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Size and Structure of Viral Genomes01:26

Size and Structure of Viral Genomes

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Viral genomes exhibit remarkable diversity in size, structure, and composition, influencing their replication strategies and interactions with host cells. These genomes consist of either DNA or RNA and may be linear or circular. Additionally, they can be single-stranded or double-stranded, with each configuration affecting how the virus propagates within a host. RNA viruses, for instance, generally have smaller genomes than DNA viruses, a factor that contributes to their high mutation rates and...
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Retrovirus Life Cycles01:10

Retrovirus Life Cycles

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Retroviruses have a single-stranded RNA genome that undergoes a special form of replication. Once the retrovirus has entered the host cell, an enzyme called reverse transcriptase synthesizes double-stranded DNA from the retroviral RNA genome. This DNA copy of the genome is then integrated into the host’s genome inside the nucleus via an enzyme called integrase. Consequently, the retroviral genome is transcribed into RNA whenever the host’s genome is transcribed, allowing the...
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Viruses with RNA Genomes01:29

Viruses with RNA Genomes

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RNA viruses are categorized into positive-strand, negative-strand, or double-stranded groups based on their genomic structure and replication mechanisms. This classification dictates how they exploit host cellular machinery for protein synthesis and replication. Some RNA viruses also utilize reverse transcription as part of their life cycle, further diversifying their replication strategies.Positive-Strand RNA VirusesPositive-strand RNA viruses have genomes that function directly as messenger...
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Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Rab Proteins01:14

Rab Proteins

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Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
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Retroviruses02:33

Retroviruses

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Retroviruses and retrotransposons both insert copies of their genetic elements into the genome of the host cell. Thus, the viral genes are passed on when the host genome is replicated or translated. A typical retroviral DNA sequence contains 3-4 genes that encode the different proteins required for its structural assembly and function as a molecular parasite. This DNA is transcribed into a single mRNA, which is very similar in structure to conventional mRNAs, i.e., it is capped at the 5’...
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Related Experiment Video

Updated: Aug 11, 2025

Visualization of HIV-1 Gag Binding to Giant Unilamellar Vesicle GUV Membranes
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Visualization of HIV-1 Gag Binding to Giant Unilamellar Vesicle GUV Membranes

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Early HIV-1 Gag Assembly on Lipid Membrane with vRNA.

Anne X-Z Zhou, John A Hammond, Kai Sheng

    Biorxiv : the Preprint Server for Biology
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    Summary

    Mass photometry revealed HIV-1 Gag assembly initiates with trimerization on membranes, requiring vRNA. Oligomer growth occurs monomer by monomer, supporting a gradual capsid lattice formation model.

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    Detection of Viral RNA by Fluorescence in situ Hybridization FISH
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    Area of Science:

    • Virology
    • Biophysics
    • Structural Biology

    Background:

    • Human Immunodeficiency Virus type 1 (HIV-1) assembly is a complex process crucial for viral replication.
    • Understanding the initial steps of Gag polyprotein assembly is key to developing antiviral strategies.

    Approach:

    • Mass photometry (MP) was employed to study the assembly of myristoylated Gag (myr-Gag) and viral RNA (vRNA) 5' UTR in a supported lipid bilayer (SLB) model.
    • MP allowed for real-time, single-molecule analysis of Gag-Gag and Gag-vRNA interactions.

    Key Points:

    • Gag trimerization on the membrane is a critical early event in HIV-1 assembly, dependent on the presence of vRNA.
    • Oligomerization proceeds through the addition of one or two Gag monomers at a time from solution, requiring vRNA.
    • These findings support a model of capsid lattice formation initiated by trimeric nucleation followed by gradual edge expansion.

    Conclusions:

    • The study provides novel insights into the dynamic, single-molecule mechanisms governing the initiation of HIV-1 capsid assembly.
    • This research highlights the interplay between Gag protein, vRNA, and lipid membranes in initiating viral structure formation.