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

Chaperones involved in hepatitis B virus morphogenesis.

R Prange1, M Werr, H Löffler-Mary

  • 1Institute for Medical Microbiology and Hygiene, Johannes-Gutenberg-Universität Mainz, Germany.

Biological Chemistry
|May 1, 1999
PubMed
Summary

Researchers identified key host cell factors, heat shock protein Hsc70 and calnexin, crucial for hepatitis B virus (HBV) assembly and morphogenesis. These chaperones are essential for proper viral envelope protein function and HBV virion production.

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

In situ and remote observations of the ultraviolet footprint of the moon Callisto by the Juno spacecraft.

Nature communications·2025
Same author

The low-frequency source of Saturn's kilometric radiation.

Science (New York, N.Y.)·2018
Same author

Structure-activity relationships of acetylcholine derivatives with Lucilia cuprina nicotinic acetylcholine receptor α1 and α2 subunits in chicken β2 subunit hybrid receptors in comparison with chicken nicotinic acetylcholine receptor α4/β2.

Insect molecular biology·2013
Same author

A 30-cm objective grating for far-UV astronomy: theoretical study and laboratory tests.

Applied optics·2010
Same author

Molecular cloning, partial genomic structure and functional characterization of succinic semialdehyde dehydrogenase genes from the parasitic insects Lucilia cuprina and Ctenocephalides felis.

Insect molecular biology·2008
Same author

Titan's atmospheric temperatures, winds, and composition.

Science (New York, N.Y.)·2005

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Hepatitis B virus (HBV) assembly requires envelopment of nucleocapsids by viral envelope proteins (S, M, L) and budding into intracellular compartments.
  • The L protein plays a critical role in HBV assembly, mediating hepatocyte binding and capsid envelopment, and exhibits a unique dual membrane topology.

Purpose of the Study:

  • To identify and characterize host cell factors involved in HBV assembly and morphogenesis.
  • To elucidate the roles of specific chaperone proteins in the HBV life cycle.

Main Methods:

  • Identification and characterization of a preS-specific sequence involved in L protein topology.
  • Investigation of interactions between viral envelope proteins and host cell chaperones (Hsc70, calnexin).

Related Experiment Videos

  • Assays to assess the impact of chaperone inhibition on HBV assembly and secretion.

    • Main Results:

    • A preS-specific sequence was identified that suppresses cotranslational translocation and binds heat shock protein Hsc70, indicating its role in HBV morphogenesis.
    • The M envelope protein requires calnexin for proper folding and trafficking, with calnexin binding to an M-specific N-glycan.
    • Inhibition of the calnexin-M interaction blocked viral envelope secretion, highlighting calnexin's essential role.

    Conclusions:

    • Heat shock protein Hsc70 and calnexin are essential chaperones involved in hepatitis B virus assembly.
    • Hsc70 participates in HBV morphogenesis by interacting with the L protein's cytosolic anchorage sequence.
    • Calnexin is critical for the proper folding, trafficking, and secretion of the M envelope protein, thereby facilitating HBV assembly.