Institute of Bioengineering, Research Center of Biotechnology of the Russian Academy of Sciences, 119071 Moscow, Russia.
The capsid proteins of many viruses are capable of spontaneous self-assembly into virus-like particles (VLPs), which do not contain the viral genome and are therefore not infectious. VLPs are structurally similar to their parent viruses and are therefore effectively recognized by the immune system and can induce strong humoral and cellular immune responses. The structural features of VLPs make them an attractive platform for the development of potential vaccines and diagnostic tools.
View Article and Find Full Text PDFVariable Assembly and Procapsid Binding of Bacteriophage P22 Terminase Subunits in Solution.
Pathogens
December 2024
Laboratory of Macromolecular Structure, Department of Molecular Biology and Biochemistry, University of California Irvine, Steinhaus Hall, Irvine, CA 92697-3900, USA.
Concatemeric viral DNA is packaged into bacteriophage P22 procapsids via a headful packaging mechanism mediated by a molecular machine consisting of small (gp3) and large (gp2) terminase subunits. Although a negative stain reconstruction exists for the terminase holoenzyme, it is not clear how this complex binds the dodecameric portal protein located at a 5-fold mismatch vertex. Herein, we describe new assemblies for the holoenzyme.
View Article and Find Full Text PDFModeling Viral Capsid Assembly: A Review of Computational Strategies and Applications.
Cells
December 2024
Department of Physics, University of Texas at El Paso, El Paso, TX 79968, USA.
Viral capsid assembly is a complex and critical process, essential for understanding viral behavior, evolution, and the development of antiviral treatments, vaccines, and nanotechnology. Significant progress in studying viral capsid assembly has been achieved through various computational approaches, including molecular dynamics (MD) simulations, stochastic dynamics simulations, coarse-grained (CG) models, electrostatic analyses, lattice models, hybrid techniques, machine learning methods, and kinetic models. Each of these techniques offers unique advantages, and by integrating these diverse computational strategies, researchers can more accurately model the dynamic behaviors and structural features of viral capsids, deepening our understanding of the assembly process.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!