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 Concept Videos

You might also read

Related Articles

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

Sort by
Same author

ESCRT-III assembles around mis-segregated DNA to protect genome stability.

Nature structural & molecular biology·2026
Same author

Capsid and integrase play essential apposing roles in viral ribonucleoprotein assembly during HIV-1 core morphogenesis.

iScience·2026
Same author

Cognitive Decline, Neurologic Involvement, and Neonatal Crisis in <i>ABCC9</i>-Related Intellectual Disability and Myopathy Syndrome.

Neurology. Genetics·2026
Same author

The host protein cyclophilin A restricts nuclear entry of HIV-1 mutants by reducing the elasticity of the viral capsid.

PLoS pathogens·2026
Same author

A Hybrid Gag Lattice as a Structural Intermediate in HIV-1 Maturation.

bioRxiv : the preprint server for biology·2026
Same author

DIALing in elevated expression setpoints with promoter shortening.

Cell systems·2025

Related Experiment Video

Updated: Apr 22, 2026

Co-immunoprecipitation of the Mouse Mx1 Protein with the Influenza A Virus Nucleoprotein
09:39

Co-immunoprecipitation of the Mouse Mx1 Protein with the Influenza A Virus Nucleoprotein

Published on: April 21, 2015

17.4K

Structural insight into HIV-1 restriction by MxB.

Jennifer L Fribourgh1, Henry C Nguyen1, Kenneth A Matreyek2

  • 1Yale University, Molecular Biophysics and Biochemistry, New Haven, CT 06520, USA.

Cell Host & Microbe
|October 15, 2014
PubMed
Summary

Myxovirus resistance protein B (MxB) restricts HIV-1 by directly binding the viral capsid. Dimerization of MxB is crucial for this antiviral mechanism, distinct from MxA.

More Related Videos

Analysis of SAMHD1 Restriction by Flow Cytometry in Human Myeloid U937 Cells
09:43

Analysis of SAMHD1 Restriction by Flow Cytometry in Human Myeloid U937 Cells

Published on: June 13, 2021

2.7K
A Restriction Enzyme Based Cloning Method to Assess the In vitro Replication Capacity of HIV-1 Subtype C Gag-MJ4 Chimeric Viruses
14:23

A Restriction Enzyme Based Cloning Method to Assess the In vitro Replication Capacity of HIV-1 Subtype C Gag-MJ4 Chimeric Viruses

Published on: August 31, 2014

15.2K

Related Experiment Videos

Last Updated: Apr 22, 2026

Co-immunoprecipitation of the Mouse Mx1 Protein with the Influenza A Virus Nucleoprotein
09:39

Co-immunoprecipitation of the Mouse Mx1 Protein with the Influenza A Virus Nucleoprotein

Published on: April 21, 2015

17.4K
Analysis of SAMHD1 Restriction by Flow Cytometry in Human Myeloid U937 Cells
09:43

Analysis of SAMHD1 Restriction by Flow Cytometry in Human Myeloid U937 Cells

Published on: June 13, 2021

2.7K
A Restriction Enzyme Based Cloning Method to Assess the In vitro Replication Capacity of HIV-1 Subtype C Gag-MJ4 Chimeric Viruses
14:23

A Restriction Enzyme Based Cloning Method to Assess the In vitro Replication Capacity of HIV-1 Subtype C Gag-MJ4 Chimeric Viruses

Published on: August 31, 2014

15.2K

Area of Science:

  • Virology
  • Structural Biology
  • Immunology

Background:

  • Myxovirus resistance (Mx) proteins are interferon-induced GTPases that inhibit viral infections.
  • MxB, unlike MxA, restricts HIV-1 through a mechanism involving the nucleus and viral capsid.

Purpose of the Study:

  • To elucidate the structural basis and molecular mechanism of MxB-mediated HIV-1 restriction.
  • To identify the key determinants of MxB involved in inhibiting HIV-1.

Main Methods:

  • X-ray crystallography to determine the MxB structure.
  • Biochemical assays to assess MxB dimerization and HIV-1 capsid binding.
  • Functional assays to evaluate MxB's restriction of HIV-1.

Main Results:

  • The crystal structure reveals MxB forms an extended antiparallel dimer, critical for its function.
  • MxB directly binds the assembled HIV-1 capsid lattice.
  • Structural differences between MxB and MxA suggest distinct antiviral mechanisms.

Conclusions:

  • MxB dimerization and N-terminal interactions with the HIV-1 capsid are essential for restriction.
  • MxB employs a distinct mechanism of antiviral action compared to MxA.
  • These findings provide a structural framework for understanding MxB's HIV-1 inhibition.