Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Rabbit endogenous retrovirus-H encodes a functional protease.

Cécile Voisset1, Richard E Myers1, Alex Carne2

  • 1Wohl Virion Centre, Windeyer Institute of Medical Sciences, University College London, 46 Cleveland Street, London W1T 4JF, UK.

The Journal of General Virology
|January 21, 2003
PubMed
Summary

Human retrovirus-5 sequences are actually from a rabbit endogenous retrovirus (RERV-H). Researchers confirmed RERV-H protease functions as a retroviral aspartic protease, crucial for viral replication.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Cellular Functional Analyses of <i>ARX</i> Variants Reveal New Insights Into Genotype-Phenotype Correlations in Neurodevelopmental Disorders Among Male and Female Patients.

Human mutation·2026
Same author

Genome sequence and annotation of ovine herpesvirus 1

The Journal of general virology·2026
Same author

The genetic architecture of HIV-1 virulence.

Virus evolution·2025
Same author

Anti-prion drugs reduce endoplasmic reticulum stress and protect human dopaminergic neurons from death.

Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie·2025
Same author

HIV-phyloTSI: subtype-independent estimation of time since HIV-1 infection for cross-sectional measures of population incidence using deep sequence data.

BMC bioinformatics·2025
Same author

Racial disparity in microvascular function among women with newly diagnosed breast cancer.

American journal of physiology. Heart and circulatory physiology·2025

Area of Science:

  • Molecular Biology
  • Virology
  • Genomics

Background:

  • Human retrovirus-5 (HERV-5) sequences previously identified in human DNA are now classified as belonging to the rabbit endogenous retrovirus H (RERV-H) family.
  • Understanding the enzymatic functions of endogenous retroviruses is critical for deciphering their role in host genomes and potential pathogenic mechanisms.

Purpose of the Study:

  • To characterize the enzymatic activity and properties of the RERV-H protease.
  • To confirm the retroviral and aspartic protease nature of RERV-H protease.

Main Methods:

  • PCR amplification of the RERV-H gag-pro region from human DNA samples.
  • Bacterial expression and purification of RERV-H protease variants.
  • In vitro protease activity assays, including self-cleavage and polyprotein cleavage.

Related Experiment Videos

  • Characterization of autocleavage sites and inhibition studies using pepstatin A and PYVPheStaAMT.
  • Structural modeling of the RERV-H protease.

    • Main Results:

    • RERV-H protease demonstrated autocleavage activity and cleaved the RERV-H Gag polyprotein precursor in vitro.
    • A mutated RERV-H protease with an inactive site confirmed the importance of the active site for function.
    • The protease exhibited sensitivity to pepstatin A and specific inhibition by PYVPheStaAMT, characteristic of aspartic proteases.
    • Structural modeling supported the classification of RERV-H protease as a retroviral aspartic protease.

    Conclusions:

    • The study confirms that human retrovirus-5 sequences originate from RERV-H.
    • RERV-H protease functions as a retroviral aspartic protease, essential for processing viral polyproteins.
    • The characterized enzymatic properties and structural model provide insights into retroviral protease mechanisms.