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

61.7K
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.
61.7K
Leaky Scanning02:28

Leaky Scanning

5.1K
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...
5.1K
Protein Complex Assembly02:41

Protein Complex Assembly

10.6K
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...
10.6K
Nucleic Acid Structure01:25

Nucleic Acid Structure

5.9K
The pentose sugar in DNA is deoxyribose, while in RNA the pentose sugar is ribose. The difference between the sugars is the presence of the hydroxyl group on the ribose's second carbon and a hydrogen on the deoxyribose's second carbon. The phosphate residue attaches to the hydroxyl group of the 5′ carbon of one sugar and the hydroxyl group of the 3′ carbon of the sugar of the next nucleotide, which forms  a 5′ to 3′ phosphodiester linkage.
DNA Structure
DNA...
5.9K

You might also read

Related Articles

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

Sort by
Same author

Differences in RNA Binding Between Segmented and Non-Segmented Negative-Strand Virus Nucleocapsids.

Microorganisms·2026
Same author

A Bacillales-specific tubular scaffold essential for NADH dehydrogenase activity.

Nature communications·2026
Same author

Integrase anchors viral RNA to the HIV-1 capsid interior.

Nature·2026
Same author

[Structure of the influenza virus ribonucleoprotein: a model for understanding the viral replication machinery].

Medecine sciences : M/S·2026
Same author

Molecular basis for occlusion of the jeilongvirus receptor-binding site by the elongated C-terminus.

mBio·2025
Same author

Dynamics driving the precursor in NifEN scaffold during nitrogenase FeMo-cofactor assembly.

Nature chemical biology·2025

Related Experiment Video

Updated: Jun 5, 2025

Multi-target Parallel Processing Approach for Gene-to-structure Determination of the Influenza Polymerase PB2 Subunit
22:10

Multi-target Parallel Processing Approach for Gene-to-structure Determination of the Influenza Polymerase PB2 Subunit

Published on: June 28, 2013

13.2K

Influenza a virus antiparallel helical nucleocapsid-like pseudo-atomic structure.

Florian Chenavier1, Eleftherios Zarkadas2, Lily-Lorette Freslon1

  • 1Univ. Grenoble Alpes, CNRS, CEA, IBS, 71 avenue des Martyrs, F-38000 Grenoble, France.

Nucleic Acids Research
|December 14, 2024
PubMed
Summary

Researchers detailed the cryo-EM structure of an influenza A virus ribonucleoprotein (RNP)-like complex. This reveals how nucleoprotein (NP) interacts with RNA, explaining the flexibility of viral RNPs crucial for replication.

More Related Videos

Purification and Visualization of Influenza A Viral Ribonucleoprotein Complexes
09:35

Purification and Visualization of Influenza A Viral Ribonucleoprotein Complexes

Published on: February 9, 2009

13.0K
Preparation of Pseudo-Typed H5 Avian Influenza Viruses with Calcium Phosphate Transfection Method and Measurement of Antibody Neutralizing Activity
07:15

Preparation of Pseudo-Typed H5 Avian Influenza Viruses with Calcium Phosphate Transfection Method and Measurement of Antibody Neutralizing Activity

Published on: November 22, 2021

2.2K

Related Experiment Videos

Last Updated: Jun 5, 2025

Multi-target Parallel Processing Approach for Gene-to-structure Determination of the Influenza Polymerase PB2 Subunit
22:10

Multi-target Parallel Processing Approach for Gene-to-structure Determination of the Influenza Polymerase PB2 Subunit

Published on: June 28, 2013

13.2K
Purification and Visualization of Influenza A Viral Ribonucleoprotein Complexes
09:35

Purification and Visualization of Influenza A Viral Ribonucleoprotein Complexes

Published on: February 9, 2009

13.0K
Preparation of Pseudo-Typed H5 Avian Influenza Viruses with Calcium Phosphate Transfection Method and Measurement of Antibody Neutralizing Activity
07:15

Preparation of Pseudo-Typed H5 Avian Influenza Viruses with Calcium Phosphate Transfection Method and Measurement of Antibody Neutralizing Activity

Published on: November 22, 2021

2.2K

Area of Science:

  • Virology
  • Structural Biology
  • Molecular Biology

Background:

  • Influenza A viruses cause seasonal epidemics and potential pandemics.
  • Viral ribonucleoproteins (vRNPs), composed of nucleoprotein (NP) and RNA, are essential for influenza virus transcription and replication.
  • Understanding vRNP structure is key to controlling influenza.

Purpose of the Study:

  • To determine the high-resolution structure of an antiparallel helical RNP-like complex of influenza A virus.
  • To elucidate the mechanism of RNA packaging and NP-NP interactions within vRNPs.
  • To explain the inherent flexibility of influenza A virus vRNPs.

Main Methods:

  • Assembly of an antiparallel helical RNP-like complex using recombinant N-terminally truncated NP and synthetic RNA.
  • 3.0 Å cryo-electron microscopy (cryo-EM) structure determination.
  • Analysis of RNA pathway and NP-NP interfaces.

Main Results:

  • The cryo-EM structure reveals the complete RNA path through NP and details NP-NP interactions driving helical assembly.
  • The structure accommodates RNA in both major and minor grooves.
  • NP binds a variable number of nucleobases (estimated 20-24), explaining RNA flexibility.

Conclusions:

  • The study provides unprecedented structural detail of influenza A virus vRNPs.
  • Findings clarify the mechanism of genome encapsidation and the flexibility of vRNPs.
  • This knowledge can inform future antiviral strategies targeting influenza virus replication.