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

Viral Structure00:56

Viral Structure

65.7K
Viruses are extraordinarily diverse in shape and size, but they all have several structural features in common. All viruses have a core that contains a DNA- or RNA-based genome. The core is surrounded by a protective coat of proteins called the capsid. The capsid is composed of subunits called capsomeres. The capsid and genome-containing core are together known as the nucleocapsid.
65.7K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

6.0K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
6.0K
Receptor-mediated Endocytosis01:39

Receptor-mediated Endocytosis

106.8K
Overview
106.8K
Leaky Scanning02:28

Leaky Scanning

5.3K
During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
5.3K
Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

7.4K
Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
7.4K
Protein Complex Assembly02:41

Protein Complex Assembly

12.4K
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.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
12.4K

You might also read

Related Articles

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

Sort by
Same author

Nanobodies against Plasmodium adhesins that block receptor engagement and malaria parasite invasion.

The Biochemical journal·2026
Same author

Antibody binding geometry and affinity control inhibitory hFcγRIIB receptor signaling.

Immunity·2026
Same author

The transmembrane domain structure of TNFR1 suppresses ligand-independent autoactivation but is not required for TNF-induced signaling.

Science signaling·2026
Same author

Complete biosynthesis of psychedelic tryptamines from three kingdoms in plants.

Science advances·2026
Same author

Spatial Relations between Coccoliths and Their Confining Membrane During Crystal Morphogenesis.

Journal of the American Chemical Society·2026
Same author

De novo enzyme design: Controlling structure to design function.

Current opinion in structural biology·2026

Related Experiment Video

Updated: Oct 3, 2025

Author Spotlight: Advancing Antiviral Strategies Through Novel Immunocapture and Mass Spectrometry Techniques
08:07

Author Spotlight: Advancing Antiviral Strategies Through Novel Immunocapture and Mass Spectrometry Techniques

Published on: January 12, 2024

865

Structure and receptor recognition by the Lassa virus spike complex.

Michael Katz1, Jonathan Weinstein2, Maayan Eilon-Ashkenazy1

  • 1Department of Chemical and Structural Biology, Weizmann Institute of Science, Rehovot, Israel.

Nature
|February 17, 2022
PubMed
Summary

Lassa virus spike structure reveals how it enters cells. The signal peptide and matriglycan binding mechanism are clarified, aiding therapeutic design.

More Related Videos

Production of Pseudotyped Particles to Study Highly Pathogenic Coronaviruses in a Biosafety Level 2 Setting
08:40

Production of Pseudotyped Particles to Study Highly Pathogenic Coronaviruses in a Biosafety Level 2 Setting

Published on: March 1, 2019

59.2K
Engineering Antiviral Agents via Surface Plasmon Resonance
13:00

Engineering Antiviral Agents via Surface Plasmon Resonance

Published on: June 14, 2022

2.5K

Related Experiment Videos

Last Updated: Oct 3, 2025

Author Spotlight: Advancing Antiviral Strategies Through Novel Immunocapture and Mass Spectrometry Techniques
08:07

Author Spotlight: Advancing Antiviral Strategies Through Novel Immunocapture and Mass Spectrometry Techniques

Published on: January 12, 2024

865
Production of Pseudotyped Particles to Study Highly Pathogenic Coronaviruses in a Biosafety Level 2 Setting
08:40

Production of Pseudotyped Particles to Study Highly Pathogenic Coronaviruses in a Biosafety Level 2 Setting

Published on: March 1, 2019

59.2K
Engineering Antiviral Agents via Surface Plasmon Resonance
13:00

Engineering Antiviral Agents via Surface Plasmon Resonance

Published on: June 14, 2022

2.5K

Area of Science:

  • Virology
  • Structural Biology
  • Glycobiology

Background:

  • Lassa virus (LASV) is a significant human pathogen causing severe illness.
  • LASV entry relies on a surface spike complex interacting with the cellular receptor matriglycan, found on α-dystroglycan.
  • The precise mechanism of LASV glycan recognition and the role of its unique signal peptide remain unclear.

Purpose of the Study:

  • To elucidate the molecular mechanism of Lassa virus entry.
  • To determine the structure and function of the native LASV spike complex, including its signal peptide.
  • To understand how LASV recognizes and binds to its cellular receptor, matriglycan.

Main Methods:

  • Cryo-electron microscopy (Cryo-EM) to solve the structure of the native LASV spike complex.
  • Biochemical and biophysical analyses to investigate the spike complex's conformation and interactions.

Main Results:

  • The complete native LASV spike complex structure was determined.
  • The signal peptide was found to cross the membrane once, with its amino terminus extracellular.
  • A double-sided domain-switching mechanism involving the signal peptide stabilizes the spike, which is preloaded with matriglycan.

Conclusions:

  • The determined structure reveals the molecular basis of LASV binding to matriglycan via α-dystroglycan.
  • Understanding the signal peptide's role and receptor engagement mechanism provides insights into viral egress.
  • This knowledge can guide the rational design of novel therapeutics targeting the LASV spike-matriglycan interaction.